step type query desc file sequence AAP1 curated CharProtDB::CH_091601,SwissProt::Q42400,TCDB::Q42400,metacyc::AT1G58360-MONOMER amino acid transporter;; Amino acid permease 1; Amino acid transporter AAP1; Neutral amino acid transporter II;; General amino acid permease 1, AAP1 (transports most neutral and acidic amino acids but not aspartate or the basic amino acids);; amino acid permease 1 MKSFNTEGHNHSTAESGDAYTVSDPTKNVDEDGREKRTGTWLTASAHIITAVIGSGVLSLAWAIAQLGWIAGTSILLIFSFITYFTSTMLADCYRAPDPVTGKRNYTYMDVVRSYLGGRKVQLCGVAQYGNLIGVTVGYTITASISLVAVGKSNCFHDKGHTADCTISNYPYMAVFGIIQVILSQIPNFHKLSFLSIMAAVMSFTYATIGIGLAIATVAGGKVGKTSMTGTAVGVDVTAAQKIWRSFQAVGDIAFAYAYATVLIEIQDTLRSSPAENKAMKRASLVGVSTTTFFYILCGCIGYAAFGNNAPGDFLTDFGFFEPFWLIDFANACIAVHLIGAYQVFAQPIFQFVEKKCNRNYPDNKFITSEYSVNVPFLGKFNISLFRLVWRTAYVVITTVVAMIFPFFNAILGLIGAASFWPLTVYFPVEMHIAQTKIKKYSARWIALKTMCYVCLIVSLLAAAGSIAGLISSVKTYKPFRTMHE Bap2 curated CharProtDB::CH_091448,TCDB::P38084 Leu/Val/Ile amino-acid permease;; Leu/Val/Ile amino acid permease MLSSEDFGSSGKKETSPDSISIRSFSAGNNFQSSSSEKTYSKQKSGSDKLIHRFADSFKRAEGSTTRTKQINENTSDLEDGVESITSDSKLKKSMKSRHVVMMSLGTGIGTGLLVANAKGLHYGGPAALIIGYILVSFETYFMIQAAGEMAVTYPTLPANFNAYSSIFISKSFGFATVWLYCFQWLTVLPLELITASMTIQFGNDKINPDIYILIFYVFLVFIHFFGVKAYGETEFIFNCCKILMIAGFIILSIVINCGGAGNDGYIGATYWHNPGAFAGDTSIGRFKNVCYILVTAYFSFGGMELFALSVQEQSNPRKSTPVAAKRSIYRIVVIYLLTMILIGFNVPYNDDQLMGAGGSATHASPYVLAASIHGVKIVPHIINAVILISVVSVANSSLYAGPRLICSLAQQGYAPKFLDYVDREGRPLRALIVCCVFGVIAFVAASSKEEIVFTWLAAIAGLSELFTWTSIMLSHLRFRQAMKVQGRSLDELGYKATTGIWGSIYGVFFNILVFVAQFWVALAPLGNGGKCDAESFFQNYLAFPIWLAFYFGYMVYNRDFTLLNPLDKIDLDFHRRIYDPELMRQEDEENKEKLRNMSLMRKAYHFWC Bap2 curated TCDB::Q2VQZ4 Arbuscular mycorrhizal fungal proline:H+ symporter, AAP1 (binds and probably transports nonpolar, hydrophobic amino acids) MASTPPTDYGKEAVLDVSETRDVETGEVKNGGLKQDLKNRHMQMIAIGGAIGAGLFVGSGGALQKGGPAALLIGYLIIGIMLLCTCLALAEMAVLYPVNGAFFTYIVRFVDPSWGFAMGWQYALAWLTVLPFELIAASITIRFWREDINMAVWVSVFLVVLMGIQIFGVRGYGEVEFVLSIIKICACVGFIILGIVINCGGVGDQGYIGVKYWRDPGAFTSFKGFCAVFVVAAFSFGGTEMVGLAAAESANPRKSIPMASKQVFWRIAIFYILNLFIVGLILPANDPRLMGASGANTKASPFVLAIQDAGIKVLPSIMNAVITVAVLSVANSCTFGSTRTIQAMAERNMAPNFFKYIDSKGRPLYCVILQIAFGLLAYIGAAPQGMEIFGWLLALTGLGFLFVWGSICLAHIRMRAGMKAQGINLGLIPYKTPFGVAGSYLGLGLNILALIASFYTALFPASGASPTAEAFFSSYLAFFSVTLLYLGYKACTRKRQMYVRPAEMDLASGAVWLEEVEPKEPFVWADTPKKVLRSFY aacS hmm TIGR01217 acetoacetate-CoA ligase (EC 6.2.1.16) TIGR01217.hmm aacS curated BRENDA::D6EQU8 acetoacetate-CoA ligase (EC 6.2.1.16) MSTENPQPLWQPDAQRIAQARITRFQAWAAEHHGAPAEGGYAALHRWSVDELDTFWKAVTEWFDVRFSTPYARVLGDRTMPGAQWFPGATLNYAEHALRAAGTRPDEPALLYVDETHEPAPVTWAELRRQVASLAAELRALGVRPGDRVSGYLPNIPQAVVALLATAAVGGVWTSCAPDFGARSVLDRFQQVEPVVLFTVDGYRYGGKEHDRRDTVAELRRELPTLRAVIHIPLLGTEAPDGTLDWETLTAADAEPVYEQVPFDHPLWVLYSSGTTGLPKAIVQSQGGILVEHLKQLGLHCDLGPGDRFFWYTSTGWMMWNFLVSGLLTGTTIVLYDGSPGFPATDAQWRIAERTGATLFGTSAAYVMACRKAGVHPARDLDLSAIQCVATTGSPLPPDGFRWLHDEFAAGGADLWIASVSGGTDVCSCFAGAVPTLPVHIGELQAPGLGTDLQSWDPSGDPLTDEVGELVVTNPMPSMPIRFWNDPDGSRYHDSYFDTYPGVWRHGDWITLTSRGSVVIHGRSDSTLNRQGVRMGSADIYEAVERLPEIRESLVIGIEQPDGGYWMPLFVHLAPGATLDDALLDRIKRTIRVNLSPRHVPDEVIEVPGIPHTLTGKRIEVPVKRLLQGTPLDKAVNPGSIDNLDLLHFYEELARKRS aacS curated BRENDA::Q86V21,SwissProt::Q86V21 acetoacetate-CoA ligase (EC 6.2.1.16);; Acetoacetyl-CoA synthetase; Acyl-CoA synthetase family member 1; Protein sur-5 homolog; EC 6.2.1.16 MSKEERPGREEILECQVMWEPDSKKNTQMDRFRAAVGAACGLALESYDDLYHWSVESYSDFWAEFWKFSGIVFSRVYDEVVDTSKGIADVPEWFKGSRLNYAENLLRHKENDRVALYIAREGKEEIVKVTFEELRQEVALFAAAMRKMGVKKGDRVVGYLPNSEHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQPKLIFSVEAVVYNGKEHNHMEKLQQVVKGLPDLKKVVVIPYVSSRENIDLSKIPNSVFLDDFLATGTSEQAPQLEFEQLPFSHPLFIMFSSGTTGAPKCMVHSAGGTLIQHLKEHLLHGNMTSSDILLCYTTVGWMMWNWMVSLLATGAAMVLYDGSPLVPTPNVLWDLVDRIGITVLVTGAKWLSVLEEKAMKPVETHSLQMLHTILSTGSPLKAQSYEYVYRCIKSSILLGSISGGTDIISCFMGHNFSLPVYKGEIQARNLGMAVEAWNEEGKAVWGESGELVCTKPIPCQPTHFWNDENGNKYRKAYFSKFPGIWAHGDYCRINPKTGGIVMLGRSDGTLNPNGVRFGSSEIYNIVESFEEVEDSLCVPQYNKYREERVILFLKMASGHAFQPDLVKRIRDAIRMGLSARHVPSLILETKGIPYTLNGKKVEVAVKQIIAGKAVEQGGAFSNPETLDLYRDIPELQGF aacS curated BRENDA::Q9D2R0 acetoacetate-CoA ligase (EC 6.2.1.16) MSKLARLEREEIMECQVMWEPDSKKDTQMDRFRAAVGTACGLALGNYNDLYHWSVRSYMDFWAEFWKFSGIVYSRMYDEVVDTSKGIADVPEWFRGSRLNYAENLLRHKENDRVALYVAREGREEIVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQPKLIFSVEAVVYNGKEHGHLEKLQRVVKGLPDLQRVVLIPYVLPREKIDISKIPNSVFLDDFLASGTGAQAPQLEFEQLPFSHPLFIMFSSGTTGAPKCMVHSAGGTLIQHLKEHMLHGNMTSSDILLYYTTVGWMMWNWMVSALATGASLVLYDGSPLVPTPNVLWDLVDRIGITILGTGAKWLSVLEEKDMKPVETHNLHTLHTILSTGSPLKAQSYEYVYRCIKSSVLLGSISGGTDIISCFMGQNSSIPVYKGEIQARNLGMAVEAWDEEGKAVWGASGELVCTKPIPCQPTHFWNDENGSKYRKAYFSKFPGVWAHGDYCRINPKTGGIIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDEVEDSLCVPQYNRDGEERVVLFLKMASGHTFQPDLVKRIRDAIRLGLSARHVPSLILETRGIPYTLNGKKVEVAVKQVMAGRTVEHRGAFSNPETLDLYRDIPELQDF aacS curated BRENDA::Q9JMI1,SwissProt::Q9JMI1 acetoacetyl-CoA synthase (EC 2.3.1.194);; Acetoacetyl-CoA synthetase; EC 6.2.1.16 MSKLARLEREEIMECQVMWEPDSKKDTQMDRFRAAVGTACGLALGNYDDLYHWSVRSYSDFWAEFWKFSGIVCSRMYDEVVDTSKGIADVPEWFRGSRLNYAENLLRHKENDRVALYVAREGREEIAKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQPKLIFSVEAVVYNGKEHGHLEKLQRVVKGLPDLQRVVLIPYVLPREKIDISKIPNSMFLDDFLASGTGAQAPQLEFEQLPFSHPLFIMFSSGTTGAPKCMVHSAGGTLIQHLKEHVLHGNMTSSDILLYYTTVGWMMWNWMVSALATGASLVLYDGSPLVPTPNVLWDLVDRIGITILGTGAKWLSVLEEKDMKPMETHNLHTLHTILSTGSPLKAQSYEYVYRCIKSTVLLGSISGGTDIISCFMGQNSSIPVYKGEIQARNLGMAVEAWDEEGKTVWGASGELVCTKPIPCQPTHFWNDENGSKYRKAYFSKYPGVWAHGDYCRINPKTGGIVMLGRSDGTLNPNGVRFGSSEIYNIVEAFDEVEDSLCVPQYNRDGEERVVLFLKMASGHTFQPDLVKHIRDAIRLGLSARHVPSLILETQGIPYTINGKKVEVAVKQVIAGKTVEHRGAFSNPESLDLYRDIPELQDF aacS curated BRENDA::Q9Z3R3,SwissProt::Q9Z3R3,reanno::Smeli:SMc00774 acetoacetate-CoA ligase (EC 6.2.1.16);; Acetoacetyl-coenzyme A synthetase; Acetoacetyl-CoA synthetase; EC 6.2.1.16;; Acetoacetate--CoA ligase (EC 6.2.1.16) MQAERPLWVPDREIVERSPMAEFIDWCGERFGRSFADYDAFHDWSVSERGAFWTAVWEHCKVIGESGEKALVDGDRMLDARFFPEARLNFAENLLRKTGSGDALIFRGEDKVSYRLTWDELRALVSRLQQALRAQGIGAGDRVAAMMPNMPETIALMLATASVGAIWSSCSPDFGEQGVLDRFGQIAPKLFIVCDGYWYNGKRQDVDSKVRAVAKSLGAPTVIVPYAGDSAALAPTVEGGVTLADFIAGFQAGPLVFERLPFGHPLYILFSSGTTGVPKCIVHSAGGTLLQHLKEHRFHCGLRDGERLFYFTTCGWMMWNWLASGLAVGATLCLYDGSPFCPDGNVLFDYAAAERFAVFGTSAKYIDAVRKGGFTPARTHDLSSLRLMTSTGSPLSPEGFSFVYEGIKPDVQLASISGGTDIVSCFVLGNPLKPVWRGEIQGPGLGLAVDVWNDEGKPVRGEKGELVCTRAFPSMPVMFWNDPDGAKYRAAYFDRFDNVWCHGDFAEWTPHGGIVIHGRSDATLNPGGVRIGTAEIYNQVEQMDEVAEALCIGQDWEDDVRVVLFVRLARGVELTEALTREIKNRIRSGASPRHVPAKIIAVADIPRTKSGKIVELAVRDVVHGRPVKNKEALANPEALDLFAGLEELKS aacS curated SwissProt::Q21166 Acetoacetyl-CoA synthetase; Suppressor of activated let-60 Ras protein 5; EC 6.2.1.16 MTAVSANGKTTEKHENGAHTNGTTNGTTNGSMNGNEISHVQKLQPVYYKPPQNLETFELSLRNHFEEKTNKKFADYREFHRFTCDNYGIFWEDLLKLSDVKLHQNYNQVIDHNLKINERPRWFNGATLNYTENVIERGTATDIAVLNASIEETVTEYTYDNLRKDVYRIATSLRNYGIGPGDTVCGFVPNTYDTLVAVFATAAVGAAWCSASVDFGPAGVLDRFRQVHPKVLFTVNHVTYKKKLIDQTDKINEIVKELPTLEKIVVSDTFTSVKFDATKYNQSDKFSSLEEFKTPIADVVLPFVYTPVPFSDPLFVMFSSGTTGIPKAMVHTVGGTLLKHIEEHLVQGDSKKHDRMFFYTTCGWMMYNWMISFLYSKGSVVLFDECPLAPDTHIIMKIAAKTQSTMIGMGAKLYDEYLRLQIPFNTLYDLSKIHTVYSTGSPLKKECFAYINTYIAPGALIASISGGTDIIGCFVGGIKSLSITPGECQCLFLGMDIKSFNYMDEEIINSDEQGELVCVTPFPSMPSHFLNDTDGKKYRDAYFARLEPFWAHGDFVRVNHSTGGVEMLGRSDATLNRGGVRIGTAEIYSVVEKIPHIADCIVAGRLVEEGMDEEVLLFVKMVPGQELTHSIQAAIVSKLRNDMSPRHVPNKIYAVDDIPYTSSGKKVEVAVKQIVSGKAVQKASSIRNPESLDHFVQYRL aacS curated reanno::acidovorax_3H11:Ac3H11_3009 Acetoacetate--CoA ligase (EC 6.2.1.16) VTSSAAATNSAPLVDSHARGATDVPLIEQTIGAFFADMVARQPEREALVSVHQGRRYTYAQLQTEAHRLASALLGMGLTPGDRVGIWSHNNAEWVLMQLATAQVGLVLVNINPAYRTAEVEYALNKVGCKLLVSMARFKTSDYLGMLRELAPEWQGQQPGHLQAAKLPQLKTVVWIDDEAGQGADEPGLLRFTELIARGNAADPRLAQVAAGLQATDPINIQFTSGTTGFPKGATLTHRNILNNGFFIGECMKLTPADRLCIPVPLYHCFGMVLGNLACFTHGATIVYPNDGFDPLTVLQTVQDERCTGLHGVPTMFIAELDHPRFAEFNLSTLRTGIMAGSPCPTEVMKRVVEQMNLREITIAYGMTETSPVSCQSSTDTPLSKRVSTVGQVQPHLEVKIVDPDTGAVVPIGQRGEFCTKGYSVMHGYWGDEAKTREAIDEGGWMHTGDLATMDAEGYVNIVGRIKDMVIRGGENIYPREIEEFLYRHPQVQDVQVVGVPDQKYGEELCAWIIAKPGTQPTEDDIRAFCKGQIAHYKVPRYIRFVTSFPMTVTGKIQKFKIRDEMKDQLGLEEQKTA aacS curated2 Q9Z3R3 Acetoacetyl-coenzyme A synthetase; Acetoacetyl-CoA synthetase; EC 6.2.1.16 MQAERPLWVPDREIVERSPMAEFIDWCGERFGRSFADYDAFHDWSVSERGAFWTAVWEHCKVIGESGEKALVDGDRMLDARFFPEARLNFAENLLRKTGSGDALIFRGEDKVSYRLTWDELRALVSRLQQALRAQGIGAGDRVAAMMPNMPETIALMLATASVGAIWSSCSPDFGEQGVLDRFGQIAPKLFIVCDGYWYNGKRQDVDSKVRAVAKSLGAPTVIVPYAGDSAALAPTVEGGVTLADFIAGFQAGPLVFERLPFGHPLYILFSSGTTGVPKCIVHSAGGTLLQHLKEHRFHCGLRDGERLFYFTTCGWMMWNWLASGLAVGATLCLYDGSPFCPDGNVLFDYAAAERFAVFGTSAKYIDAVRKGGFTPARTHDLSSLRLMTSTGSPLSPEGFSFVYEGIKPDVQLASISGGTDIVSCFVLGNPLKPVWRGEIQGPGLGLAVDVWNDEGKPVRGEKGELVCTRAFPSMPVMFWNDPDGAKYRAAYFDRFDNVWCHGDFAEWTPHGGIVIHGRSDATLNPGGVRIGTAEIYNQVEQMDEVAEALCIGQDWEDDVRVVLFVRLARGVELTEALTREIKNRIRSGASPRHVPAKIIAVADIPRTKSGKIVELAVRDVVHGRPVKNKEALANPEALDLFAGLEELKS aapJ curated TCDB::Q52812 AapJ, component of General L-amino acid porter; transports basic and acidic amino acids preferentially, but also transports aliphatic amino acids (catalyzes both uptake and efflux) MKNKLLSAAIGAAVLAVGASAASATTLSDVKAKGFVQCGVNTGLTGFAAPDASGNWAGFDVDFCKAVASAVFGDPTKVKYTPTNAKERFTALQSGEIDVLSRNTTWTINRDTALGFNFRPVTYYDGQGFMVRKGLNVKSALELSGAAICVQSGTTTELNLADYFKTNNLQYNPVVFENLPEVNAAYDAGRCDVYTTDQSGLYSLRLTLKNPDEHIILPEIISKEPLGPAVRQGDDQWFDIVSWTAYALINAEEFGITQANVDEMKNSPNPDIKRFLGSETDTKIGTDLGLTNDWAANVIKGVGNYGEIFERNIGQGSPLKIARGLNALWNKGGIQYAPPVR aapJ ignore reanno::Smeli:SMc02118 ABC transporter for L-Glutamine, L-Histidine, and other L-amino acids, periplasmic substrate-binding component MARRILTALVGAAVVGIGTHAASAATLDDVKAKGFVQCGVNTGLAGFAAPDASGNWSGFDVDYCKAIAAAIFGDGSKVKYTPLSAKERFPALQSGEVDVLARNTTWSINRDTALGFNFRPVNYYDGQGFMVRKELDVKSALELSGAAVCVQTGTTTELNLADYFKANNLQYNPVVFEKLEEVNAAYDAGRCDVYTTDQSGLYSLRLTLSKPDDHIVLPEIISKEPLAPAVRQGDDQWFDIVSWVHYALVQAEEFGVTQANLEEMKKSTNPDVQRFLGVEADSKIGTDLGLTNEWAVNIVKAVGNYGEVFDRNIGAGSPLKIERGLNALWNKGGLQYAPPVR aapM curated TCDB::Q52814 AapM, component of General L-amino acid porter; transports basic and acidic amino acids preferentially, but also transports aliphatic amino acids (catalyzes both uptake and efflux) MSVADKPFVRTSILAAEPPPPGERGAVAWIRRNLLATPKDVILTILALALIAWAVPHLVNWLFIQAVWSGPDRTFCATTLQGGIQPDGWSGACWAFISAKYDQFIFGRYPLGERWRPAIVGILFILLLVPMLIPSAPRKGLNAILLFAVLPVIAFWLLHGGFGLEVVETPLWGGLMVTLVLSFVGIAVSLPVGILLALGRRSRMPVIRMLCVTFIEVIRGVPLITVLFMASVMLPLFLPTGWNVDKLLRALIGVSIFTSAYMAEVIRGGLQAIPKGQFEGADSLGLGYWQKTRLIIMPQAIKLVIPSIVNTFIGTFKDTSLVTIIGMFDLLGIVKLNFSDANWASAVTPITGLIFAGFIFWLFCFGMSRYSGFMERHLDTGHKR aapM ignore reanno::Smeli:SMc02120 ABC transporter for L-Glutamine, L-Histidine, and other L-amino acids, permease component 2 MSTNQASFVRASMIEASPAPSLESGAVSWLRKNLFATPKDTALTIISLLILAWLVPPAIQWLFIDAAWSGGGRGVCATLSQGGSQPEGWSGACWAFVNAKFAQFLFGRYPLDERWRPALVGILFVLLLVPMLIPRIPYKGLNALLLLVALPILSAILLPGGWFGLTYVETPLWGGLMVTLVLSFVGIAVSLPLGILLALGRRSNMPVIKMLCTVFIEVIRGVPLITVLFMASVMLPLFLPQGVTFDKFLRALIGVSLFASAYMAEVVRGGLQAIPKGQYEGADSLGLSFWQKMGFIVLPQALKLVIPGIVNTFIGLFKDTSLVSIIGMFDLLGIVRLNFSDTNWATAVTPLTGLIFAGFVFWLFCFGMSRYSGFMERLLDRSQR aapP curated TCDB::Q52815 AapP, component of General L-amino acid porter; transports basic and acidic amino acids preferentially, but also transports aliphatic amino acids (catalyzes both uptake and efflux) MAEAPAKKLTVSATEVAVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKIDEVRREVGMVFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNEPAAFFDNPQHERTKLFLSQILH aapP ignore reanno::Smeli:SMc02121 ABC transporter for L-Glutamine, L-Histidine, and other L-amino acids, ATPase component MANTATAPKLAVSTTDVAIEITNMNKWYGDFHVLRDINLRVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKIDEVRREVGMVFQHFNLFPHLTILENCTLAPIWVRKMPKKEAEQVAMHFLERVKIPEQALKYPGQLSGGQQQRVAIARSLCMRPKILLFDEPTSALDPEMVKEVLDTMVGLAEEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERTKLFLSQILH aapQ curated TCDB::Q52813 AapQ, component of General L-amino acid porter; transports basic and acidic amino acids preferentially, but also transports aliphatic amino acids (catalyzes both uptake and efflux) MTHEAVDTTPLHGTGWSFRSAMYDPKYRSIFYQILTIVILVGFVWWVAHNTAVNLARSNTASGFGFLRGRAGFEIGQSLITFSSDSTYARALLVGILNTLLVAVTGIFTATIIGFLIGIGRLSRNWLIAKLCTVYVEVFRNIPPLLVIFFWYLGVLSVLPQPRESVGLPFSMYLNNRGLAFPKPIFDTGMIAVGIALVIAIVASIIIARWAHKRQAATGQPFHTVWTAIALIVGLPLLVFVVSGFPLTFDVPVAGKFNLTGGSVVGPEFMSLFLALSFYTASFIAEIVRGGIRGVPKGQSEAAGALGLHPSSVTRLVVVPQALRIIIPPLTSQYLNLTKNSSLAIAIGFSDLVAVGGTILNQSGQAIEIVCIWGIVYLSLSILTSLFMNWFNAKMALVER aapQ ignore reanno::Smeli:SMc02119 ABC transporter for L-Glutamine, L-Histidine, and other L-amino acids, permease component 1 MAIGVTNAPERSRSSGSIINDPQVRGIFYQAITIIILAALIYWIVDNTVDNLRRANIASGYDFVRSRAGFDVGQSLISFTSDSTYGRALLVGFINTLLVAITGIITATIIGFIVGIGRLSHNWIIAKLSLAYVEVFRNIPPLLVIFFWYSGVLSILPQARDALALPFDIFLSNRGVAFPRPIAEEGAEYTLLAFVIAVAASVFFARYARKRQLATGERLPVLWTVLGLIIGLPLVTFLVTGAPITFDIPVAGKFNLTGGSVVGPEFMSLFLALSFYTAAFIAEIVRAGIRGVSKGQTEAAHALGIRPALTTRLVVVPQAMRIIIPPLTSQYLNLTKNSSLAVAIGYADLVAVGGTILNQTGQSIEIVSIWLIVYLSLSLATSLFMNWYNARMALVER atoA curated SwissProt::P56006,metacyc::HP0691-MONOMER Succinyl-CoA:3-ketoacid coenzyme A transferase subunit A; Succinyl-CoA:3-oxoacid CoA-transferase; OXCT A; EC 2.8.3.5;; succinyl-CoA:acetoacetate CoA-transferase subunit A (EC 2.8.3.5) MNKVITDLDKALSALKDGDTILVGGFGLCGIPEYAIDYIYKKGIKDLIVVSNNCGVDDFGLGILLEKKQIKKIIASYVGENKIFESQMLNGEIEVVLTPQGTLAENLHAGGAGIPAYYTPTGVGTLIAQGKESREFNGKEYILERAITGDYGLIKAYKSDTLGNLVFRKTARNFNPLCAMAAKICVAEVEEIVPAGELDPDEIHLPGIYVQHIYKGEKFEKRIEKITTRSTK atoA curated ecocyc::ATOD-MONOMER,metacyc::ATOD-MONOMER acetyl-CoA:acetoacetyl-CoA transferase subunit α;; acetyl-CoA:acetoacetyl-CoA transferase subunit α MKTKLMTLQDATGFFRDGMTIMVGGFMGIGTPSRLVEALLESGVRDLTLIANDTAFVDTGIGPLIVNGRVRKVIASHIGTNPETGRRMISGEMDVVLVPQGTLIEQIRCGGAGLGGFLTPTGVGTVVEEGKQTLTLDGKTWLLERPLRADLALIRAHRCDTLGNLTYQLSARNFNPLIALAADITLVEPDELVETGELQPDHIVTPGAVIDHIIVSQESK atoA curated reanno::psRCH2:GFF1045 acetyl-CoA:acetoacetate CoA transferase, A subunit (EC 2.8.3.8) MNKIYPSAAHALEGLVEDGMTIAVGGFGLCGIPEQLIAALRDSGKKDLTAISNNAGVDGFGLGLLLETRQISKMVSSYVGENKEFERQYLAGELALEFTPQGTLAEKLRAGGAGIPAFYTKTGYGTLVAEGKETRQFNGEWYVMEESLTADLALVKAWKADKAGNLLFRKTARNFNPLAAMAGEVCVVEVEEIVETGELDPDQIHLPGIYVHRIVHNPNPEKRIEKRTVRS atoA curated reanno::pseudo6_N2E2:Pf6N2E2_2111 Dehydrocarnitine CoA-transferase and acetoacetate CoA-transferase, subunit A MAGFDKRVSSYEEALEGLKDGMTVIAGGFGLCGIPENLIAEIKRKGIRDLTVVSNNCGVDGFGLGVLLEDRQIRKVVASYVGENALFEQQLLSGEIEVVLTPQGTLAEKMRAGGAGIPAFFTATGVGTPVAEGKEVREFHGRQYLMEESITGDFAIVKGWKADHFGNVIYRHTAQNFNPLAATAGKITVVEVEEIVEPGELDPTQIHTPGIYVDRVICGTFEKRIEQRTVRK atoA ignore BRENDA::B2GV06,SwissProt::B2GV06 3-oxoacid CoA-transferase (EC 2.8.3.5);; Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial; 3-oxoacid CoA-transferase 1; Somatic-type succinyl-CoA:3-oxoacid CoA-transferase; SCOT-s; EC 2.8.3.5 MAALKLLSSGLRLCASARNSRGALHKGCACYFSVSTRHHTKFYTDPVEAVKDIPNGATLLVGGFGLCGIPENLIGALLKTGVKDLTAVSNNAGVDNFGLGLLLRSKQIKRMISSYVGENAEFERQFLSGELEVELTPQGTLAERIRAGGAGVPAFYTSTGYGTLVQEGGSPIKYNKDGSVAIASKPREVREFRGQHFILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAGTTVVEVEEIVDIGSFAPEDIHIPKIYVHRLIKGEKYEKRIERLSLRKEGEGKAKSGKPGEDVRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNMTVHLQSENGVLGLGPYPLKDEADADLINAGKETVTVLPGASFFSSDESFAMIRGGHVNLTMLGAMQVSKYGDLANWMIPGKMVKGMGGAMDLVSSSKTKVVVTMEHSAKGNAHKIMEKCTLPLTGKQCVNRIITEKGVFDVDKKNGLTLIELWEGLTVDDIRKSTGCDFAVSPNLMPMQQIST atoA ignore BRENDA::P55809,SwissProt::P55809,metacyc::HS01447-MONOMER 3-oxoacid CoA-transferase (EC 2.8.3.5);; Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial; 3-oxoacid CoA-transferase 1; Somatic-type succinyl-CoA:3-oxoacid CoA-transferase; SCOT-s; EC 2.8.3.5;; succinyl-CoA:3-ketoacid-coenzyme A transferase 1, mitochondrial (EC 2.8.3.5) MAALKLLSSGLRLCASARGSGATWYKGCVCSFSTSAHRHTKFYTDPVEAVKDIPDGATVLVGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGVDNFGLGLLLRSKQIKRMVSSYVGENAEFERQYLSGELEVELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGGSPIKYNKDGSVAIASKPREVREFNGQHFILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAETTVVEVEEIVDIGAFAPEDIHIPQIYVHRLIKGEKYEKRIERLSIRKEGDGEAKSAKPGDDVRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNITVHLQSENGVLGLGPYPRQHEADADLINAGKETVTILPGASFFSSDESFAMIRGGHVDLTMLGAMQVSKYGDLANWMIPGKMVKGMGGAMDLVSSAKTKVVVTMEHSAKGNAHKIMEKCTLPLTGKQCVNRIITEKAVFDVDKKKGLTLIELWEGLTVDDVQKSTGCDFAVSPKLMPMQQIAN atoA ignore BRENDA::Q63TL3 3-oxoacid CoA-transferase (EC 2.8.3.5) MNKVYPSAAAALEGVVHDGQTFAVGGFGLCGIPEALIAALRDSAVKGITCISNNAGVDGFGLGLLLETRQIKKMISSYVGENKEFERQYLSGELELEFTPQGTLAEKLRAGGAGIPAFFTQTGYGTVIAEGKETREFDGKHYVLEPSLTADVALVKAWKADKSGNLVYRRTARNFNPMCAMAGRITIAEVEEIVENGELDPDAIHTPGIFVQRLVLNATPEKRIEQRVVRAKGD atoA ignore BRENDA::Q9D0K2 3-oxoacid CoA-transferase (EC 2.8.3.5) MAALKLLSSGLRLGASARSSRGALHKGCVCYFSVSTRHHTKFYTDPVEAVKDIPNGATLLVGGFGLCGIPENLIGALLKTGVKDLTAVSNNAGVDNFGLGLLLRSKQIKRMISSYVGENAEFERQFLSGELEVELTPQGTLAERIRAGGAGVPAFYTSTGYGTLVQEGGSPIKYNKDGSVAIASKPREVREFNGQHFILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAGTTVVEVEEIVDIGSFAPEDIHIPKIYVHRLIKGEKYEKRIERLSLRKEGDGKGKSGKPGGDVRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNMTVHLQSENGVLGLGPYPLKDEADADLINAGKETVTVLPGASFFSSDESFAMIRGGHVNLTMLGAMQVSKYGDLANWMIPGKMVKGMGGAMDLVSSSKTKVVVTMEHSAKGNAHKIMEKCTLPLTGKQCVNRIITEKGVFDVDKKNGLTLIELWEGLTVDDIKKSTGCDFAVSPNLMPMQQIST atoA ignore BRENDA::Q9JJN4 3-oxoacid CoA-transferase (EC 2.8.3.5) MAALRLLAWALPRGVSALRPPPALPHRLIRRYVSDRSGSVHFYTDPVKAVEGVKDGSTVMLGGFGLCGIPENLIGALKTKGVKDLKIVSSNVGVDDFGLGILLASKQVRRVVCSYLGENALCEKLYLAGELELEMTPQGTLAERIRAGGTGVPAFYTPTGYGTLVQEGGSPIRYAPDGHLITLSEPREVREFQGRFYLLEHAIRADFALIKGWKADRSGNVIFRGSARNFNVPMCKAADISVVEVEEIVDVGTFAPEDIHVPNIYVDRVIKGPKFEKRIERLTTRDSKPAPGSKDNDPSRTRIIKRAALEFQDGMYANLGIGIPVLASNYISPKMTVYLHSENGILGLGPFPLKNEVDADVINAGKQTVTVVPGGCFFASDDSFAMIRGGHLQLTMLGAMQVSQYGDLANWMVPGKKVKGMGGAMDLVSSKKTRVVVTMEHCTKTKQPKILKKCTMPLTGKRCVDLIITEKAVFEVNHSKGLTLVELWEGSSVDDIKATTACSFAVSPNLKPMQQIKLDA atoA ignore SwissProt::Q29551,BRENDA::Q29551 Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial; 3-oxoacid CoA-transferase 1; Somatic-type succinyl-CoA:3-oxoacid CoA-transferase; SCOT-s; EC 2.8.3.5;; 3-oxoacid CoA-transferase (EC 2.8.3.5) MAALTLLSSRLRLCASAYRSGGAWSQGCAGYFSTSTRRHTKFYTDAVEAVKDIPNGATVLVGGFGLCGIPENLIGALLKTGVKELTAVSNNAGVDNFGLGLLLQSKQIKRMISSYVGENAEFERQYLAGELEVELTPQGTLAERIRAGGAGVPAFYTSTGYGTLVQEGGSPIKYNKDGSIAIASKPREVREFNGQHFILEEAIRGDFALVKAWKADQAGNVTFRKSARNFNLPMCKAAETTVVEVEEIVDIGSFAPEDIHIPKIYVHRLVKGEKYEKRIERLSVRKEEDVKTRSGKLGDNVRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNMTVHLQSENGILGLGPYPLQNEVDADLINAGKETVTVLPGASYFSSDESFAMIRGGHVNLTMLGAMQVSKYGDLANWMIPGKLVKGMGGAMDLVSSAKTKVVVTMEHSAKGNAHKIMEKCTLPLTGKQCVNRIITEKAVFDVDSKKGLTLIELWEGLTVDDIKKSTGCDFAVSPKLIPMQQVTT atoA ignore SwissProt::Q5XIJ9 Succinyl-CoA:3-ketoacid coenzyme A transferase 2A, mitochondrial; 3-oxoacid CoA-transferase 2A; Testis-specific succinyl-CoA:3-oxoacid CoA-transferase 1; SCOT-t1; EC 2.8.3.5 MAALRLLAWAFSRRVSAHRPQPTLPHHLIRHYPTTRCGKVKFYTDPVKAVEGIKDGASVMLGGFGLCGIPENLIGALKTKGVKDLKIISSNVGVDDFGLGILLASKQVRRVVCSYLGENKLCEQLYLAGKLELEMTPQGTLAERIRAGGTGVPAFYTPTGYGTQVQEGGVPIRYSPEGHLITLSQPREVREFEGQHHLLERAIRADFALIKGWKADRSGNVIFRGSARNFNVPMCKAADISVVEVEEIVDVGTFAPEDIHIPNIYVKRVIKGPRFEKRIERLTTRDSPPAPGSKDQDPKRTRIIKRAALEFKDGMYANLGIGIPVLASNYISPKMTVYLHSENGILGLGPFPLKKEVDPDIINAGKQTVTVIPGGCFFASDDSFAMIRGGHIQLTMLGAMQVSKYGDLANWMVPGKKVKGMGGAMDLVSSKKTKVVVTMEHCTKTKQPKILEKCTMPLTGKSCVDLIITEKAVFEVDRSKGLKLVELWEGSSLDEVKATTGCSFKVCPNLKPMQQIKSDA atoA ignore SwissProt::Q9BYC2,BRENDA::Q9BYC2 Succinyl-CoA:3-ketoacid coenzyme A transferase 2, mitochondrial; 3-oxoacid CoA-transferase 2A; Testis-specific succinyl-CoA:3-oxoacid CoA-transferase; SCOT-t; EC 2.8.3.5;; 3-oxoacid CoA-transferase (EC 2.8.3.5) MAALRLLASVLGRGVPAGGSGLALSQGCARCFATSPRLRAKFYADPVEMVKDISDGATVMIGGFGLCGIPENLIAALLRTRVKDLQVVSSNVGVEDFGLGLLLAARQVRRIVCSYVGENTLCESQYLAGELELELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGGAPIRYTPDGHLALMSQPREVREFNGDHFLLERAIRADFALVKGWKADRAGNVVFRRSARNFNVPMCKAADVTAVEVEEIVEVGAFPPEDIHVPNIYVDRVIKGQKYEKRIERLTILKEEDGDAGKEEDARTRIIRRAALEFEDGMYANLGIGIPLLASNFISPSMTVHLHSENGILGLGPFPTEDEVDADLINAGKQTVTVLPGGCFFASDDSFAMIRGGHIQLTMLGAMQVSKYGDLANWMIPGKKVKGMGGAMDLVSSQKTRVVVTMQHCTKDNTPKIMEKCTMPLTGKRCVDRIITEKAVFDVHRKKELTLRELWEGLTVDDIKKSTGCAFAVSPNLRPMQQVAP atoA ignore SwissProt::Q9ESL0 Succinyl-CoA:3-ketoacid coenzyme A transferase 2B, mitochondrial; 3-oxoacid CoA-transferase 2B; Testis-specific succinyl-CoA:3-oxoacid CoA-transferase 2; SCOT-t2; EC 2.8.3.5 MAALRLLAWALPRGVSALRPRPALPHRLIRRYVSDRSGSVHFYTDPVKAVEGVKDGSTVMLGGFGLCGIPENLIGALKTKGVKDLKIVSSNVGVDDFGLGILLASKQVRRVVCSYLGENALCEKLYLAGELELEMTPQGTLAERIRACGTGVPAFYTPTGYGTLVQEGGSPIRYAPDGHLITLSEPREVREFQGRFYLLEHAIRADFALIKGWKADRSGNVIFRGSARNFNVPMCKAADISVVEVEEIVDVGTFAPEDIHIPNIYVDRVIKGPKFEKRIERLTTRDSKPAPGSKDNDPSRTRIIKRAALEFQDGMYANLGIGIPVLASNYISPKMTVYLHSENGILGLGPFPLKNEVDADVINAGKQTVTVVPGGCFFASDDSFAMIRGGHLQLTMLGAMQVSQYGDLANWMVPGKKVKGMGGAMDLVSSKKTRVVVTMEHCTKTKQPKILKKCTMPLTGKRCVDLIITEKAVFEVNHSKGLTLVELWEGSSVDDIKATTACSFAVSPNLKPMQQIKLDA atoA ignore SwissProt::Q9W058,BRENDA::Q9W058 Succinyl-CoA:3-ketoacid-coenzyme A transferase, mitochondrial; 3-oxoacid CoA-transferase; EC 2.8.3.5;; 3-oxoacid CoA-transferase (EC 2.8.3.5) MLCRLVGNRSLGARYTASIKAIACYSTSGKQRNGKIYESAIDAVADVQDGAQILFGGFGICGIPEKMINALKQKGVKNITGVSNNGGVDDTGLGVLIKQKQVSKVIGSYVGENTELVRQYLEGELAVELTPQGTLAEKIRAGGAGIPAFYTPTGYATLVQEGGAPIKYSKDGKVEISSEKKPVKEFNGKNYVMEESIFADFAFVKAQKADPLGNLVFNKAARNFNAPMCRAAKITVAEVEEIVPIGALSPDEIHVPGIYINRIFKGTNYNKRVERLRITEPKDPSKPAPPPNPAQVLRERIARRVALEFHDGMYANLGIGIPVLSSNYIPKGMNVMLQSENGILGLGPFPTKDKVDPDLINAGKESVTVVPGASYFGSDDSFAMIRGGHVDITILGAMEVSATGDLANWMIPGKLVKGMGGAMDLVAAPGTKVIITMEHNARDGSPKILDTCSLPLTGKGVIDMIISEKAVFTVEKGVGLTLIEVAEGYTVDDIIASTGAKFTVSPNLKKMGQIPV atoA ignore metacyc::HP0692-MONOMER succinyl-CoA:acetoacetate CoA-transferase subunit B (EC 2.8.3.5) MREAIIKRAAKELKEGMYVNLGIGLPTLVANEVSGMNIVFQSENGLLGIGAYPLEGSVDADLINAGKETITVVPGASFFNSADSFAMIRGGHIDLAILGGMEVSQNGDLANWMIPKKLIKGMGGAMDLVHGAKKVIVIMEHCNKYGESKVKKECSLPLTGKGVVHQLITDLAVFEFSNNAMKLVELQEGVSLDQVKEKTEAEFEVRL atoA ignore reanno::Cup4G11:RR42_RS06555 3-oxoacid CoA-transferase (EC 2.8.3.5) MNKVYASAAEALAGVVRDGQTIAVGGFGLCGIPEALIAALRDSGAKQLTCISNNAGVDGFGLGLLLATRQIKKMISSYVGENKEFERQYLAGELELEFTPQGTLAEKLRAGGSGIPAFFTKTGVGTIVADGKEIREFDGQQYVMERALTADVALVKAYKADRAGNLVFRRTARNFNPMCAMAGKVTIVEVEHLVDTGTLDPDEVHTPGIFVQRIVLNANPEKRIEQRTVRAAG atoA ignore reanno::SB2B:6937186 3-oxoacid CoA-transferase (EC 2.8.3.5) MALSREQLAQRVAKELKDGYYVNLGIGIPTLVANYIPDGMQVMLQSENGLLGMGEFPTEETIDPDLINAGKQTVTAVKGASFFSSAESFAMIRGGHVDLTVLGAFEVDVEGSIASWMIPGKLVKGMGGAMDLVAGADNIIVTMMHADKYGNSKLLPKCELPLTGFGCIKRVLTDLAFIEIKDGAFHLLERAPGVTVEEIVEKTAGKLIVPEHVPEMQF atoA ignore reanno::SB2B:6937187 3-oxoacid CoA-transferase (EC 2.8.3.5) MAGLYKVVDSYDQALAGLTDNMTIMVGGFGLCGIPEGLINQMVKLGTKGLTAISNNAGVDDFGLGLLLQNKQISTMIASYVGENATFERQMLSGELNVILTPQGTLAEKIRAGGAGIPAFFTATGYGTPVAEGKETREIKGRHYVLEESLTADFALIRAWKADTMGNLVFRKTAANFNPMMATAGKITVVEVEEIVEPGELDPDHIHTPGIYVDRIIKGSFEKRIEQRTVKKA atoB curated BRENDA::A4YEH9,metacyc::MONOMER-13740 acetyl-CoA C-acetyltransferase (EC 2.3.1.9);; acetyl-CoA C-acetyltransferase (EC 2.3.1.16) MPDVYIVSAVRTPIGRFGGSLKSVKPQMLGAIAIKEALRRANTDPSRVELTIMGNVLRSGHGQDLARQAALLAGIPWEVDGYCVDMVCSSGMMGVTNAAQMIKSGDADVVVAGGMESMSQSMLAVNSEVRWGVKFLSGKSLNFIDTMLVDGLTDPFNLKLMGQEADMVARERDISRRELDEVAFESHRRAHQAWEKGLFKSEVIPVNLDEGKLERDEGIRPDTTMEKLSSLKPAFTENGYHTAGNSSQISDGAVAMVLMSEKAVKEFGVDPVAKILGYSWVGIESWRFTEAPLYSVRKLLTRLNMNITQFDYFENNEAFAVNNVLFHRYLGVPYDQLNVFGGAIALGHPIGASGARIMVTLLNVLSKMNATRGIASICHGVGGSTAIALELLRPL atoB curated BRENDA::B1YB71 acetyl-CoA C-acetyltransferase (EC 2.3.1.9) MDVVVVGYVRTPIGKFGGAFKDVKPPHLAAFTIKKLLERTGVDGKLVEEVIFGSTLQGGVGQNVARYAALLAGLPVDVSAFTVNRVCSSGMQAIIEAYREIALGDASVVIAGGVESMSTQPICVSHEARWGLRHSIGRRFELTDLMVFDGLTDPATGMLMGEEADMVAKEHKIAREELDKVAYESHMRAWRATENKWFDDMEPVEGEFGGVKLDRDEGIRPDTSLEKLAKLKPAFKPDGLHTAGNSSQLSDGAAALLLMSEEKARELGVKPIARILGYSWHMLEPWRFTEAPVYAIQKLLRKLGVSVDYFDYYEANEAFAVVNVLVNRVLGVPYDRMNVFGGAIALGHPLGASGTRIVTTLISVLRRMGGRRGVAALCHGTGGGTAVALELI atoB curated BRENDA::B7XEI5 acetyl-CoA C-acetyltransferase (EC 2.3.1.9) MSVAVKGVFIVGAKRTPFGTFGGVFRNTSATELQTIAATAALKEANVAPDQVDTVTVGQVMSGTQTDGIYTPRHAALKAGIPQEKPVLGINRLCGSGFQSVINGAQDILTGAAKVSLAGGVENMSQAPFAVRGVRFGTTLGLNYAFEDTLWAGLTDSYCGLPMGMTAEKLGAQYSITRDEVDNFALQSQQRWKTSNDAGVFKAEIEPVTLTIKRKQVSVAVDEHPRPQTTLEGLKKLPPVFKKEGLVTAGTASGISDGAGAIVLASEEAAKGLKPLARLVGWSVVGVDPSIMGVGPVPAIQNLLKATNMTLNDVDLIEINEAFCAQTLACAKALKLDMNKLNVNGGATALGHPLGASGSRITAHLVHELRRRGLKRAIGSACIGGGQGIALMVEAV atoB curated BRENDA::D0EUY6 acetyl-CoA C-acetyltransferase (EC 2.3.1.9) MAASDSTITPRDVCIVGVARTPMGVFLGTLSSVPATKLGSIAIEAALKRANVDPAIVEEVFFGNVLSANLGQAPARQAALGAGLSKSVVCTTVNKVCASGMKATMLAAQSIQLGINDVVVAGGMENMSNVPKYLAEARKGSRLGHDSLVDGMLKDGLWDVYKDVGMGVCAELCADNHQITRENQDNYAVQSFERRISAQENGYFGWEIIPVEVSGGRGRPSTIVDKDEGLGKFDAAKLRKLRPSFKETGGTVTAGNASSISDGATPLVLVSGEKALKLGLQVIAKITGYADAAQDPELFTTAPAIAVPKAIANAGLETSKIDYYEINEAFAVVALANQKLLGLDSHKVNVHGGAVSLGHPLGCSGARILVTLLGVLKQKNGKYGVGGVCNGGGGASALVVELL atoB curated BRENDA::D2IH11 acetyl-CoA C-acetyltransferase (EC 2.3.1.9) MQIMDKINPRDVCIVGVARTPMGDFLGSLSSLPATKLGSIAIQSALQRANIDPRLVQEVFFGNVLSANLGQAPARQAALGAGIPDTVVCTTINKVCSSGMKATMIAAQSIQVGANDIVVAGGMESMSNTPKYVAGSRRGSRLGHDAIIDGMIKDGLWDVYNDFGMGVCGELCADTYKITRQDQDDYAVRSFNRGIAAQKNGAFKWEIVPVEVSGGRGKVPMVVDKDEGLTKFDATKLRNLRPSFKVEGGSVTAGNASSISDGAAALVLVSGEKALKLGLKVIAKIRGFADAAQAPELFTTAPSLAIPKAISNAGLTASQIDYYEINEAFSVVALANQKLLKIGDSQLNAHGGAVSLGHPLGCSGARILVTLLGVLRQNNGRFGVAGICNGGGGASALVLELMPSAGTLSKL atoB curated BRENDA::G7YHN5 acetyl-CoA C-acetyltransferase (EC 2.3.1.9) MGGLSLSTPCTAVNKICASGMKSIMLAAQSIALGHQSVICAGGMESMSNAPFYLARQMPTYGGAQLLDSVVWDGLTDSKYGIHMGRCCEKTVSDLKITREEQDAYAKLSYERSQTAAKNDVFLSEITPVQIANKKSPTGFDEVSEDEEYKRVDFQRFPTLKPAFVRAEDGGTITAANASTLNDGAAAAILASASYAAKDRTLKPLARIVAYADAATDTIDFSIAPHLAVEKLLTITGVKKEDVVLWEINEAFSAVVLANMRLLGLDVKNVNVHGGAVSCGHPVG atoB curated BRENDA::I3R3D1 acetyl-CoA C-acetyltransferase (subunit 2/2) (EC 2.3.1.9) MDRVAIIGASMTQFGQRDAWIRELLAEAGQAALADADVSPDEIEHLYVSNMASGEFEGQTGVPNALAHDLAAMPAYTARIDQTSSSGGAGVYAAWQSVASGASDMTMLVGGEKMTHRSTAEATDVIASLTHPVEYKHGVTLPSFAGLTARLYLDTYDAPRESLGKVAVKNHKNGLDNPHAQFRKEVDLETVLDSPVVADPLRLYDFCPITDGSAALVFCSESVAREYTDDYVVISGIGGATDTHVVHERADPTTMGGVVNSSDIAYEMADLEPDDIDVAELHDMFTILEFLQSEDLGFFEKGEGWKAVEEGVTDRDGELPINTSGGLKSKGHPLGASGVAQVYEIYKQLIGDAGDRQVDADIGLACNVGGFGNCVTTTIMESQ atoB curated BRENDA::I3RA72 acetyl-CoA C-acetyltransferase (subunit 2/2) (EC 2.3.1.9) MEVAVIGSSMTKFGQRSAWIRELLSEAGQACLEDAGVAPASVDHLYVSNMASGEFEGQTGVMNALAHDLGVIPAYTQRIDQTSSSGGAGIYEAWQSIASGVSEMTLLVGGEKMTHKTTGESTDIIASCTHPEEYKHGVTLPSFAGMTARNYLERFDAPRESLARVAVKNHRNGVDNPKAQFQKEIDIETALESPIIADPLRLYDFCPITDGSAAMMFTTEERAQEITDEYAIVSGVGGATDTHVVHERDDPTVMGGVVESSKQAYEMAGVGPDDLDVAELHDMFTILEFLQLEGIGVADHGAAWELAMDGVTAKDGGLPINTSGGLKSKGHPLGASGVAQGVEIYEQLVGEAGPRQVEADTALACNVGGFGNCVITTIMEAAK atoB curated BRENDA::P42765,SwissProt::P42765,metacyc::HS09539-MONOMER acetyl-CoA C-acyltransferase (EC 2.3.1.16);; 3-ketoacyl-CoA thiolase, mitochondrial; Acetyl-CoA acetyltransferase; Acetyl-CoA acyltransferase; Acyl-CoA hydrolase, mitochondrial; Beta-ketothiolase; Mitochondrial 3-oxoacyl-CoA thiolase; T1; EC 2.3.1.16; EC 2.3.1.9; EC 3.1.2.-; EC 3.1.2.1; EC 3.1.2.2;; 3-ketoacyl-CoA thiolase, mitochondrial (EC 2.3.1.16) MALLRGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLGSDIKLEDSLWVSLTDQHVQLPMAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQSTA atoB curated BRENDA::P45359,metacyc::THLCLOS-MONOMER acetyl-CoA C-acetyltransferase (EC 2.3.1.9);; acetoacetyl-CoA thiolase monomer (EC 2.3.1.16) MKEVVIASAVRTAIGSYGKSLKDVPAVDLGATAIKEAVKKAGIKPEDVNEVILGNVLQAGLGQNPARQASFKAGLPVEIPAMTINKVCGSGLRTVSLAAQIIKAGDADVIIAGGMENMSRAPYLANNARWGYRMGNAKFVDEMITDGLWDAFNDYHMGITAENIAERWNISREEQDEFALASQKKAEEAIKSGQFKDEIVPVVIKGRKGETVVDTDEHPRFGSTIEGLAKLKPAFKKDGTVTAGNASGLNDCAAVLVIMSAEKAKELGVKPLAKIVSYGSAGVDPAIMGYGPFYATKAAIEKAGWTVDELDLIESNEAFAAQSLAVAKDLKFDMNKVNVNGGAIALGHPIGASGARILVTLVHAMQKRDAKKGLATLCIGGGQGTAILLEKC atoB curated BRENDA::Q0K368 acetyl-CoA C-acetyltransferase (EC 2.3.1.9) MAEAYIVAAVRTAGGRKGGKLSGWHPADLAAQVLDALVERTGADPALVEDVIMGCVSQVGEQAGNVARNAILASRLPESVPGTSVDRQCGSSQQALHFAAQAVMSGAMDIVIAAGVESMTRVPMGLSSQLPAKNGFGVPKSPGIEARYPGVQFSQFTGAEMIARKYDLSREQLDAYALQSHQRAIAATKSGRFTAEILPVEVRTADGANGEMHTTDEGVRYDATLESIGSVKLIAEGGRVTAASASQICDGAAGLMVVNEAGLKKLGVKPLARVHAMTVIGHDPVVMLEAPLPATEVALKKAGLRIGDIDLFEVNEAFAPVPLAWLKATGADPARLNVHGGAIALGHPLGGSGAKLMTTLVHALHTHGKRYGLQTMCEGGGLANVTIVERL atoB curated BRENDA::Q0KAI3 acetyl-CoA C-acetyltransferase (EC 2.3.1.9) MQQAVIVDAIRSPMGRSKPGSAFTELHATELLAQVIKGLVERNKLDPGLVDDVITGCVTQAGEQSAGPGRVAWLAAGFPDHVPATTIDRKCGSSQQAVHFAAQGIMAGAYDIVIACGIESMSRVPMGSARIGQNPYGPSMEARYAPGLVSQGVAAELVAAKYELSRHDMDSYSARSHELAATARESGAFRREILGISTPNGLVEQDETIRPGTSVEKLGTLQASFRNDELSARFPQIGWNVTAGNASQISDGASAMLLMSESMAQRLGLKPRARFVAFDVCGDDPVMMLTAPIPASQRAIKKSGLKLDQIDHYEINEAFACVPLAWQRALGADPARLNPRGGAIALGHPLGASGVRLMTTMLHALEDSGQRYGLQSMCEAGGMANATIIERL atoB curated BRENDA::Q86AD9 acetyl-CoA C-acetyltransferase (EC 2.3.1.9) MISNLSKVLNSNVKRMYTTAKNLESVVIVSAVRTPIGSIGGSLSTIPGTKLSSITIEEAVKRAGIKPSDVDEAIIGNVISANLGQAPARQCALGAGLEQKTITTTINKVCSSGMKAIVFGAQSIALGHSKTVVAGGFESMSQVPYYADKMRFGAKYGNQTFIDGLVRDGLADAYNGSAMGVCGDDCADKYKITREQQDKFAVDSYLRALEAQKNGFFNDEIVQVPIVGRGGKVTYVVEDEEPKKVLFDKIPNLKPAFTPNGTVTPANASKLNDGASSVILMSESHAKELGLKPLARIIGYADAEQAPIEFPTAPALAIPKALKNAGINMSQVDLFEINEAFAVVGLANAKILDIDHNKLNVNGGAVALGHPIGSSGCRIVVTLTHLLQNKNLKYGVAAICNGGGGSTALVLEKL atoB curated BRENDA::Q8S4Y1 acetyl-CoA C-acetyltransferase (EC 2.3.1.9) MAHTSESVNPRDVCIVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANLGQAPARQAALGAGIPNSVICTTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLAEARKGSRFGHDSLVDGMLKDGLWDVYNDCGMGSCAELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGRPSTIVDKDEGLGKFDAAKLRKLRPSFKENGGTVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQVDYYEINEAFAVVALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKYGVGGVCNGGGGASALVLELL atoB curated BRENDA::Q8VCH0,SwissProt::Q8VCH0 acetyl-CoA C-acyltransferase (EC 2.3.1.16);; 3-ketoacyl-CoA thiolase B, peroxisomal; Acetyl-CoA acyltransferase B; Beta-ketothiolase B; Peroxisomal 3-oxoacyl-CoA thiolase B; EC 2.3.1.155; EC 2.3.1.16; EC 2.3.1.9 MHRLQVVLGHLAGRPESSSALQAAPCSAGFLQASASDVVVVHGRRTPIGRASRGCFKDTTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVLQPGAGAIMARIAQFLSGIPETVPLSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSQRGNHGNISSRLLENEKARDCLIPMGITSENVAERFGVSRQKQDAFALASQQKAASAQSRGCFHAEIVPVTTTVLNDKGDKKTITVSQDEGVRPSTTMQGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRAYGVVSMCIGTGMGAAAVFEYPGN atoB curated BRENDA::Q9FIK7 acetyl-CoA C-acetyltransferase (EC 2.3.1.9) MAPPVSDDSLQPRDVCVVGVARTPIGDFLGSLSSLTATRLGSIAIQAALKRAHVDPALVEEVFFGNVLTANLGQAPARQAALGAGIPYSVICTTINKVCAAGMKSVMLASQSIQLGLNDIVVAGGMESMSNVPKYLPDARRGSRLGHDTVVDGMMKDGLWDVYNDFGMGVCGEICADQYRITREEQDAYAIQSFERGIAAQNTQLFAWEIVPVEVSTGRGRPSVVIDKDEGLGKFDAAKLKKLRPSFKEDGGSVTAGNASSISDGAAALVLVSGEKALELGLHVIAKIRGYADAAQAPELFTTTPALAIPKAIKRAGLDASQVDYYEINEAFSVVALANQKLLGLDPERLNAHGGAVSLGHPLGCSGARILVTLLGVLRAKKGKYGVASICNGGGGASALVLEFMSEKTIGYSAL atoB curated SwissProt::P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 MSTPSIVIASARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWGMNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCAHLAGGVKMGDFKMIDTMIKDGLTDAFYGYHMGTTAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDITVDADEYIRHGATLDSMAKLRPAFDKEGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL atoB curated SwissProt::P07871 3-ketoacyl-CoA thiolase B, peroxisomal; Acetyl-CoA acyltransferase B; Beta-ketothiolase B; Peroxisomal 3-oxoacyl-CoA thiolase B; EC 2.3.1.155; EC 2.3.1.16; EC 2.3.1.9 MHRLQVVLGHLAGRSESSSALQAAPCSAGFPQASASDVVVVHGRRTPIGRAGRGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGNISSRLLENEKARDCLIPMGITSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTVLDDKGDRKTITVSQDEGVRPSTTMEGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFASQALYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRAYGVVSMCIGTGMGAAAVFEYPGN atoB curated SwissProt::P13437 3-ketoacyl-CoA thiolase, mitochondrial; Acetyl-CoA acetyltransferase; Acetyl-CoA acyltransferase; Acyl-CoA hydrolase, mitochondrial; Beta-ketothiolase; Mitochondrial 3-oxoacyl-CoA thiolase; EC 2.3.1.16; EC 2.3.1.9; EC 3.1.2.-; EC 3.1.2.1; EC 3.1.2.2 MALLRGVFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTETGALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRFGTKFGLDLKLEDTLWAGLTDQHVKLPMGMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQNLPPVFKKEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEAFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQNTA atoB curated SwissProt::P14611,metacyc::MONOMER-13086 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9;; acetyl-CoA acetyltransferase subunit (EC 2.3.1.16) MTDVVIVSAARTAVGKFGGSLAKIPAPELGAVVIKAALERAGVKPEQVSEVIMGQVLTAGSGQNPARQAAIKAGLPAMVPAMTINKVCGSGLKAVMLAANAIMAGDAEIVVAGGQENMSAAPHVLPGSRDGFRMGDAKLVDTMIVDGLWDVYNQYHMGITAENVAKEYGITREAQDEFAVGSQNKAEAAQKAGKFDEEIVPVLIPQRKGDPVAFKTDEFVRQGATLDSMSGLKPAFDKAGTVTAANASGLNDGAAAVVVMSAAKAKELGLTPLATIKSYANAGVDPKVMGMGPVPASKRALSRAEWTPQDLDLMEINEAFAAQALAVHQQMGWDTSKVNVNGGAIAIGHPIGASGCRILVTLLHEMKRRDAKKGLASLCIGGGMGVALAVERK atoB curated SwissProt::P24752,metacyc::HS01167-MONOMER Acetyl-CoA acetyltransferase, mitochondrial; Acetoacetyl-CoA thiolase; T2; EC 2.3.1.9;; acetyl-CoA acetyltransferase monomer (EC 2.3.1.16) MAVLAALLRSGARSRSPLLRRLVQEIRYVERSYVSKPTLKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQGEYGLASICNGGGGASAMLIQKL atoB curated SwissProt::P41338,metacyc::YPL028W-MONOMER Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Ergosterol biosynthesis protein 10; EC 2.3.1.9;; Erg10 (EC 2.3.1.16) MSQNVYIVSTARTPIGSFQGSLSSKTAVELGAVALKGALAKVPELDASKDFDEIIFGNVLSANLGQAPARQVALAAGLSNHIVASTVNKVCASAMKAIILGAQSIKCGNADVVVAGGCESMTNAPYYMPAARAGAKFGQTVLVDGVERDGLNDAYDGLAMGVHAEKCARDWDITREQQDNFAIESYQKSQKSQKEGKFDNEIVPVTIKGFRGKPDTQVTKDEEPARLHVEKLRSARTVFQKENGTVTAANASPINDGAAAVILVSEKVLKEKNLKPLAIIKGWGEAAHQPADFTWAPSLAVPKALKHAGIEDINSVDYFEFNEAFSVVGLVNTKILKLDPSKVNVYGGAVALGHPLGCSGARVVVTLLSILQQEGGKIGVAAICNGGGGASSIVIEKI atoB curated SwissProt::P45363 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 MSDTIVIVDAGRTAIGTFGGALSALQATDIGTTVLKALIERTGIAPEQVSEVILGQVLTAGCGQNPARQTTLMAGLPHTVPAMTINKVCGSGLKAVHLAMQAVACGDAEIVIAGGQESMSQSSHVLPRSREGQRMGDWPMKDTMIVDGLWDAFNQCHMGVTAENIAKKYAFTREAQDAFAAASQQKAEAAIQSGRFADEIIPVSIPQRKGDPLVFDTDEFPRPGTTAETLGRLRPAFDKQGTVTAGNASGINDGAAMVVVMKESKAKELGLTPMARLVAFSSAGVDPAIMGTGPIPASTDCLKKAGWAPADLDLVEANEAFAAQAMSVNQEMGWDLSKVNVNGGAIAIGHPIGASGARVLVTLLYEMQKRDAKKGLATLCIGGGQGVALAVERL atoB curated SwissProt::P45369 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 MNENIVIVDAGRSAIGTFSGSLSSLSATEIGTAVLKGLLARTGLAPEQIDEVILGQVLTAGVGQNPARQTTLKAGLPHSVPAMTINKVCGSGLKAVHLAMQAIACGDADIVIAGGQESMSQSSHVLPRSRDGQRMGDWSMKDTMIVDGLWDAFNNYHMGTTAENIAQKYGFTREQQDAFAAASQQKTEAAQKAGRFQDEIIPIEIPQRKGDPKVFDADEFPRHGTTAESLGKLRPAFSRDGSVTAGNASGINDGAAMVVVMKESKAKELGLKPMARLVAFASAGVDPAIMGTGPIPASTKCLEKAGWTPADLDLIEANEAFAAQAMSVNQDMGWDLSKVNVNGGAIAIGHPIGASGARVLVTLLYEMQKRDAKKGLATLCIGGGQGVALAVERM atoB curated SwissProt::P45855 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; EC 2.3.1.9 MRKTVIVSAARTPFGKFGGVLKEVKAAELGGIVMKEALQQAGVSGDDVEGNVMGMVVQAGSGQIPSRQAARLAGMPWSVPSETLNKVCASGLRAVTLCDQMIRAQDADILVAGGMESMSNIPYAVPAGRWGARMGDGELRDLMVYDGLTCAFDEVHMAVHGNTAAKEYAISRREQDEWALRSHARAAKAADEGKFQDEIVPVNWIGRKGKPNVVDKDEAIRRDTSLDQLAKLAPIYASDGSITAGNAPGVNDGAGAFVLMSEEKAAELGKRPLATILGFSTTGMPAHELAAAPGFAINKLLKKNGLTVQDIDLFEVNEAFASVVLTCEKIVGFDLEKVNVNGGAIALGHPIGASGARILMTLVYELKRRGGGLGVAAICSGAAQGDAVLVQVH atoB curated SwissProt::P50174,reanno::Smeli:SMc03879 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9;; Acetyl-CoA acetyltransferase (EC 2.3.1.9) MSNPSIVIASAARTAVGSFNGAFGNTLAHELGAAAIKAVLERAGVEAGEVDEVILGQVLPAGEGQNPARQAAMKAGLPQEKTAWGMNQLCGSGLRAVALGMQQIATGDAKVIVAGGMESMSMAPHCAHLRGGVKMGDYKMIDTMIKDGLTDAFYGYHMGITAENVARKWQLTREEQDEFALASQNKAEAAQKAGRFADEIVPFVVKTRKGDVNVDQDEYIRHGATLDSIAKLRPAFDKEGTVTAGNASGLNDGAAAALLMTEAEAARRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVADIELVEANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGVSKGLATLCIGGGMGVAMCVERL atoB curated SwissProt::P73825 Acetyl-CoA acetyltransferase; Beta-ketothiolase PhaA; EC 2.3.1.9 MRDVFIVAAKRTPLGRFGGSLTNFSAADLGAHVMKSVLAQAGVGGDQLDLYIMGNVLRAGHGQLIPRQAALKAEIPDTVDGYAVDMVCSSAMMSVINAALTIRAGEGDLILAGGTESMSQTGFYLSHRARWGYKFLMGAPENLTDLLLHDGLTDSTNGEGMGEQTEKLAAEHGFSRIELDEVACLSQQRAAHATESGYFDSEIAPIEITSRKGTQVLASDEGIRSDTTVESLGKLRSAFAKDGVLTAGNCSQITDGAAALLLASGEAVEKYQLKPLAKILGGSWAAGTPSRFPELPITASQKLLAKLDKTLADFDLFENNEAFSVSNLLFERRLGVDRDKLNVNGGAIALGHPIGASGARIMVTLLYALQQRDKTLGLAALCHGTGGGTAIALERV atoB curated SwissProt::Q0AVM3 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; EC 2.3.1.9 MTREVVLVGACRTPVGTFGGTLKDVGSAQLGAIVMGEAIKRAGIKAEQIDEVIFGCVLQAGLGQNVARQCMINAGIPKEVTAFTINKVCGSGLRAVSLAAQVIKAGDADIIMAGGTENMDKAPFILPNARWGYRMSMPKGDLIDEMVWGGLTDVFNGYHMGITAENINDMYGITREEQDAFGFRSQTLAAQAIESGRFKDEIVPVVIKGKKGDIVFDTDEHPRKSTPEAMAKLAPAFKKGGSVTAGNASGINDAAAAVIVMSKEKADELGIKPMAKVVSYASGGVDPSVMGLGPIPASRKALEKAGLTIDDIDLIEANEAFAAQSIAVARDLGWADKMEKVNVNGGAIAIGHPIGSSGARILVTLLYEMQKRGSKKGLATLCIGGGMGTALIVEAL atoB curated SwissProt::Q0KBP1,metacyc::MONOMER-16779 Beta-ketothiolase BktB; Acetyl-CoA acetyltransferase; Acetyl-CoA acyltransferase; EC 2.3.1.16; EC 2.3.1.9;; β-ketothiolase (EC 2.3.1.16) MTREVVVVSGVRTAIGTFGGSLKDVAPAELGALVVREALARAQVSGDDVGHVVFGNVIQTEPRDMYLGRVAAVNGGVTINAPALTVNRLCGSGLQAIVSAAQTILLGDTDVAIGGGAESMSRAPYLAPAARWGARMGDAGLVDMMLGALHDPFHRIHMGVTAENVAKEYDISRAQQDEAALESHRRASAAIKAGYFKDQIVPVVSKGRKGDVTFDTDEHVRHDATIDDMTKLRPVFVKENGTVTAGNASGLNDAAAAVVMMERAEAERRGLKPLARLVSYGHAGVDPKAMGIGPVPATKIALERAGLQVSDLDVIEANEAFAAQACAVTKALGLDPAKVNPNGSGISLGHPIGATGALITVKALHELNRVQGRYALVTMCIGGGQGIAAIFERI atoB curated SwissProt::Q9BWD1,metacyc::ENSG00000120437-MONOMER Acetyl-CoA acetyltransferase, cytosolic; Acetyl-CoA transferase-like protein; Cytosolic acetoacetyl-CoA thiolase; EC 2.3.1.9;; acetyl-CoA acetyltransferase (EC 2.3.1.16) MNAGSDPVVIVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWSCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHLAYLRTGVKIGEMPLTDSILCDGLTDAFHNCHMGITAENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEVKTDEFPRHGSNIEAMSKLKPYFLTDGTGTVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQRE atoB curated SwissProt::Q9UQW6 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Ergosterol biosynthesis protein 10; EC 2.3.1.9 MVNTEVYIVSAVRTPMGSFGGSFASLPATKLGSIAIKGALERVNIKPSDVDEVFMGNVVSANLGQNPARQCALGAGLPRSIVCTTVNKVCASGMKATILGAQTIMTGNAEIVVAGGTESMSNAPYYAPKNRFGAKYGNVELVDGLLRDGLSDAYDGLPMGNAAELCAEEHSIDRASQDAFAISSYKRAQNAQATKAFEQEIVPVEVPVGRGKPNKLVTEDEEPKNLNEDKLKSVRAVFKSNGTVTAANASTLNDGASALVLMSAAKVKELGLKPLAKIIGWGEAAQDPERFTTSPSLAIPKALKHAGIEASQVDYYEINEAFSVVAVANTKILGLDPERVNINGGGVAMGHPLGSSGSRIICTLAYILAQKDAKIGVAAVCNGGGGASSIVIERV atoB curated ecocyc::ACETYL-COA-ACETYLTRANSFER-MONOMER,metacyc::ACETYL-COA-ACETYLTRANSFER-MONOMER acetyl-CoA acetyltransferase (EC 2.3.1.16; EC 2.3.1.9);; acetyl-CoA acetyltransferase (EC 2.3.1.16) MKNCVIVSAVRTAIGSFNGSLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAGLGQNPARQALLKSGLAETVCGFTVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPYLLDAKARSGYRLGDGQVYDVILRDGLMCATHGYHMGITAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVTRKKTFVFSQDEFPKANSTAEALGALRPAFDKAGTVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQLADIDLIEANEAFAAQFLAVGKNLGFDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGIAMVIERLN atoB curated reanno::Phaeo:GFF329 acetyl-CoA:acetyl-CoA C-acetyltransferase / acetyl-CoA:propanoyl-CoA 2-C-acetyltransferase (EC 2.3.1.9; EC 2.3.1.16) MTNVVIASAARTAVGSFGGAFAKTPAHDLGAAVLQAVVERAGIDKSEVSETILGQVLTAAQGQNPARQAHINAGLPQESAAWSLNQVCGSGLRAVALAAQHIQLGDAAIVCAGGQENMTLSPHAANLRAGHKMGDMSYIDTMIRDGLWDAFNGYHMGQTAENVAEKWQISREMQDEFAVASQNKAEAAQKAGKFADEIAAFTVKTRKGDIIVDQDEYIRHGATIEAMQKLRPAFAKDGSVTAANASGLNDGAAATLLMSADDAEKRGIEPLARIASYATAGLDPSIMGVGPIYASRKALEKAGWSVDDLDLVEANEAFAAQACAVNKDMGWDPAIVNVNGGAIAIGHPIGASGCRVLNTLLFEMKRRDAKKGLATLCIGGGMGVAMCVERP atoB curated reanno::pseudo13_GW456_L13:PfGW456L13_2411 Acetyl-CoA C-acetyltransferase (EC 2.3.1.9) MNTPEIYVVSAARTAIGTFGGSLKDVPLADLATTAVKAALERAAVDPALVGHLVMGNVIPTETRDAYISRVAAMNAGIPKETPAYNVNRLCGSGLQAIINAAQTLMLGDADIVVGAGAESMSRGPYLMPAARWGSRMGNAQVIDYMLGILHDPFHGIHMGITAENVAARNGITREMQDALAFEDQQRAAHAIANGYFSEQIATVEIQDRKGVKLFSVDEHPRATSLEQLAAMKPAFKKDGSVTAGNASGLNDGAAALVMASGNAVQANNLKPLARLVSYAHAGVEPEFMGLGPIPATRLALKRAGLTVADLDVIEANIAFAAQACAVSQELDLDPAKVNPNGSGIALGHPVGATGAIIATKAIHELHRTGGRYALVTMCIGGGQGIAAIFERV atoB curated reanno::pseudo3_N2E3:AO353_25685 acetyl-CoA:acetyl-CoA C-acetyltransferase / acetyl-CoA:propanoyl-CoA 2-C-acetyltransferase (EC 2.3.1.9; EC 2.3.1.16) MTMSHDPIVIVSAVRTPMGGFQGELKSLSAPQLGAAAIRAAVERAGVAADAVEEVLFGCVLSAGLGQAPARQAALGAGLDKSTRCTTLNKMCGSGMEAAILAHDMLLAGSADVVVAGGMESMSNAPYLLDRARSGYRMGHGKVLDHMFLDGLEDAYDKGRLMGTFAEDCAEANGFTREAQDEFAIASTTRAQQAIKDGSFNAEIVPLQVIVGKEQKLITDDEQPPKAKLDKIASLKPAFRDGGTVTAANSSSISDGAAALLLMRRSEAEKRGLKPLAVIHGHAAFADTPGLFPVAPVGAIKKLLKKTGWSLDEVELFEVNEAFAVVSLVTMTKLEIPHSKVNVHGGACALGHPIGASGARILVTLLSALRQKGLKRGVAAICIGGGEATAMAVECLY atoB curated reanno::pseudo5_N2C3_1:AO356_21640 acetyl-CoA C-acetyltransferase [EC: 2.3.1.9] MQEVVIVAATRTAIGSFQGSLAAIPAPELGAAVIRRLLEQTGLSGEQVDEVILGQVLTAGSGQNPARQASILAGLPHAVPALTLNKVCGSGLKALHLGAQAIRCGDAEVIIAGGMENMSLAPYVLPAARTGLRMGHAKMIDSMITDGLWDAFNDYHMGITAENLVDKYGISREEQDAFAAASQQKAVAAIEGGRFADEITPILIPQRKGDPVAFATDEQPRAGTTAESLGKLKPAFKKDGSVTAGNASSLNDGAAAVILMSAEKAKALGLPVLAKISAYANAGVDPAIMGIGPVSATRRCLDKAGWSLEQLDLIEANEAFAAQSLAVARELKWDMDKVNVNGGAIALGHPIGASGCRVLVSLLHEMIKRDAKKGLATLCIGGGQGVALALERA atoB curated2 P07097 Acetyl-CoA acetyltransferase; EC 2.3.1.9; Acetoacetyl-CoA thiolase; Beta-ketothiolase MSTPSIVIASARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWGMNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCAHLAGGVKMGDFKMIDTMIKDGLTDAFYGYHMGTTAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDITVDADEYIRHGATLDSMAKLRPAFDKEGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL atoB curated2 P44873 Acetyl-CoA acetyltransferase; EC 2.3.1.9; Acetoacetyl-CoA thiolase MENVVIVSAVRTPIGSFNGALSSVSAVDLGAIVIQEAIKRANIESALVNEVIMGNVLQAGLGQNPARQAALKAGIEKEIPSLTINKVCGSGLKSVALGAQSIISGDADIVVVGGMENMSQAPYLLDSKVRQGVKMGNLTLRDTMIEDGLTCASNHYHMGITAENIAEQYGISRQAQDELALRSQTLASQAVQLGVFDKEIVPVMVKTRKGDIIVSRDEYPKADTTAEGLAKLKPAFKKEGTVTAGNASGINDGAAALILVSESKAHALGLKAIAKIRSYASGGVDPSVMGLGPVPATQKALKKAGINLDDIDLIEANEAFASQFLGVGKDLNLDMNKTNIHGGAIALGHPIGASGARILVTLLHNLIEKDKKLGLATLCIGGGQGISMIVERL atoB curated2 P45359 Acetyl-CoA acetyltransferase; EC 2.3.1.9; Acetoacetyl-CoA thiolase MKEVVIASAVRTAIGSYGKSLKDVPAVDLGATAIKEAVKKAGIKPEDVNEVILGNVLQAGLGQNPARQASFKAGLPVEIPAMTINKVCGSGLRTVSLAAQIIKAGDADVIIAGGMENMSRAPYLANNARWGYRMGNAKFVDEMITDGLWDAFNDYHMGITAENIAERWNISREEQDEFALASQKKAEEAIKSGQFKDEIVPVVIKGRKGETVVDTDEHPRFGSTIEGLAKLKPAFKKDGTVTAGNASGLNDCAAVLVIMSAEKAKELGVKPLAKIVSYGSAGVDPAIMGYGPFYATKAAIEKAGWTVDELDLIESNEAFAAQSLAVAKDLKFDMNKVNVNGGAIALGHPIGASGARILVTLVHAMQKRDAKKGLATLCIGGGQGTAILLEKC atoB curated2 P45363 Acetyl-CoA acetyltransferase; EC 2.3.1.9; Acetoacetyl-CoA thiolase; Beta-ketothiolase MSDTIVIVDAGRTAIGTFGGALSALQATDIGTTVLKALIERTGIAPEQVSEVILGQVLTAGCGQNPARQTTLMAGLPHTVPAMTINKVCGSGLKAVHLAMQAVACGDAEIVIAGGQESMSQSSHVLPRSREGQRMGDWPMKDTMIVDGLWDAFNQCHMGVTAENIAKKYAFTREAQDAFAAASQQKAEAAIQSGRFADEIIPVSIPQRKGDPLVFDTDEFPRPGTTAETLGRLRPAFDKQGTVTAGNASGINDGAAMVVVMKESKAKELGLTPMARLVAFSSAGVDPAIMGTGPIPASTDCLKKAGWAPADLDLVEANEAFAAQAMSVNQEMGWDLSKVNVNGGAIAIGHPIGASGARVLVTLLYEMQKRDAKKGLATLCIGGGQGVALAVERL atoB curated2 P45855 Acetyl-CoA acetyltransferase; EC 2.3.1.9; Acetoacetyl-CoA thiolase MRKTVIVSAARTPFGKFGGVLKEVKAAELGGIVMKEALQQAGVSGDDVEGNVMGMVVQAGSGQIPSRQAARLAGMPWSVPSETLNKVCASGLRAVTLCDQMIRAQDADILVAGGMESMSNIPYAVPAGRWGARMGDGELRDLMVYDGLTCAFDEVHMAVHGNTAAKEYAISRREQDEWALRSHARAAKAADEGKFQDEIVPVNWIGRKGKPNVVDKDEAIRRDTSLDQLAKLAPIYASDGSITAGNAPGVNDGAGAFVLMSEEKAAELGKRPLATILGFSTTGMPAHELAAAPGFAINKLLKKNGLTVQDIDLFEVNEAFASVVLTCEKIVGFDLEKVNVNGGAIALGHPIGASGARILMTLVYELKRRGGGLGVAAICSGAAQGDAVLVQVH atoB curated2 P66927 Probable acetyl-CoA acetyltransferase; EC 2.3.1.9; Acetoacetyl-CoA thiolase MIVAGARTPIGKLMGSLKDFSASELGAIAIKGALEKANVPASLVEYVIMGQVLTAGAGQMPARQAAVAAGIGWDVPALTINKMCLSGIDAIALADQLIRAREFDVVVAGGQESMTKAPHLLMNSRSGYKYGDVTVLDHMAYDGLHDVFTDQPMGALTEQRNDVDMFTRSEQDEYAAASHQKAAAAWKDGVFADEVIPVNIPQRTGDPLQFTEDEGIRANTTAAALAGLKPAFRGDGTITAGSASQISDGAAAVVVMNQEKAQELGLTWLAEIGAHGVVAGPDSTLQSQPANAINKALDREGISVDQLDVVEINEAFAAVALASIRELGLNPQIVNVNGGAIAVGHPLGMSGTRITLHAALQLARRGSGVGVAALCGAGGQGDALILRAG atoB curated2 P73825 Acetyl-CoA acetyltransferase; EC 2.3.1.9; Beta-ketothiolase PhaA MRDVFIVAAKRTPLGRFGGSLTNFSAADLGAHVMKSVLAQAGVGGDQLDLYIMGNVLRAGHGQLIPRQAALKAEIPDTVDGYAVDMVCSSAMMSVINAALTIRAGEGDLILAGGTESMSQTGFYLSHRARWGYKFLMGAPENLTDLLLHDGLTDSTNGEGMGEQTEKLAAEHGFSRIELDEVACLSQQRAAHATESGYFDSEIAPIEITSRKGTQVLASDEGIRSDTTVESLGKLRSAFAKDGVLTAGNCSQITDGAAALLLASGEAVEKYQLKPLAKILGGSWAAGTPSRFPELPITASQKLLAKLDKTLADFDLFENNEAFSVSNLLFERRLGVDRDKLNVNGGAIALGHPIGASGARIMVTLLYALQQRDKTLGLAALCHGTGGGTAIALERV atoB curated2 Q0KBP1 Beta-ketothiolase BktB; EC 2.3.1.16; EC 2.3.1.9; Acetyl-CoA acetyltransferase; Acetyl-CoA acyltransferase MTREVVVVSGVRTAIGTFGGSLKDVAPAELGALVVREALARAQVSGDDVGHVVFGNVIQTEPRDMYLGRVAAVNGGVTINAPALTVNRLCGSGLQAIVSAAQTILLGDTDVAIGGGAESMSRAPYLAPAARWGARMGDAGLVDMMLGALHDPFHRIHMGVTAENVAKEYDISRAQQDEAALESHRRASAAIKAGYFKDQIVPVVSKGRKGDVTFDTDEHVRHDATIDDMTKLRPVFVKENGTVTAGNASGLNDAAAAVVMMERAEAERRGLKPLARLVSYGHAGVDPKAMGIGPVPATKIALERAGLQVSDLDVIEANEAFAAQACAVTKALGLDPAKVNPNGSGISLGHPIGATGALITVKALHELNRVQGRYALVTMCIGGGQGIAAIFERI atoB curated2 Q5HIU0 Probable acetyl-CoA acyltransferase; EC 2.3.1.9; Acetoacetyl-CoA thiolase MTRVVLAAAYRTPIGVFGGAFKDVPAYDLGATLIEHIIKETGLNPSEIDEVIIGNVLQAGQGQNPARIAAMKGGLPETVPAFTVNKVCGSGLKSIQLAYQSIVTGENDIVLAGGMENMSQSPMLVNNSRFGFKMGHQSMVDSMVYDGLTDVFNQYHMGITAENLAEQYGISREEQDTFAVNSQQKAVRAQQNGEFDSEIVPVSIPQRKGEPIVVTKDEGVRENVSVEKLSRLRPAFKKDGTVTAGNASGINDGAAMMLVMSEDKAKELNIEPLAVLDGFGSHGVDPSIMGIAPVGAVEKALKRSKKELSDIDVFELNEAFAAQSLAVDRELKLPPEKVNVKGGAIALGHPIGASGARVLVTLLHQLNDEVETGLTSLCIGGGQAIAAVVSKYK atoB ignore BRENDA::B8YJJ0 acetyl-CoA C-acyltransferase (EC 2.3.1.16) MALTAAWHKYDAIVSRFVFDGLRRVGLQEIQGHPSVITAHLPFIASPTPQVTFVLAYLLIVVCGVAALRTRKSSAPREDPAWLRLLVQAHNLVLISLSAYMSSAACYYAWKYGYRFWGTNYSPKERDMGGLIYTFYVSKLYEFVDTLIMLLKGKVEQVSFLHVYHHASISTIWWAIAYVAPGGDAWYCCFLNSLVHVLMYTYYLLATLLGKDAKARRKYLWWGRYLTQFQMFQFVTMMLEAAYTWAYSPYPKFLSKLLFFYMITLLALFANFYAQKHGSSRAAKQKLQ atoB ignore BRENDA::I3R3D0 acetyl-CoA C-acetyltransferase (subunit 1/2) (EC 2.3.1.9) MSDDTPAMEAYRYPDGSITYPGHPVGPGGEEPVGTVDLSGYTATVLTWTTSTATPPGVRQPNTLAIVEFDVDGEPARAIGQVTTEDVDIGDEVEPVYCEELREPGAGIREPESQEWDGYRFEPV atoB ignore BRENDA::I3RA71 acetyl-CoA C-acetyltransferase (subunit 1/2) (EC 2.3.1.9) MTLEAGKCPNGHVSYPTHPRCRKCGEPQTETLDLSDRTGKVVTWTHSTATPPGVRQPNTMAIVEFEVDGQAVRALGQVTTDDIETGDVVEPVYVEELRDPEVGIKAPESQSWDGYRWDPV atoB ignore BRENDA::P07256,SwissProt::P07256 acetyl-CoA C-acetyltransferase (EC 2.3.1.9);; Cytochrome b-c1 complex subunit 1, mitochondrial; Complex III subunit 1; Core protein I; Ubiquinol-cytochrome c oxidoreductase core protein 1; Ubiquinol-cytochrome c reductase 44 kDa protein MLRTVTSKTVSNQFKRSLATAVATPKAEVTQLSNGIVVATEHNPSAHTASVGVVFGSGAANENPYNNGVSNLWKNIFLSKENSAVAAKEGLALSSNISRDFQSYIVSSLPGSTDKSLDFLNQSFIQQKANLLSSSNFEATKKSVLKQVQDFEENDHPNRVLEHLHSTAFQNTPLSLPTRGTLESLENLVVADLESFANNHFLNSNAVVVGTGNIKHEDLVNSIESKNLSLQTGTKPVLKKKAAFLGSEVRLRDDTLPKAWISLAVEGEPVNSPNYFVAKLAAQIFGSYNAFEPASRLQGIKLLDNIQEYQLCDNFNHFSLSYKDSGLWGFSTATRNVTMIDDLIHFTLKQWNRLTISVTDTEVERAKSLLKLQLGQLYESGNPVNDANLLGAEVLIKGSKLSLGEAFKKIDAITVKDVKAWAGKRLWDQDIAIAGTGQIEGLLDYMRIRSDMSMMRW atoB ignore BRENDA::P22307,SwissProt::P22307,metacyc::HS03991-MONOMER propanoyl-CoA C-acyltransferase (EC 2.3.1.176);; Non-specific lipid-transfer protein; NSL-TP; Propanoyl-CoA C-acyltransferase; SCP-chi; SCPX; Sterol carrier protein 2; SCP-2; Sterol carrier protein X; SCP-X; EC 2.3.1.176;; Non-specific lipid-transfer protein (EC 2.3.1.16) MSSSPWEPATLRRVFVVGVGMTKFVKPGAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVFGDSTCGQRAIYHSLGMTGIPIINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKGSLGIKFSDRTIPTDKHVDLLINKYGLSAHPVAPQMFGYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYGLQSKAVEILAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGIGGAVVVTLYKMGFPEAASSFRTHQIEAVPTSSASDGFKANLVFKEIEKKLEEEGEQFVKKIGGIFAFKVKDGPGGKEATWVVDVKNGKGSVLPNSDKKADCTITMADSDFLALMTGKMNPQSAFFQGKLKITGNMGLAMKLQNLQLQPGNAKL atoB ignore BRENDA::P28790 acetyl-CoA C-acyltransferase (EC 2.3.1.16) MSLNPRDVVIVDFGRTPMGRSKGGMHRNTRAEDMSAHLISKVLERNSKVDPGEVEDVIWGCVNQTLEQGWNIARMASLMTQIPHTSAAQTVSRLCGSSMSALHTAAQAIMTGNGDVFVVGGVEHMGHVSMMHGVDPNPHMSLYAAKASGMMGLTAEMLGKMHGISREQQDAFAVRSHQLAHKATVEGKFKDEIIPMQGYDENGFLKIFDYDETIRPDTTLESLAALKPAFNPKGGTVTAGTSSQITDGASCMIVMSAQRAKDLGLEPLAVIRSMAVAGVDPAIMGYGPVPATQKALKRAGLNMADIDFIELNEAFAAQALPVLKDLKVLDKMNEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTFGLSTMCIGLGQGIATVFERV atoB ignore BRENDA::Q22100,SwissProt::Q22100 acetyl-CoA C-acyltransferase (EC 2.3.1.16);; Acetyl-CoA acetyltransferase homolog, mitochondrial; 3-ketoacyl-CoA thiolase; EC 2.3.1.- MLSSSGHAIRRGITTSAALSNKHAFIVGAARTPIGSFRSSLSSVTAPELASVAIKAALERGAVKPSSIQEVFLGQVCQANAGQAPARQAALGAGLDLSVAVTTVNKVCSSGLKAIILAAQQIQTGHQDFAIGGGMESMSQVPFYVQRGEIPYGGFQVIDGIVKDGLTDAYDKVHMGNCGEKTSKEMGITRKDQDEYAINSYKKSAKAWENGNIGPEVVPVNVKSKKGVTIVDKDEEFTKVNFDKFTSLRTVFQKDGTITAANASTLNDGAAAVIVASQEAVSEQSLKPLARILAYGDAATHPLDFAVAPTLMFPKILERAGVKQSDVAQWEVNEAFSCVPLAFIKKLGVDPSLVNPHGGAVSIGHPIGMSGARLITHLVHTLKSGQIGVAAICNGGGGSSGMVIQKL atoB ignore BRENDA::Q56WD9,SwissProt::Q56WD9,metacyc::AT2G33150-MONOMER acetyl-CoA C-acyltransferase (EC 2.3.1.16);; 3-ketoacyl-CoA thiolase 2, peroxisomal; Acetyl-CoA acyltransferase 2; Beta-ketothiolase 2; Peroxisomal 3-oxoacyl-CoA thiolase 2; Peroxisome defective protein 1; EC 2.3.1.16;; 3-ketoacyl-CoA thiolase 2, peroxisomal (EC 2.3.1.16) MEKAIERQRVLLEHLRPSSSSSHNYEASLSASACLAGDSAAYQRTSLYGDDVVIVAAHRTPLCKSKRGNFKDTYPDDLLAPVLRALIEKTNLNPSEVGDIVVGTVLAPGSQRASECRMAAFYAGFPETVAVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGLESMTTNPMAWEGSVNPAVKKFAQAQNCLLPMGVTSENVAQRFGVSRQEQDQAAVDSHRKAAAATAAGKFKDEIIPVKTKLVDPKTGDEKPITVSVDDGIRPTTTLASLGKLKPVFKKDGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPVLGVFRTFAAVGVDPAIMGIGPAVAIPAAVKAAGLELDDIDLFEINEAFASQFVYCRNKLGLDPEKINVNGGAMAIGHPLGATGARCVATLLHEMKRRGKDCRFGVVSMCIGTGMGAAAVFERGDGVDELRNARKVEAQGLLSKDAR atoB ignore BRENDA::Q64428,SwissProt::Q64428 long-chain-3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.211); acetyl-CoA C-acyltransferase (EC 2.3.1.16);; Trifunctional enzyme subunit alpha, mitochondrial; Monolysocardiolipin acyltransferase; TP-alpha; EC 2.3.1.-; EC 4.2.1.17; EC 1.1.1.211 MVASRAIGSLSRFSAFRILRSRGCICHSFTTSSALLSRTHINYGVKGDVAVIRINSPNSKVNTLNKEVQSEFVEVMNEIWANDQIRSAVLISSKPGCFVAGADINMLASCTTPQEAARISQEGQKMFEKLEKSPKPVVAAISGSCLGGGLELAIACQYRIATKDRKTVLGVPEVLLGILPGAGGTQRLPKMVGVPAAFDMMLTGRNIRADRAKKMGLVDQLVDPLGPGIKSPEERTIEYLEEVAVNFAKGLADRKVSAKQSKGLMEKLTSYAMTIPFVRQQVYKTVEEKVKKQTKGLYPAPLKIIDAVKTGLEQGNDAGYLAESEKFGELALTKESKALMGLYNGQVLCKKNKFGAPQKTVQQLAILGAGLMGAGIAQVSVDKGLKTLLKDTTVTGLGRGQQQVFKGLNDKVKKKALTSFERDSIFSNLIGQLDYKGFEKADMVIEAVFEDLAVKHKVLKEVESVTPEHCIFASNTSALPINQIAAVSQRPEKVIGMHYFSPVDKMQLLEIITTDKTSKDTTASAVAVGLKQGKVIIVVKDGPGFYTTRCLAPMMSEVIRILQEGVDPKKLDALTTGFGFPVGAATLADEVGIDVAQHVAEDLGKAFGERFGGGSVELLKLMVSKGFLGRKSGKGFYIYQSGSKNKNLNSEIDNILVNLRLPAKPEVSSDEDIQYRVITRFVNEAVLCLQEGILATPEEGDIGAVFGLGFPPCLGGPFRFVDLYGAQKVVDRLRKYESAYGTQFTPCQLLRDLANNSSKKFYQ atoB ignore BRENDA::Q66Q58 acetyl-CoA C-acyltransferase (EC 2.3.1.16) MPRKVFVVGVGMTNFIKPSTGPDYPELGKEAVLAALADARIKYTDIQQAVCGYVFGDSTCGQRVLYQVGMTGIPIFNVNNNCSTGSNALYLAKKLIEGGVSDVMLAVGFEKMAPGALAAGVFNDRTNPLDKHTLKMAELAELTGAPMTAQYFGNAAAEHMKKYGTTELHLAKIAAKNHRHGAKNPRAQGKREYTVEEVLNSRRIYGPLTKLECCPTSDGAGAAVLMSEEAVIRYGLQAKAVEIIGMEMATDTPAVFEENSLMKVAGYDMTALAAKRLYQNTGVSPKQVDVVELHDCFAANEMITYEGLQLCGEGEAGKFIDAGDNTYGGRVVVNPSGGLIAKGHPLGATGLAQCAELVWQLRGEAGNRQVPRAKIALQHNLGLGGAVVVTMYRKGFADIAPNAVAVAGNPEDFKVYKYMKILEEAMANDTDNLIEKVRGIYGFKVKNGPNGAEGYWVINAKEGKGKVTYNSSEKPEVTFTVSDEDVVDLISGKLNPQKAFFQGKIKIQGNMGLAMKLTDLQRQAAGKIDTIRSKL atoB ignore BRENDA::Q6W6X6 acetyl-CoA C-acyltransferase (EC 2.3.1.16) MERAIERQRVLLEHLRPSSTSSSLENLSVSVCAAGDSAAYQRNSVFGDDVVIVAAYRSPLCKAKRGGLKDTYPDDILAPVLKALIEKTNINPAEVGDIVVGSVLGAGSQRASECRMAAFYAGFPETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGLESMTANPMAWEGSVNPKVKTMAQAQDCLLPMGITSENVAQKFSITRQEQDQAAVGSHRKAAAATAAGRFKDEIIPIKTKIVDPKTGDEKPVTISVDDGIRPGTSLADLAKLKPVFRKDGSTTAGTSSQVSDGAGAVLLMKRSIALQKGLPILGVFRTFAAVGVPPSIMGIGPAVAIPAAVKAAGLQIDDIDLFEINEAFASQFVYCQKKLEIDPQKINVNGGAMAIGHPLGATGARCVATLLHEMKRRGRDCRFGVVSMCIGTGMGAAAVFERGDACDELCNAKAK atoB ignore BRENDA::Q921H8,SwissProt::Q921H8 acetyl-CoA C-acyltransferase (EC 2.3.1.16);; 3-ketoacyl-CoA thiolase A, peroxisomal; Acetyl-CoA acyltransferase A; Beta-ketothiolase A; Peroxisomal 3-oxoacyl-CoA thiolase A; EC 2.3.1.16 MHRLQVVLGHLAGRPESSSALQAAPCSARFPQASASDVVVVHGRRTPIGRASRGGFKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVLEPGAGAVMARIAQFLSGIPETVPLSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMGNPGNISSRLLESEKARDCLTPMGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTTVLDDKGDKKTITVSQDEGVRPSTTMQGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRAYGVVSMCIGTGMGAAAVFEYPGN atoB ignore BRENDA::Q9H5J4,SwissProt::Q9H5J4,metacyc::HS10142-MONOMER acetyl-CoA C-acyltransferase (EC 2.3.1.16); very-long-chain 3-oxoacyl-CoA synthase (EC 2.3.1.199);; Elongation of very long chain fatty acids protein 6; 3-keto acyl-CoA synthase ELOVL6; ELOVL fatty acid elongase 6; ELOVL FA elongase 6; Fatty acid elongase 2; hELO2; Fatty acyl-CoA elongase; Long-chain fatty-acyl elongase; Very long chain 3-ketoacyl-CoA synthase 6; Very long chain 3-oxoacyl-CoA synthase 6; EC 2.3.1.199;; long chain fatty acid elongase 6 (EC 2.3.1.199) MNMSVLTLQEYEFEKQFNENEAIQWMQENWKKSFLFSALYAAFIFGGRHLMNKRAKFELRKPLVLWSLTLAVFSIFGALRTGAYMVYILMTKGLKQSVCDQGFYNGPVSKFWAYAFVLSKAPELGDTIFIILRKQKLIFLHWYHHITVLLYSWYSYKDMVAGGGWFMTMNYGVHAVMYSYYALRAAGFRVSRKFAMFITLSQITQMLMGCVVNYLVFCWMQHDQCHSHFQNIFWSSLMYLSYLVLFCHFFFEAYIGKMRKTTKAE atoB ignore CharProtDB::CH_123484 protein similar to acetyl-CoA acetyltransferase MVPPVYIVSTARTPIGSFQGTLSSLTYSDLGAHAVKAALNKVPQIKPEDVDEIVFGGVLQANVGQAPARQVALKAGLTDKIVASTVNKVCASGLKAIIIGAQNIICGTSDIVVVGGAESMTNTPYYLPTARNGARFGDSTLIDGIQKDGLLDVYEQKLMGVAAEKCAADHGFTREQQDEFAIKSYQKAGNALKQGKFNQEIAPVTIKGVRGKPDVVVEKDEEIEKFNEAKLKSARAVFQKENGTVTGPNASKINDGAAALILVSEAKLKELGLKPLAKINGWGEAARNPIDFTIAPALAVPKAVKHAGLTLDQVDFFELNEAFSVVGLANAEICQIPLEKLNAYGGAVALGHPLGCSGARIVVTLLSVLIQEGGKIGCAGVCNGGGGASSIVIEKVDSDFKL atoB ignore SwissProt::I6XHI4,metacyc::G185E-7823-MONOMER Steroid 3-ketoacyl-CoA thiolase; Acetyl-CoA acetyltransferase FadA5; Beta-ketoacyl-CoA thiolase; EC 2.3.1.16;; steroid 3-ketoacyl-CoA thiolase monomer (EC 2.3.1.16; EC 2.3.1.176) MGYPVIVEATRSPIGKRNGWLSGLHATELLGAVQKAVVDKAGIQSGLHAGDVEQVIGGCVTQFGEQSNNISRVAWLTAGLPEHVGATTVDCQCGSGQQANHLIAGLIAAGAIDVGIACGIEAMSRVGLGANAGPDRSLIRAQSWDIDLPNQFEAAERIAKRRGITREDVDVFGLESQRRAQRAWAEGRFDREISPIQAPVLDEQNQPTGERRLVFRDQGLRETTMAGLGELKPVLEGGIHTAGTSSQISDGAAAVLWMDEAVARAHGLTPRARIVAQALVGAEPYYHLDGPVQSTAKVLEKAGMKIGDIDIVEINEAFASVVLSWARVHEPDMDRVNVNGGAIALGHPVGCTGSRLITTALHELERTDQSLALITMCAGGALSTGTIIERI atoB ignore SwissProt::O32177 3-ketoacyl-CoA thiolase; Acetyl-CoA acyltransferase; Beta-ketothiolase; EC 2.3.1.16 MKEAVIVSGARTPVGKAKKGSLATVRPDDLGAICVKETLKRAGGYEGNIDDLIIGCATPEAEQGLNMARNIGALAGLPYTVPAITVNRYCSSGLQSIAYAAEKIMLGAYDTAIAGGAESMSQVPMMGHVTRPNLALAEKAPEYYMSMGHTAEQVAKKYGVSREDQDAFAVRSHQNAAKALAEGKFKDEIVPVEVTVTEIGEDHKPMEKQFVFSQDEGVRPQTTADILSTLRPAFSVDGTVTAGNSSQTSDGAAAVMLMDREKADALGLAPLVKFRSFAVGGVPPEVMGIGPVEAIPRALKLAGLQLQDIGLFELNEAFASQAIQVIRELGIDEEKVNVNGGAIALGHPLGCTGTKLTLSLIHEMKRRNEQFGVVTMCIGGGMGAAGVFELC atoB ignore SwissProt::P09110,metacyc::HS00752-MONOMER 3-ketoacyl-CoA thiolase, peroxisomal; Acetyl-CoA acyltransferase; Beta-ketothiolase; Peroxisomal 3-oxoacyl-CoA thiolase; EC 2.3.1.16;; 3-ketoacyl-CoA thiolase, peroxisomal (EC 2.3.1.223; EC 2.3.1.16) MQRLQVVLGHLRGPADSGWMPQAAPCLSGAPQASAADVVVVHGRRTAICRAGRGGFKDTTPDELLSAVMTAVLKDVNLRPEQLGDICVGNVLQPGAGAIMARIAQFLSDIPETVPLSTVNRQCSSGLQAVASIAGGIRNGSYDIGMACGVESMSLADRGNPGNITSRLMEKEKARDCLIPMGITSENVAERFGISREKQDTFALASQQKAARAQSKGCFQAEIVPVTTTVHDDKGTKRSITVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAGNSSQVSDGAAAILLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVALGHPLGCTGARQVITLLNELKRRGKRAYGVVSMCIGTGMGAAAVFEYPGN atoB ignore SwissProt::P21151,ecocyc::FADA-MONOMER,metacyc::FADA-MONOMER 3-ketoacyl-CoA thiolase FadA; Acetyl-CoA acyltransferase; Beta-ketothiolase; Fatty acid oxidation complex subunit beta; EC 2.3.1.16;; 3-ketoacyl-CoA thiolase (EC 2.3.1.16);; 3-ketoacyl-CoA thiolase (EC 2.3.1.16) MEQVVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLARNPALEAAALDDIYWGCVQQTLEQGFNIARNAALLAEVPHSVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHGVDFHPGLSRNVAKAAGMMGLTAEMLARMHGISREMQDAFAARSHARAWAATQSAAFKNEIIPTGGHDADGVLKQFNYDEVIRPETTVEALATLRPAFDPVNGMVTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSASDIGVFEMNEAFAAQILPCIKDLGLIEQIDEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIATVFERV atoB ignore SwissProt::P27796 3-ketoacyl-CoA thiolase, peroxisomal; Acetyl-CoA acyltransferase; Beta-ketothiolase; Peroxisomal 3-oxoacyl-CoA thiolase; EC 2.3.1.16 MSQRLQSIKDHLVESAMGKGESKRKNSLLEKRPEDVVIVAANRSAIGKGFKGAFKDVNTDYLLYNFLNEFIGRFPEPLRADLNLIEEVACGNVLNVGAGATEHRAACLASGIPYSTPFVALNRQCSSGLTAVNDIANKIKVGQIDIGLALGVESMTNNYKNVNPLGMISSEELQKNREAKKCLIPMGITNENVAANFKISRKDQDEFAANSYQKAYKAKNEGLFEDEILPIKLPDGSICQSDEGPRPNVTAESLSSIRPAFIKDRGTTTAGNASQVSDGVAGVLLARRSVANQLNLPVLGRYIDFQTVGVPPEIMGVGPAYAIPKVLEATGLQVQDIDIFEINEAFAAQALYCIHKLGIDLNKVNPRGGAIALGHPLGCTGARQVATILRELKKDQIGVVSMCIGTGMGAAAIFIKE atoB ignore SwissProt::P55084 Trifunctional enzyme subunit beta, mitochondrial; TP-beta; EC 2.3.1.155; EC 2.3.1.16 MTILTYPFKNLPTASKWALRFSIRPLSCSSQLRAAPAVQTKTKKTLAKPNIRNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKLMLDLNKAKSMGQRLSLISKFRFNFLAPELPAVSEFSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSDVVPFKVPGKDTVTKDNGIRPSSLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAENYMGRKTKVGLPPLEKFNNWGGSLSLGHPFGATGCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEAYPK atoB ignore SwissProt::P76503,ecocyc::G7213-MONOMER,metacyc::G7213-MONOMER 3-ketoacyl-CoA thiolase FadI; ACSs; Acetyl-CoA acyltransferase; Acyl-CoA ligase; Beta-ketothiolase; Fatty acid oxidation complex subunit beta; EC 2.3.1.16;; 3-ketoacyl-CoA thiolase FadI (EC 2.3.1.16);; 3-ketoacyl-CoA thiolase FadI (EC 2.3.1.16) MGQVLPLVTRQGDRIAIVSGLRTPFARQATAFHGIPAVDLGKMVVGELLARSEIPAEVIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYSVSRACATSFQAVANVAESLMAGTIRAGIAGGADSSSVLPIGVSKKLARVLVDVNKARTMSQRLKLFSRLRLRDLMPVPPAVAEYSTGLRMGDTAEQMAKTYGITREQQDALAHRSHQRAAQAWSDGKLKEEVMTAFIPPYKQPLVEDNNIRGNSSLADYAKLRPAFDRKHGTVTAANSTPLTDGAAAVILMTESRAKELGLVPLGYLRSYAFTAIDVWQDMLLGPAWSTPLALERAGLTMSDLTLIDMHEAFAAQTLANIQLLGSERFAREALGRAHATGEVDDSKFNVLGGSIAYGHPFAATGARMITQTLHELRRRGGGFGLVTACAAGGLGAAMVLEAE atoB ignore SwissProt::Q570C8 3-ketoacyl-CoA thiolase 5, peroxisomal; Acetyl-CoA acyltransferase 5; Beta-ketothiolase 5; Peroxisomal 3-oxoacyl-CoA thiolase 5; EC 2.3.1.16 MERAMERQKILLRHLNPVSSSNSSLKHEPSLLSPVNCVSEVSPMAAFGDDIVIVAAYRTAICKARRGGFKDTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAMECRVAAYFAGFPDSVPVRTVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMSTDHIPGGGFHGSNPRAQDFPKARDCLLPMGITSENVAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVATKIVDPETKAEKAIVVSVDDGVRPNSNMADLAKLKTVFKQNGSTTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLAGLNVSDIDLFEINEAFASQYVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRGKDCRFGVISMCIGTGMGAAAVFERGDSVDNLSNARVANGDSH atoB ignore SwissProt::Q60587 Trifunctional enzyme subunit beta, mitochondrial; TP-beta; EC 2.3.1.155; EC 2.3.1.16 MTTILTSTFRNLSTTSKWALRFSVRPLSCSSQVQSAPAVQTKSKKTLAKPNLKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRKMMLDLNKAKTLAQRLSLLTKFRLNFLSPELPAVAEFSTNETMGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSDIVPFKVPGKDTVSKDNGIRPSSLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAQNYMGRKTKVGAPPLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGGQYALVAACAAGGQGHAMIVEAYPK atoB ignore SwissProt::Q8LF48 3-ketoacyl-CoA thiolase 1, peroxisomal; Acetyl-CoA acyltransferase 1; Beta-ketothiolase 1; Peroxisomal 3-oxoacyl-CoA thiolase 1; EC 2.3.1.16 MEKATERQRILLRHLQPSSSSDASLSASACLSKDSAAYQYGDDVVIVAAQRTALCKAKRGSFKDTFPDELLASVLRALIEKTNVNPSEVGDIVVGTVLGPGSQRASECRMAAFYAGFPETVPIRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGLESMTTNPRGWKGSVNPNVKKFEQAHNCLLPMGITSENVAHRFNVSREEQDQAAVDSHRKAASATASGKFKDEITPVKTKIVDPKTGDEKPITVSVDDGIRPNTTLSGLAKLKPVFKEDGTTTAGNSSQLSDGAGAVLLMRRNVAMQKGLPILGVFRTFSAVGVDPAIMGVGPAVAIPAAVKAAGLELNDVDLFEINEAFASQFVYCRNKLGLDAEKINVNGGAIAIGHPLGATGARCVATLLHEMKRRGKDCRFGVVSMCIGSGMGAAAVFERGGGVDELCDVRKV atoB ignore SwissProt::Q8SVA6 3-ketoacyl-CoA thiolase, peroxisomal; Acetyl-CoA acyltransferase; Beta-ketothiolase; Peroxisomal 3-oxoacyl-CoA thiolase; EC 2.3.1.16 MISHEDVVVVGALRTPIGRATRGKLRSLRNDELVTAAIRGIIEKTGIDPRLIEEVILGHCLSSMEGNVAARMGVLRAGVPVETPVMIINRLCGSGLESVGLIAEKIRSGRIEIGLAGGFESMTSYGLPKEYTLSRGGACEDAEDCMLTLGEVSEMLGKTHGVTRSEADEYAVTSQKRALEATKKGHFLAEIIPMRVGDETVERDEGIRETSLGTIESLKPVFRQDGVCTSANSSQLSDGASAVLLMKRRRADELGLPVVAEFIDFIAVGLKPRDMGLGPVVAIEKLLKRNGLEKDQISYFEINEAFASQVLCCLRKLQIGEDRVNRYGGSIALGHPIGASGARIVCTLLSVMKNEALEGYGVASLCVGAGHGVAALFRRAAGSKPQDIKNT atoB ignore metacyc::G185E-7833-MONOMER 3-oxo-acyl CoA thiolase (EC 2.3.1.16) MTEAYVIDAVRTAVGKRGGALAGIHPVDLGALAWRGLLDRTDIDPAAVDDVIAGCVDAIGGQAGNIARLSWLAAGYPEEVPGVTVDRQCGSSQQAISFGAQAIMSGTADVIVAGGVQNMSQIPISSAMTVGEQFGFTSPTNESKQWLHRYGDQEISQFRGSELIAEKWNLSREEMERYSLTSHERAFAAIRAGHFENEIITVETESGPFRVDEGPRESSLEKMAGLQPLVEGGRLTAAMASQISDGASAVLLASERAVKDHGLRPRARIHHISARAADPVFMLTGPIPATRYALDKTGLAIDDIDTVEINEAFAPVVMAWLKEIKADPAKVNPNGGAIALGHPLGATGAKLFTTMLGELERIGGRYGLQTMCEGGGTANVTIIERL atoB ignore metacyc::G1G01-2278-MONOMER FadA (EC 2.3.1.16) MSLNPRDVVIVDFGRTPMGRSKGGMHRNTRAEDMSAHLISKLLERNGKVDPKEVEDVIWGCVNQTLEQGWNIARMASLMTPIPHTSAAQTVSRLCGSSMSALHTAAQAIMTGNGDVFVVGGVEHMGHVSMMHGVDPNPHLSLHAAKASGMMGLTAEMLGKMHGITREQQDLFGLRSHQLAHKATVEGKFKDEIIPMQGYDENGFLKVFDFDETIRPETTLEGLASLKPAFNPKGGTVTAGTSSQITDGASCMIVMSGQRAMDLGIQPLAVIRSMAVAGVDPAIMGYGPVPSTQKALKRAGLTMADIDFIELNEAFAAQALPVLKDLKVLDKMDEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVATMCVGLGQGITTVFERV atoB ignore metacyc::MONOMER-13468 acetyl-CoA acetyltransferase (EC 2.3.1.16) MREVVIVSAVRTAIGSFGGTLKDVSAVDLGAIVIKEAVKRAGIKPEQVDEVIFGNVIQAGVGQSLARQSAVYAGLPVEVPAFTVNKLCGSGLRTVSLAASLISNGDADTIVVGGSENMSASPYLIPKARFGYRMGEAKIYDAMLHDGLIDSFNNYHMGITAENIAEKWGITREDQDKFALASQQKAEAAIKAGKFKDEIVPVTVKMKKKEVVFDTDEDPRFGTTIETLAKLKPAFKRDGTGTVTAGNSSGINDSSAALILMSADKAKELGVKPMAKYVDFASAGLDPAIMGYGPYYATKKVLAKTNLTIKDFDLIEANEAFAAQSIAVARDLEFDMSKVNVNGGAIALGHPVGCSGARILVTLLHEMQKRDAKKGLATLCIGGGQGTAVVVER atoB ignore metacyc::MONOMER-13585 acetyl-CoA acetyltransferase (EC 2.3.1.16) MTNVVIVSAARTAVGSFNGAFASTPAHDLGAAVIEAVVARAGIDKADVSETILGQVLTAGQGQNPARQAHIKAGLPQESAAWSINQVCGSGLRAVALAAQHVQLGDASIVVAGGQENMSLSPHVAHLRAGQKMGDLSFIDSMIKDGLWDAFNGYHMGQTAENVAAKWQISRDMQDEFAVASQNKAEAAQKAGRFADEIVPFVIKTRKGDVTVDADEYIRHGATLDAMAKLRPAFIKDGTVTAANASGINDGAAAVLVMSAEEAEKRGLSPLARIASYATAGLDPSIMGVGPIHASRKALEKAGWKVGDLDLVEANEAFAAQACAVNKDMGWDPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMQRRNAKKGLATLCIGGGMGVAMCLERP atoB ignore metacyc::MONOMER-14375 3-oxoacyl CoA thiolase (EC 2.3.1.16) MSAHVQVIGVGMVKFVKPGAHEPYEIMASKAIRAALADAGISYDKIQQAYASYVFGDSACGQAALYRVGMTGIPLFNVNNNCSSGSSALFLARQAVLSGSVDCALAFGFEEMRPGALGAVWNDRTSPLLEMEDQLEKIVPGLPSASNAHRLFGSAALAYIEKTDANPNIFAKVAVKTRKHAMNNPLAIFNQPLTVEEVMQSPVIFAPYLTRLEACPPSCGAAAAIVCSEKFARRHGLARGINILAQAMTTDRPARNDNPIDLAGADMTRNAAAQVYAQAGIGPEDIDVVELHDCFTSNEVITYEGLGLCGDGEAEKFIAAGDNTYGGKYVINPSGGLMSKGHPLGATGLAQCTELVSQLRGGAGARQVSGARLALQHNLGLGGACVVTLYGKSA atoB ignore metacyc::MONOMER-17590 fatty acid oxidation complex β subunit (EC 2.3.1.16) MSLNPRDVVIVDFGRTPMGRSKGGMHRNTRAETMSAHLISKLLERNPKVDPAEVEDVIWGCVNQTLEQGWNIARMASLMTQIPHTSAAQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVGMMHGVDPNPHLSLYAAKASGMMGLTAEMLGKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIIPMEGYDENGFLKVFDFDETIRPETTVETLAELKPAFNPKGGTVTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALKRAGLTIADIDFVELNEAFAAQALPVLKDLKLLDKMDEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMCVGLGQGITTVFERI atoB ignore metacyc::MONOMER-18244 acetyl-CoA acetyltransferase/HMG-CoA reductase (EC 1.1.1.34; EC 2.3.1.16) MKTVVIIDALRTPIGKYKGSLSQVSAVDLGTHVTTQLLKRHSTISEEIDQVIFGNVLQAGNGQNPARQIAINSGLSHEIPAMTVNEVCGSGMKAVILAKQLIQLGEAEVLIAGGIENMSQAPKLQRFNYETESYDAPFSSMMYDGLTDAFSGQAMGLTAENVAEKYHVTREEQDQFSVHSQLKAAQAQAEGIFADEIAPLEVSGTLVEKDEGIRPNSSVEKLGTLKTVFKEDGTVTAGNASTINDGASALIIASQEYAEAHGLPYLAIIRDSVEVGIDPAYMGISPIKAIQKLLARNQLTTEEIDLYEINEAFAATSIVVQRELALPEEKVNIYGGGISLGHAIGATGARLLTSLSYQLNQKEKKYGVASLCIGGGLGLAMLLERPQQKKNSRFYQMSPEERLASLLNEGQISADTKKEFENTALSSQIANHMIENQISETEVPMGVGLHLTVDETDYLVPMATEEPSVIAALSNGAKIAQGFKTVNQQRLMRGQIVFYDVADAESLIDELQVRETEIFQQAELSYPSIVKRGGGLRDLQYRAFDESFVSVDFLVDVKDAMGANIVNAMLEGVAELFREWFAEQKILFSILSNYATESVVTMKTAIPVSRLSKGSNGREIAEKIVLASRYASLDPYRAVTHNKGIMNGIEAVVLATGNDTRAVSASCHAFAVKEGRYQGLTSWTLDGEQLIGEISVPLALATVGGATKVLPKSQAAADLLAVTDAKELSRVVAAVGLAQNLAALRALVSEGIQKGHMALQARSLAMTVGATGKEVEAVAQQLKRQKTMNQDRALAILNDLRKQ atoB ignore metacyc::MONOMER-19852 acetyl-CoA C-acetyltransferase (EC 2.3.1.16) MSTDDPVVIVSAARTPIGGLLGDLAALAAWELGAVAIRAAVERAGVPGDAVDEVLMGNCLMAGQGQAPARQAARKAGLPDSAGAVTLSKMCGSGMRALMFGHDMLAAGSAEVVVAGGMESMTNAPHLSFVRKGLKYGAAVLYDHMALDGLEDAYERGKSMGVFAEQCVSYYSFRREAMDAFAVASTQRAIAAHNDGSFDWEIAPVTLAGRAGDVTVDRDEQPFKAKLDKITALKPAFGKDGTITAATSSSISDGAAALVLMRASTARARGLAPIAVLRAHAVHAQAPAWFSTAPAGAIRKVLQKTGWSVRDVDLWEINEAFAAVTMAAMTDFELPHERVNVHGGACALGHPIGASGARIVVTLLGALQRRGLRRGVAALCIGGGEATALAVELP atoB ignore metacyc::MONOMER-20831 acetyl-CoA C-acetyltransferase (EC 2.3.1.16) MQDVVIVAATRTAVGSFQGSLASIPAPELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGSGQNPARQASILAGLPHAVPSLTLNKVCGSGLKALHLGAQAIRCGDAEVIIAGGMENMSLAPYVLPAARTGLRMGHAKMIDSMITDGLWDAFNDYHMGITAENLVDKYGISREAQDAFAAASQQKATAAIEAGRFVDEITPILIPQRKGDPVAFAVDEQPRAGTTAESLAKLKPAFKKDGSVTAGNASSLNDGAAAVLLMSADKAKALGLPVLARIASYANAGVDPAIMGIGPVSATRRCLDKAGWSLGDLDLIEANEAFAAQSLAVGKELEWDAEKVNVNGGAIAIGHPIGASGCRVLVTLLHEMIKRDAKKGLATLCIGGGQGVALALERS atoB ignore metacyc::MONOMER-3207 subunit of β-ketoadipyl CoA thiolase (EC 2.3.1.174; EC 2.3.1.16) MRDVFICDAIRTPIGRFGGALAGVRADDLAAVPLKALIEPNPAVQWDQVDEVFFGCANQAGEDNRNVARMALLLAGLPESIPGVTLNRLCASGMDAIGTAFRAIASGEMELAIAGGVESMSRAPFVMGKAESGYSRNMKLEDTTIGWRFINPLMKSQYGVDSMPETADNVADDYQVSRADQDAFALRSQQKAAAAQAAGFFAEEIVPVRIAHKKGETIVERDEHLRPETTLEALTKLKPVNGPDKTVTAGNASGVNDGAAALILASAEAVKKHGLTPRARVLGMASGGVAPRVMGIGPVPAVRKLTERLGVAVSDFDVIELNEAFASQGLAVLRELGVADDAPQVNPNGGAIALGHPLGMSGARLVLTALHQLEKSGGRKGLATMCVGVGQGLALAIERV atoB ignore reanno::ANA3:7022768 Acetyl-CoA C-acyltransferase (EC 2.3.1.16) MKQAVIVDCIRTPMGRSKAGVFRNVRAETLSAELMKGLLLRNPQLDPNTIEDVIWGCVQQTLEQGFNIARNASLLAGIPKTAGAVTVNRLCGSSMEAIHQAARAIMTGMGDTFIIGGVEHMGHVPMNHGVDFHPGLANNVAKASGMMGLTAEMLGKLHGITREQQDAFAVRSHQRAHAATVEGRFAKEIYGIEGHDANGALIKVLHDEVIRPETSMESLAALRPVFDPANGTVTAGTSSALSDGASAMLVMEESKARALGLPIRARIRSMAVAGCDAAIMGYGPVPATQKALARAGITVNDLDVIELNEAFAAQSLPCVKDLGLLDVVEDKINLNGGAIALGHPLGCSGARISTTLINLMEHKDATLGLATMCIGLGQGIATVFERV atoB ignore reanno::MR1:200842 3-ketoacyl-CoA thiolase [isoleucine degradation] (EC 2.3.1.16) MSTELLNQEIVIVAAKRTPMGSFQGSLSGITSLSLAATAIKALLADTQVAPDKVDEVLMGCVLPAGLGQAPARQATLGAGLPLSVGATTVNKVCGSGMKTVMLAHDLIKAGSAKVVIAGGMESMSQAPYLLDKARAGIRMGHGKVLDHMFLDGLEDAYTGGAMGTFAQKTADEFGITREQMDAFALSSLEKANAAINSGAFKTEIVPVTVSDRRGDVTIDTDEQPGNARPEKIPTLRPAFAKDGTITAANSSSISDGAAALMLTTRANAEQLGLTVLATIKGHTTHAQEPALFTTAPVGAMAKLLSNVGWSKDEVDLFEINEAFAMVTMLAVSELGLDMTKVNVNGGACALGHPIGCSGARLLVTLIHALKARGLKRGVASLCIGGGEATAMAIEV atoB ignore reanno::Marino:GFF1551 Acetyl-CoA C-acyltransferase (EC 2.3.1.16) MGRAKNGCFRNVRAETLSANLIEALFERNPKLDPKEVEDVIWGCVNQTKEQGFNVARQISLLTRIPHESAAQTVNRLCGSAMSAIHTAAQAIMTGNGDVFFVGGVEHMGHVPMTEGFDHNPAASKYSAKASNMMGLTAEMLAKMHGITREQQDEFGARSHRLAHEATLEGRFKNEIVPIEGHDENGFKVLIEEDETIRPETTAESLSQLKPAFDPKNGTVTAGTSSQLTDGAAAMVLMSAERAEALGLKPIAKIRSMAVAGCDPAIMGYGPVPATKKALKRAGLKVEDIDFWELNEAFAGQSLPVLKDLKLLGVMEEKVNLNGGAIALGHPLGCSGARISTTLLNVMQAKGGKLGVSTMCIGLGQGIATVWERL atoB ignore reanno::SB2B:6935813 Acetyl-CoA C-acyltransferase (EC 2.3.1.16) MKQAVIVDCIRTPMGRSKGGVFRNVRAETLSAELMKALLLRNPGVDPNTIEDVIWGCVQQTLEQGFNIARNASLLAGVPKTAGAVTVNRLCGSSMEALHQASRAIMTGMGDTFIIGGVEHMGHVPMNHGVDFHPGLAANVAKASGMMGLTAEMLGKLHGISREMQDQFAVRSHQRAHAASIEGRFANEIYAIEGHDANGALIKVDYDEVIRPETTLESLAGLRPVFDPANGTVTAGTSSALSDGAAAMLVMEEEKARALGLTIRARVRSMAVAGCDAAIMGYGPVPATQKALARAGLSIQDMDVIELNEAFAAQSLPCVKDLGLMDVVEDKVNLNGGAIALGHPLGCSGARISTTLINLMEHKDATLGLATMCIGLGQGIATVFERV atoB ignore reanno::acidovorax_3H11:Ac3H11_2994 3-ketoacyl-CoA thiolase (EC 2.3.1.16) MSTTIQDPIVIVGAARTPMGSLQGDFSSLAAHDLGGAAIKAAIERAGVSPDAVGEVLFGNCLMAGQGQAPARQAAFKGGLPKGAGAVTLSKMCGSGMKAAMMAHDMLLAGSHDVMVAGGMESMTNAPYLLQKGRGGYRLGHDRIFDHMMLDGLEDAYEAGRSMGTFGEDCAAKYSFTREQQDAFATASVQRAKAATESGAFAAEIVPVTVKTRAGETVVSVDEGPGKVKLEKIATLKPAFKKDGTITAASSSSINDGAAALVMMRESTAKKLGAKPLARIVSHATHAQEPEWFATAPLGATQKALAKAGWQVGDVQLWEINEAFAVVPMALMKELDLPHDKVNVNGGACALGHPIGASGARIMVTLIHALKARGLTKGLATLCIGGGEATAVALELV atoB ignore reanno::pseudo13_GW456_L13:PfGW456L13_2982 3-ketoacyl-CoA thiolase (EC 2.3.1.16) MTMSNDPIVIVSAVRTPMGGFQGELKSLTAPQLGAAAIKAAVERAGVASDSVDEVLFGCVLPAGLGQAPARQAALGAGLDKSTRCTTLNKMCGSGMEAAILAHDMLLAGSADVVVAGGMESMSNAPYLLDRARAGYRMGHGRVQDSMFLDGLEDAYDKGRLMGTFAEDCAETNGFSREAQDAFAIASTTRAQQAIKDGSFKAEIVPLTVTVGKEQVVISNDEQPPKARLDKIASLKPAFREGGTVTAANSSSISDGAAALVLMRQSQAQKQGLKPLAVIHGHAAFADTPGLFPVAPIGAIKKLMKKTGWSLNDVDLVEVNEAFAVVGMAAMTHLEIPHEKLNVHGGACALGHPIGASGARILVTLLSALRQKGLKRGVAAICIGGGEATAMAVECLY atoD curated ecocyc::ATOA-MONOMER,metacyc::ATOA-MONOMER acetyl-CoA:acetoacetyl-CoA transferase subunit β;; acetyl-CoA:acetoacetyl-CoA transferase subunit β MDAKQRIARRVAQELRDGDIVNLGIGLPTMVANYLPEGIHITLQSENGFLGLGPVTTAHPDLVNAGGQPCGVLPGAAMFDSAMSFALIRGGHIDACVLGGLQVDEEANLANWVVPGKMVPGMGGAMDLVTGSRKVIIAMEHCAKDGSAKILRRCTMPLTAQHAVHMLVTELAVFRFIDGKMWLTEIADGCDLATVRAKTEARFEVAADLNTQRGDL atoD curated metacyc::HP0692-MONOMER succinyl-CoA:acetoacetate CoA-transferase subunit B (EC 2.8.3.5) MREAIIKRAAKELKEGMYVNLGIGLPTLVANEVSGMNIVFQSENGLLGIGAYPLEGSVDADLINAGKETITVVPGASFFNSADSFAMIRGGHIDLAILGGMEVSQNGDLANWMIPKKLIKGMGGAMDLVHGAKKVIVIMEHCNKYGESKVKKECSLPLTGKGVVHQLITDLAVFEFSNNAMKLVELQEGVSLDQVKEKTEAEFEVRL atoD curated reanno::psRCH2:GFF1044 acetyl-CoA:acetoacetate CoA transferase, B subunit (EC 2.8.3.8) MAWTREQMAQRAAQELQDGFYVNLGIGLPTLVANYIPEGMDVWLQSENGLLGIGPFPTEEEIDPDLINAGKQTVTALPGSSFFDNAQSFAMIRGGHINLAILGAMQVSEKGDLANWMIPGKMVKGMGGAMDLVAGVKRVVVLMEHTAKGGAHKILPACDLPLTGLGVVDRIITDLGVLDVTEQGLKLVELAEGVSFDELQEATGSPIQR atoD curated reanno::pseudo6_N2E2:Pf6N2E2_2112 Dehydrocarnitine CoA-transferase and acetoacetate CoA-transferase, subunit B MALSREQMAQRVAREMQDGYYVNLGIGIPTLVANYIPEGMEVMLQSENGLLGMGAFPTEAEVDADMINAGKQTVTARIGASIFSSAESFAMIRGGHIDLTVLGAFEVDVEGNIASWMIPGKLVKGMGGAMDLVAGAENIIVTMTHASKDGESKLLPRCSLPLTGAGCIKRVLTDLAYLEIQDGAFILKERAPGVSVEEIVAKTAGKLIVPDHVPEMQFAAQ atoD ignore BRENDA::B2GV06,SwissProt::B2GV06 3-oxoacid CoA-transferase (EC 2.8.3.5);; Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial; 3-oxoacid CoA-transferase 1; Somatic-type succinyl-CoA:3-oxoacid CoA-transferase; SCOT-s; EC 2.8.3.5 MAALKLLSSGLRLCASARNSRGALHKGCACYFSVSTRHHTKFYTDPVEAVKDIPNGATLLVGGFGLCGIPENLIGALLKTGVKDLTAVSNNAGVDNFGLGLLLRSKQIKRMISSYVGENAEFERQFLSGELEVELTPQGTLAERIRAGGAGVPAFYTSTGYGTLVQEGGSPIKYNKDGSVAIASKPREVREFRGQHFILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAGTTVVEVEEIVDIGSFAPEDIHIPKIYVHRLIKGEKYEKRIERLSLRKEGEGKAKSGKPGEDVRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNMTVHLQSENGVLGLGPYPLKDEADADLINAGKETVTVLPGASFFSSDESFAMIRGGHVNLTMLGAMQVSKYGDLANWMIPGKMVKGMGGAMDLVSSSKTKVVVTMEHSAKGNAHKIMEKCTLPLTGKQCVNRIITEKGVFDVDKKNGLTLIELWEGLTVDDIRKSTGCDFAVSPNLMPMQQIST atoD ignore BRENDA::P55809,SwissProt::P55809,metacyc::HS01447-MONOMER 3-oxoacid CoA-transferase (EC 2.8.3.5);; Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial; 3-oxoacid CoA-transferase 1; Somatic-type succinyl-CoA:3-oxoacid CoA-transferase; SCOT-s; EC 2.8.3.5;; succinyl-CoA:3-ketoacid-coenzyme A transferase 1, mitochondrial (EC 2.8.3.5) MAALKLLSSGLRLCASARGSGATWYKGCVCSFSTSAHRHTKFYTDPVEAVKDIPDGATVLVGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGVDNFGLGLLLRSKQIKRMVSSYVGENAEFERQYLSGELEVELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGGSPIKYNKDGSVAIASKPREVREFNGQHFILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAETTVVEVEEIVDIGAFAPEDIHIPQIYVHRLIKGEKYEKRIERLSIRKEGDGEAKSAKPGDDVRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNITVHLQSENGVLGLGPYPRQHEADADLINAGKETVTILPGASFFSSDESFAMIRGGHVDLTMLGAMQVSKYGDLANWMIPGKMVKGMGGAMDLVSSAKTKVVVTMEHSAKGNAHKIMEKCTLPLTGKQCVNRIITEKAVFDVDKKKGLTLIELWEGLTVDDVQKSTGCDFAVSPKLMPMQQIAN atoD ignore BRENDA::Q63TL3 3-oxoacid CoA-transferase (EC 2.8.3.5) MNKVYPSAAAALEGVVHDGQTFAVGGFGLCGIPEALIAALRDSAVKGITCISNNAGVDGFGLGLLLETRQIKKMISSYVGENKEFERQYLSGELELEFTPQGTLAEKLRAGGAGIPAFFTQTGYGTVIAEGKETREFDGKHYVLEPSLTADVALVKAWKADKSGNLVYRRTARNFNPMCAMAGRITIAEVEEIVENGELDPDAIHTPGIFVQRLVLNATPEKRIEQRVVRAKGD atoD ignore BRENDA::Q9D0K2 3-oxoacid CoA-transferase (EC 2.8.3.5) MAALKLLSSGLRLGASARSSRGALHKGCVCYFSVSTRHHTKFYTDPVEAVKDIPNGATLLVGGFGLCGIPENLIGALLKTGVKDLTAVSNNAGVDNFGLGLLLRSKQIKRMISSYVGENAEFERQFLSGELEVELTPQGTLAERIRAGGAGVPAFYTSTGYGTLVQEGGSPIKYNKDGSVAIASKPREVREFNGQHFILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAGTTVVEVEEIVDIGSFAPEDIHIPKIYVHRLIKGEKYEKRIERLSLRKEGDGKGKSGKPGGDVRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNMTVHLQSENGVLGLGPYPLKDEADADLINAGKETVTVLPGASFFSSDESFAMIRGGHVNLTMLGAMQVSKYGDLANWMIPGKMVKGMGGAMDLVSSSKTKVVVTMEHSAKGNAHKIMEKCTLPLTGKQCVNRIITEKGVFDVDKKNGLTLIELWEGLTVDDIKKSTGCDFAVSPNLMPMQQIST atoD ignore BRENDA::Q9JJN4 3-oxoacid CoA-transferase (EC 2.8.3.5) MAALRLLAWALPRGVSALRPPPALPHRLIRRYVSDRSGSVHFYTDPVKAVEGVKDGSTVMLGGFGLCGIPENLIGALKTKGVKDLKIVSSNVGVDDFGLGILLASKQVRRVVCSYLGENALCEKLYLAGELELEMTPQGTLAERIRAGGTGVPAFYTPTGYGTLVQEGGSPIRYAPDGHLITLSEPREVREFQGRFYLLEHAIRADFALIKGWKADRSGNVIFRGSARNFNVPMCKAADISVVEVEEIVDVGTFAPEDIHVPNIYVDRVIKGPKFEKRIERLTTRDSKPAPGSKDNDPSRTRIIKRAALEFQDGMYANLGIGIPVLASNYISPKMTVYLHSENGILGLGPFPLKNEVDADVINAGKQTVTVVPGGCFFASDDSFAMIRGGHLQLTMLGAMQVSQYGDLANWMVPGKKVKGMGGAMDLVSSKKTRVVVTMEHCTKTKQPKILKKCTMPLTGKRCVDLIITEKAVFEVNHSKGLTLVELWEGSSVDDIKATTACSFAVSPNLKPMQQIKLDA atoD ignore SwissProt::P56006,metacyc::HP0691-MONOMER Succinyl-CoA:3-ketoacid coenzyme A transferase subunit A; Succinyl-CoA:3-oxoacid CoA-transferase; OXCT A; EC 2.8.3.5;; succinyl-CoA:acetoacetate CoA-transferase subunit A (EC 2.8.3.5) MNKVITDLDKALSALKDGDTILVGGFGLCGIPEYAIDYIYKKGIKDLIVVSNNCGVDDFGLGILLEKKQIKKIIASYVGENKIFESQMLNGEIEVVLTPQGTLAENLHAGGAGIPAYYTPTGVGTLIAQGKESREFNGKEYILERAITGDYGLIKAYKSDTLGNLVFRKTARNFNPLCAMAAKICVAEVEEIVPAGELDPDEIHLPGIYVQHIYKGEKFEKRIEKITTRSTK atoD ignore SwissProt::Q29551,BRENDA::Q29551 Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial; 3-oxoacid CoA-transferase 1; Somatic-type succinyl-CoA:3-oxoacid CoA-transferase; SCOT-s; EC 2.8.3.5;; 3-oxoacid CoA-transferase (EC 2.8.3.5) MAALTLLSSRLRLCASAYRSGGAWSQGCAGYFSTSTRRHTKFYTDAVEAVKDIPNGATVLVGGFGLCGIPENLIGALLKTGVKELTAVSNNAGVDNFGLGLLLQSKQIKRMISSYVGENAEFERQYLAGELEVELTPQGTLAERIRAGGAGVPAFYTSTGYGTLVQEGGSPIKYNKDGSIAIASKPREVREFNGQHFILEEAIRGDFALVKAWKADQAGNVTFRKSARNFNLPMCKAAETTVVEVEEIVDIGSFAPEDIHIPKIYVHRLVKGEKYEKRIERLSVRKEEDVKTRSGKLGDNVRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNMTVHLQSENGILGLGPYPLQNEVDADLINAGKETVTVLPGASYFSSDESFAMIRGGHVNLTMLGAMQVSKYGDLANWMIPGKLVKGMGGAMDLVSSAKTKVVVTMEHSAKGNAHKIMEKCTLPLTGKQCVNRIITEKAVFDVDSKKGLTLIELWEGLTVDDIKKSTGCDFAVSPKLIPMQQVTT atoD ignore SwissProt::Q5XIJ9 Succinyl-CoA:3-ketoacid coenzyme A transferase 2A, mitochondrial; 3-oxoacid CoA-transferase 2A; Testis-specific succinyl-CoA:3-oxoacid CoA-transferase 1; SCOT-t1; EC 2.8.3.5 MAALRLLAWAFSRRVSAHRPQPTLPHHLIRHYPTTRCGKVKFYTDPVKAVEGIKDGASVMLGGFGLCGIPENLIGALKTKGVKDLKIISSNVGVDDFGLGILLASKQVRRVVCSYLGENKLCEQLYLAGKLELEMTPQGTLAERIRAGGTGVPAFYTPTGYGTQVQEGGVPIRYSPEGHLITLSQPREVREFEGQHHLLERAIRADFALIKGWKADRSGNVIFRGSARNFNVPMCKAADISVVEVEEIVDVGTFAPEDIHIPNIYVKRVIKGPRFEKRIERLTTRDSPPAPGSKDQDPKRTRIIKRAALEFKDGMYANLGIGIPVLASNYISPKMTVYLHSENGILGLGPFPLKKEVDPDIINAGKQTVTVIPGGCFFASDDSFAMIRGGHIQLTMLGAMQVSKYGDLANWMVPGKKVKGMGGAMDLVSSKKTKVVVTMEHCTKTKQPKILEKCTMPLTGKSCVDLIITEKAVFEVDRSKGLKLVELWEGSSLDEVKATTGCSFKVCPNLKPMQQIKSDA atoD ignore SwissProt::Q9BYC2,BRENDA::Q9BYC2 Succinyl-CoA:3-ketoacid coenzyme A transferase 2, mitochondrial; 3-oxoacid CoA-transferase 2A; Testis-specific succinyl-CoA:3-oxoacid CoA-transferase; SCOT-t; EC 2.8.3.5;; 3-oxoacid CoA-transferase (EC 2.8.3.5) MAALRLLASVLGRGVPAGGSGLALSQGCARCFATSPRLRAKFYADPVEMVKDISDGATVMIGGFGLCGIPENLIAALLRTRVKDLQVVSSNVGVEDFGLGLLLAARQVRRIVCSYVGENTLCESQYLAGELELELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGGAPIRYTPDGHLALMSQPREVREFNGDHFLLERAIRADFALVKGWKADRAGNVVFRRSARNFNVPMCKAADVTAVEVEEIVEVGAFPPEDIHVPNIYVDRVIKGQKYEKRIERLTILKEEDGDAGKEEDARTRIIRRAALEFEDGMYANLGIGIPLLASNFISPSMTVHLHSENGILGLGPFPTEDEVDADLINAGKQTVTVLPGGCFFASDDSFAMIRGGHIQLTMLGAMQVSKYGDLANWMIPGKKVKGMGGAMDLVSSQKTRVVVTMQHCTKDNTPKIMEKCTMPLTGKRCVDRIITEKAVFDVHRKKELTLRELWEGLTVDDIKKSTGCAFAVSPNLRPMQQVAP atoD ignore SwissProt::Q9ESL0 Succinyl-CoA:3-ketoacid coenzyme A transferase 2B, mitochondrial; 3-oxoacid CoA-transferase 2B; Testis-specific succinyl-CoA:3-oxoacid CoA-transferase 2; SCOT-t2; EC 2.8.3.5 MAALRLLAWALPRGVSALRPRPALPHRLIRRYVSDRSGSVHFYTDPVKAVEGVKDGSTVMLGGFGLCGIPENLIGALKTKGVKDLKIVSSNVGVDDFGLGILLASKQVRRVVCSYLGENALCEKLYLAGELELEMTPQGTLAERIRACGTGVPAFYTPTGYGTLVQEGGSPIRYAPDGHLITLSEPREVREFQGRFYLLEHAIRADFALIKGWKADRSGNVIFRGSARNFNVPMCKAADISVVEVEEIVDVGTFAPEDIHIPNIYVDRVIKGPKFEKRIERLTTRDSKPAPGSKDNDPSRTRIIKRAALEFQDGMYANLGIGIPVLASNYISPKMTVYLHSENGILGLGPFPLKNEVDADVINAGKQTVTVVPGGCFFASDDSFAMIRGGHLQLTMLGAMQVSQYGDLANWMVPGKKVKGMGGAMDLVSSKKTRVVVTMEHCTKTKQPKILKKCTMPLTGKRCVDLIITEKAVFEVNHSKGLTLVELWEGSSVDDIKATTACSFAVSPNLKPMQQIKLDA atoD ignore SwissProt::Q9W058,BRENDA::Q9W058 Succinyl-CoA:3-ketoacid-coenzyme A transferase, mitochondrial; 3-oxoacid CoA-transferase; EC 2.8.3.5;; 3-oxoacid CoA-transferase (EC 2.8.3.5) MLCRLVGNRSLGARYTASIKAIACYSTSGKQRNGKIYESAIDAVADVQDGAQILFGGFGICGIPEKMINALKQKGVKNITGVSNNGGVDDTGLGVLIKQKQVSKVIGSYVGENTELVRQYLEGELAVELTPQGTLAEKIRAGGAGIPAFYTPTGYATLVQEGGAPIKYSKDGKVEISSEKKPVKEFNGKNYVMEESIFADFAFVKAQKADPLGNLVFNKAARNFNAPMCRAAKITVAEVEEIVPIGALSPDEIHVPGIYINRIFKGTNYNKRVERLRITEPKDPSKPAPPPNPAQVLRERIARRVALEFHDGMYANLGIGIPVLSSNYIPKGMNVMLQSENGILGLGPFPTKDKVDPDLINAGKESVTVVPGASYFGSDDSFAMIRGGHVDITILGAMEVSATGDLANWMIPGKLVKGMGGAMDLVAAPGTKVIITMEHNARDGSPKILDTCSLPLTGKGVIDMIISEKAVFTVEKGVGLTLIEVAEGYTVDDIIASTGAKFTVSPNLKKMGQIPV atoD ignore reanno::Cup4G11:RR42_RS06555 3-oxoacid CoA-transferase (EC 2.8.3.5) MNKVYASAAEALAGVVRDGQTIAVGGFGLCGIPEALIAALRDSGAKQLTCISNNAGVDGFGLGLLLATRQIKKMISSYVGENKEFERQYLAGELELEFTPQGTLAEKLRAGGSGIPAFFTKTGVGTIVADGKEIREFDGQQYVMERALTADVALVKAYKADRAGNLVFRRTARNFNPMCAMAGKVTIVEVEHLVDTGTLDPDEVHTPGIFVQRIVLNANPEKRIEQRTVRAAG atoD ignore reanno::SB2B:6937186 3-oxoacid CoA-transferase (EC 2.8.3.5) MALSREQLAQRVAKELKDGYYVNLGIGIPTLVANYIPDGMQVMLQSENGLLGMGEFPTEETIDPDLINAGKQTVTAVKGASFFSSAESFAMIRGGHVDLTVLGAFEVDVEGSIASWMIPGKLVKGMGGAMDLVAGADNIIVTMMHADKYGNSKLLPKCELPLTGFGCIKRVLTDLAFIEIKDGAFHLLERAPGVTVEEIVEKTAGKLIVPEHVPEMQF atoD ignore reanno::SB2B:6937187 3-oxoacid CoA-transferase (EC 2.8.3.5) MAGLYKVVDSYDQALAGLTDNMTIMVGGFGLCGIPEGLINQMVKLGTKGLTAISNNAGVDDFGLGLLLQNKQISTMIASYVGENATFERQMLSGELNVILTPQGTLAEKIRAGGAGIPAFFTATGYGTPVAEGKETREIKGRHYVLEESLTADFALIRAWKADTMGNLVFRKTAANFNPMMATAGKITVVEVEEIVEPGELDPDHIHTPGIYVDRIIKGSFEKRIEQRTVKKA bcaP curated TCDB::S6EX81 Branched chain amino acid (Leucine/isoleucine/valine) uptake transporter of 469 aas and 12 TMSs, BcaP or CitA MGFMRKADFELYRDADKHYNQVLTTRDFLALGVGTIISTSIFTLPGQVAAQFAGPGVVFSYLLAALVAGFVALAYAEMSTVMPFAGSAYSWISVLFGEGFGWIAGWALLAEYFIAVAFVGSGFSANLQQLLAPLGFHLPKVLANPFGTDGGVVDIISLLVILLSAIIVFRGASDAGRISQILVVLKVAAVIAFIIVGITVIKPANYHPFIPPHNPKTGFGGFSGIWSGVSMIFLAYIGFDSIAANSAEAKNPQKTMPRGIIGSLLIAVVLFAAVTLVLVGMHPYSAYAGNAAPVGWALQQSGYSVLSEVVTAIALAGMFIALLGMVLAGSRLLYAFGRDGLLPKGLGKMNARNLPANGVWTLAIVAIVIGAFFPFAFLAQLISAGTLIAFMFVTLGIYSLRRRQGKDLPEATYKMPFYPVLPALGFIGSLFVFWGLDVQAKLYSGIWFLIGILIYFAYGNRRSRKSEEK bkdA curated BRENDA::Q72GU1 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) (EC 1.2.4.4) MVKETHRFEPFTEEPIRLIGEEGEWLGDFPLDLEGEKLRRLYRDMLAARMLDERYTILIRTGKTSFIAPAAGHEAAQVAIAHAIRPGFDWVFPYYRDHGLALALGIPLKELFGQMLATKADPNKGRQMPEHPGSKALNFFTVASPIASHVPPAAGAAISMKLLRTGQVAVCTFGDGATSEGDWYAGINFAAVQGAPAVFVCENNFYAISVDYRHQTHSPTIADKAHAFGIPGYLVDGMDVLASYYVVKEAVERARRGEGPSLVELRVYRYGPHSSADDDSRYRPKEEVAFWRKKDPIPRFRRFLEARGLWNEEWEEDVREEIRAELERGLKEAEEAGPVPPEWMFADVFAEKPWHLLRQEALLKEEL bkdA curated CharProtDB::CH_121278 2-oxoisovalerate dehydrogenase subunit alpha; EC 1.2.4.4 MNEYAPLRLHVPEPTGRPGCQTDFSYLRLNDAGQARKPPVDVDAADTADLSYSLVRVLDEQGDAQGPWAEDIDPQILRQGMRAMLKTRIFDSRMVVAQRQKKMSFYMQSLGEEAIGSGQALALNRTDMCFPTYRQQSILMARDVSLVEMICQLLSNERDPLKGRQLPIMYSVREAGFFTISGNLATQFVQAVGWAMASAIKGDTKIASAWIGDGATAESDFHTALTFAHVYRAPVILNVVNNQWAISTFQAIAGGESTTFAGRGVGCGIASLRVDGNDFVAVYAASRWAAERARRGLGPSLIEWVTYRAGPHSTSDDPSKYRPADDWSHFPLGDPIARLKQHLIKIGHWSEEEHQATTAEFEAAVIAAQKEAEQYGTLANGHIPSAASMFEDVYKEMPDHLRRQRQELGV bkdA curated SwissProt::O45924 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial; Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain; EC 1.2.4.4 MHRALLNASRRVATVRSMASTVEGDAFRLSEYSSKYLGHRKAAFTEKLEIVNADDTPALPIYRVTNAVGDVIDKSQDPNFDEQTSLKMYKTMTQLNIMDRILYDSQRQGRISFYMTSFGEEGNHVGSAAALEPQDLIYGQYREAGVLLWRGYTMENFMNQCYGNADDLGKGRQMPMHFGTKERNFVTISSPLTTQLPQAVGSAYAFKQQKDNNRIAVVYFGDGAASEGDAHAAFNFAATLKCPIIFFCRNNGYAISTPTSEQYGGDGIAGKGPAYGLHTIRVDGNDLLAVYNATKEARRVALTNRPVLIEAMTYRLGHHSTSDDSTAYRSSDEVQTWGDKDHPITRFKKYITERGWWNEEKEMEWQKEVKKRVLTEFAAAEKRKKAHYHDLFEDVYDELPLRLRRQRDELDAHVAEYKEHYPMLETLQSKP bkdA curated SwissProt::P11178 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial; Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain; BCKDE1A; BCKDH E1-alpha; EC 1.2.4.4 MQGSAKMAMAVAVAVARVWRPSRGLGRTGLPLLRLLGARGLARFHPHRWQQQQHFSSLDDKPQFPGASAEFIDKLEFIQPNVISGIPIYRVMDRQGQIINPSEDPHLPQEKVLKFYKSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALDDTDLVFGQYREAGVLMYRDYPLELFMAQCYGNVSDLGKGRQMPVHYGCRERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEGAASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGILSIRVDGNDVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDHPISRLRHHLQSRGWWDDEQEKAWRKQSRKKVMEAFEQAERKLKPNPSLIFSDVYQEMPAQLRKQQESLARHLQTYGEHYPLDHFEK bkdA curated SwissProt::P12694,metacyc::MONOMER-12005 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial; Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain; BCKDE1A; BCKDH E1-alpha; EC 1.2.4.4;; branched-chain α-keto acid dehydrogenase E1 component α subunit (EC 1.2.4.4) MAVAIAAARVWRLNRGLSQAALLLLRQPGARGLARSHPPRQQQQFSSLDDKPQFPGASAEFIDKLEFIQPNVISGIPIYRVMDRQGQIINPSEDPHLPKEKVLKLYKSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALDNTDLVFGQYREAGVLMYRDYPLELFMAQCYGNISDLGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEGAASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDHPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQAERKPKPNPNLLFSDVYQEMPAQLRKQQESLARHLQTYGEHYPLDHFDK bkdA curated SwissProt::P9WIS3 3-methyl-2-oxobutanoate dehydrogenase subunit alpha; Branched-chain alpha-ketoacid dehydrogenase E1 component subunit alpha; BCKADH E1-alpha; EC 1.2.4.4 MGEGSRRPSGMLMSVDLEPVQLVGPDGTPTAERRYHRDLPEETLRWLYEMMVVTRELDTEFVNLQRQGELALYTPCRGQEAAQVGAAACLRKTDWLFPQYRELGVYLVRGIPPGHVGVAWRGTWHGGLQFTTKCCAPMSVPIGTQTLHAVGAAMAAQRLDEDSVTVAFLGDGATSEGDVHEALNFAAVFTTPCVFYVQNNQWAISMPVSRQTAAPSIAHKAIGYGMPGIRVDGNDVLACYAVMAEAAARARAGDGPTLIEAVTYRLGPHTTADDPTRYRSQEEVDRWATLDPIPRYRTYLQDQGLWSQRLEEQVTARAKHVRSELRDAVFDAPDFDVDEVFTTVYAEITPGLQAQREQLRAELARTD bkdA curated SwissProt::Q5SLR4 2-oxoisovalerate dehydrogenase subunit alpha; Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain; BCKDH E1-alpha; EC 1.2.4.4 MVKETHRFETFTEEPIRLIGEEGEWLGDFPLDLEGEKLRRLYRDMLAARMLDERYTILIRTGKTSFIAPAAGHEAAQVAIAHAIRPGFDWVFPYYRDHGLALALGIPLKELLGQMLATKADPNKGRQMPEHPGSKALNFFTVASPIASHVPPAAGAAISMKLLRTGQVAVCTFGDGATSEGDWYAGINFAAVQGAPAVFIAENNFYAISVDYRHQTHSPTIADKAHAFGIPGYLVDGMDVLASYYVVKEAVERARRGEGPSLVELRVYRYGPHSSADDDSRYRPKEEVAFWRKKDPIPRFRRFLEARGLWNEEWEEDVREEIRAELERGLKEAEEAGPVPPEWMFEDVFAEKPWHLLRQEALLKEEL bkdA curated SwissProt::Q84JL2 2-oxoisovalerate dehydrogenase subunit alpha 2, mitochondrial; Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain; BCKDE1A; BCKDH E1-alpha; EC 1.2.4.4 MALHLRSSFSSKSTLLNILRHNLGFGSRSHVTRHIRQILPHDPPLRGSQNPISRLCNTMAEPETLSSFVQHEYANNHQVMDFPGGKVAFTPEIQFISESDKERVPCYRVLDDNGQLITNSQFVQVSEEVAVKIYSDMVTLQIMDNIFYEAQRQGRLSFYATAIGEEAINIASAAALTPQDVIFPQYREPGVLLWRGFTLQEFANQCFGNKSDYGKGRQMPVHYGSNKLNYFTVSATIATQLPNAVGAAYSLKMDKKDACAVTYFGDGGTSEGDFHAALNIAAVMEAPVLFICRNNGWAISTPTSDQFRSDGVVVKGRAYGIRSIRVDGNDALAMYSAVHTAREMAIREQRPILIEALTYRVGHHSTSDDSTRYRSAGEIEWWNKARNPLSRFRTWIESNGWWSDKTESDLRSRIKKEMLEALRVAEKTEKPNLQNMFSDVYDVPPSNLREQELLVRQTINSHPQDYPSDVPL bkdA curated SwissProt::Q9LPL5 2-oxoisovalerate dehydrogenase subunit alpha 1, mitochondrial; Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain; BCKDE1A; BCKDH E1-alpha; EC 1.2.4.4 MAIWFARSKTLVSSLRHNLNLSTILIKRDYSHRPIFYTTSQLSSTAYLSPFGSLRHESTAVETQADHLVQQIDEVDAQELDFPGGKVGYTSEMKFIPESSSRRIPCYRVLDEDGRIIPDSDFIPVSEKLAVRMYEQMATLQVMDHIFYEAQRQGRISFYLTSVGEEAINIASAAALSPDDVVLPQYREPGVLLWRGFTLEEFANQCFGNKADYGKGRQMPIHYGSNRLNYFTISSPIATQLPQAAGVGYSLKMDKKNACTVTFIGDGGTSEGDFHAGLNFAAVMEAPVVFICRNNGWAISTHISEQFRSDGIVVKGQAYGIRSIRVDGNDALAVYSAVRSAREMAVTEQRPVLIEMMTYRVGHHSTSDDSTKYRAADEIQYWKMSRNPVNRFRKWVEDNGWWSEEDESKLRSNARKQLLQAIQAAEKWEKQPLTELFNDVYDVKPKNLEEQELGLKELVKKQPQDYPPGFHV bkdA curated metacyc::MONOMER-11683 2-keto-isovalerate dehydrogenase component α subunit (EC 1.2.4.4) MSTNRHQALGLTDQEAVDMYRTMLLARKIDERMWLLNRSGKIPFVISCQGQEAAQVGAAFALDREMDYVLPYYRDMGVVLAFGMTAKDLMMSGFAKAADPNSGGRQMPGHFGQKKNRIVTGSSPVTTQVPHAVGIALAGRMEKKDIAAFVTFGEGSSNQGDFHEGANFAAVHKLPVIFMCENNKYAISVPYDKQVACENISDRAIGYGMPGVTVNGNDPLEVYQAVKEARERARRGEGPTLIETISYRLTPHSSDDDDSSYRGREEVEEAKKSDPLLTYQAYLKETGLLSDEIEQTMLDEIMAIVNEATDEAENAPYAAPESALDYVYAK bkdA curated reanno::Smeli:SMc03201 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) (EC 1.2.4.4) MDEFSRLSLHVPEPAVRPGDLPDFSNVKIPKAGSVPRPDVDVDPEEIRDLAYSIIRVLNREGEAVGPWAGFLSDEELLTGLRHMMLLRAFDARMLMAQRQGKTSFYMQHLGEEAVSCAFRKALRKGDMNFPTYRQAGLLIADDYPMVEMMNQIFSNELDPCHGRQLPVMYTSKEHGFFTISGNLATQYVQAVGWAMASAIKNDTRIAAGWIGDGSTAESDFHSALVFASTYKAPVILNIVNNQWAISTFQGIARGGSGTFAARGLGFGIPALRVDGNDYLAVYAVARWAAERARLNLGPTLIEYVTYRVGAHSTSDDPSAYRPKTESEAWPLGDPVLRLKKHLILRGAWSEERHAQAEAEIMDEVIQAQKEAERHGTLHAGGRPSVRDIFEGVYAEMPPHIRRQRQKAGY bkdA curated reanno::pseudo13_GW456_L13:PfGW456L13_3540 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) (EC 1.2.4.4) MTQAYEPLRLHVPEPSGRPGCKTDFSYLHLTDAGTVRKPPIDVEPADTADLARGLIRVLDDQGNALGPWAENVPVEILRKGMRAMLKTRIYDNRMVVAQRQKKMSFYMQSLGEEAIGSAQALALNIDDMCFPTYRQQSILMARDVPLVDLICQLLSNERDPLKGRQLPIMYSVKDSGFFTISGNLATQFVQAVGWGMASAIKGDTKIASAWIGDGATAESDFHTALTFAHVYRAPVILNVVNNQWAISTFQAIAGGEATTFAGRGVGCGIASLRVDGNDFYAVYAASAWAAERARRNLGPTMIEWVTYRAGPHSTSDDPSKYRPADDWSHFPLGDPIARLKQHLIKIGQWSEEEHAAVSAELEAQVIAAQKEAEQYGTLAGGQIPSAATMFEDVYKEMPEHLKRQRQELGI bkdA curated reanno::pseudo3_N2E3:AO353_26635 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) (EC 1.2.4.4) MNQAYEPLRLHVPEPSGRPGCKTDFSYLRLTDAGTVRKPPIDVEPADTADLAKGLIRVLDDQGNALGPWAEGVPVEILRKGMRAMLKTRIFDNRMVVAQRQKKMSFYMQSLGEEAIGSAQALALNIDDMCFPTYRQQSILMAREVPLVDLICQLLSNERDPLKGRQLPIMYSVKDAGFFTISGNLATQFVQGVGWGMASAIKGDTKIASAWIGDGATAESDFHTALTFAHVYRAPVILNVVNNQWAISTFQAIAGGEATTFAGRGVGCGIASLRVDGNDFVAVYAASAWAAERARRNLGPTMIEWVTYRAGPHSTSDDPSKYRPADDWSHFPLGDPIARLKQHLVKIGQWSEEEHVALSAELEAEIIAAQKEAEQYGTLAGGQIPSAATMFEDVYKEMPEHLKRQRQELGI bkdA curated reanno::pseudo5_N2C3_1:AO356_22990 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) (EC 1.2.4.4) MNPAYEPLRLHVPEPSGRPGCKTDFSYLHLSDAGTVRKPPIDVEPADTADLARSLIRVLDDQGNALGDWAADIPVEILRKGMRAMLKTRIYDNRMVVAQRQKKMSFYMQSLGEEAIGSAQALALNIDDMCFPTYRQQSILMAREVPLVDLICQLLSNERDPLKGRQLPIMYSVKDAGFFTISGNLATQFIQGVGWGMASAIKGDTKIASAWIGDGATAESDFHTALTFAHVYRAPVILNVVNNQWAISTFQAIAGGEATTFAGRGVGCGIASLRVDGNDFMAVYAASRWAAERARRNLGPALIEWVTYRAGPHSTSDDPSKYRPADDWSHFPLGDPIARLKQHMVKIGQWSEEEHAAVSAELEAEVIAAQKEAEQYGTLAGGQIPSAATMFEDVYKEMPEHLKRQRQQLGI bkdA curated reanno::pseudo6_N2E2:Pf6N2E2_481 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) (EC 1.2.4.4) MNPAYEPLRLHVPEPSGRPGCKTDFSYLHLSDAGTVRKPSIDVEPADTADLARSLIRVLDDQGNAHGPWAEDVPLDILRKGMRAMLKTRIYDNRMVVAQRQKKMSFYMQSLGEEAIGSGQALALNIDDMCFPTYRQQSILMAREVPLVGMICQLLSNERDPLKGRQLPIMYSVKDAGFFTISGNLATQFIQGVGWGMASAIKGDTKIASAWIGDGATAESDFHTALTFAHVYRAPVILNVVNNQWAISTFQAIAGGEATTFAGRGVGCGIASLRVDGNDFMAVYAASRWAAERARRNLGPALIEWVTYRAGPHSTSDDPSKYRPADDWSHFPLGDPIARLKQHMVKIGQWSEEEHAAVTAELEAEVIAAQKEAEQYGTLAGGQIPSAATMFEDVYKEMPEHLKRQRQQLGI bkdB curated BRENDA::Q9HIA4 branched-chain-2-oxoacid decarboxylase (subunit 2/2) (EC 4.1.1.72) MNMVQALNSAMDLKMSEDDSVIILGEDVGRDGGVFRVTDGLQAKYGPQRVIDTPLSELGIVGMAIGMAVNGLKPIPEIQFQDFIYTSMDQIINQMAKIRYRSGGDYTVPLVLRTPVGGGIKGGLYHSQSGEAYFAHTAGLTVVSPSNPYDAKGLLISAIESPDPVIFLEPKRLYRAQKVEVPDEKYTIPLRKANVLKQGNDVTIVTYGSMVPTVMSVASKSKYDVEVIDLRTIAPMDRDTIISSVKKTGRVVIVHEAPRTLGVGAEISAMISERAIEYLYAPIVRVTGPDTPFPYRLEEYYLPNEGRINAALDRVMSFR bkdB curated CharProtDB::CH_121283 2-oxoisovalerate dehydrogenase subunit beta; EC 1.2.4.4 MATTTMTMIQALRSAMDVMLERDDNVVVYGQDVGYFGGVFRCTEGLQTKYGKSRVFDAPISESGIVGTAVGMGAYGLRPVVEIQFADYFYPASDQIVSEMARLRYRSAGEFIAPLTLRMPCGGGIYGGQTHSQSPEAMFTQVCGLRTVMPSNPYDAKGLLIASIECDDPVIFLEPKRLYNGPFDGHHDRPVTPWSKHPHSAVPDGYYTVPLDKAAITRPGNDVSVLTYGTTVYVAQVAAEESGVDAEVIDLRSLWPLDLDTIVESVKKTGRCVVVHEATRTCGFGAELVSLVQEHCFHHLEAPIERVTGWDTPYPHAQEWAYFPGPSRVGAALKKVMEV bkdB curated SwissProt::P21953,metacyc::MONOMER-12006 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial; Branched-chain alpha-keto acid dehydrogenase E1 component beta chain; BCKDE1B; BCKDH E1-beta; EC 1.2.4.4;; branched-chain α-keto acid dehydrogenase E1 component β subunit (EC 1.2.4.4) MAVVAAAAGWLLRLRAAGAEGHWRRLPGAGLARGFLHPAATVEDAAQRRQVAHFTFQPDPEPREYGQTQKMNLFQSVTSALDNSLAKDPTAVIFGEDVAFGGVFRCTVGLRDKYGKDRVFNTPLCEQGIVGFGIGIAVTGATAIAEIQFADYIFPAFDQIVNEAAKYRYRSGDLFNCGSLTIRSPWGCVGHGALYHSQSPEAFFAHCPGIKVVIPRSPFQAKGLLLSCIEDKNPCIFFEPKILYRAAAEEVPIEPYNIPLSQAEVIQEGSDVTLVAWGTQVHVIREVASMAKEKLGVSCEVIDLRTIIPWDVDTICKSVIKTGRLLISHEAPLTGGFASEISSTVQEECFLNLEAPISRVCGYDTPFPHIFEPFYIPDKWKCYDALRKMINY bkdB curated SwissProt::P9WIS1 3-methyl-2-oxobutanoate dehydrogenase subunit beta; Branched-chain alpha-ketoacid dehydrogenase E1 component subunit beta; BCKADH E1-beta; EC 1.2.4.4 MTQIADRPARPDETLAVAVSDITQSLTMVQAINRALYDAMAADERVLVFGEDVAVEGGVFRVTEGLADTFGADRCFDTPLAESAIIGIAVGLALRGFVPVPEIQFDGFSYPAFDQVVSHLAKYRTRTRGEVDMPVTVRIPSFGGIGAAEHHSDSTESYWVHTAGLKVVVPSTPGDAYWLLRHAIACPDPVMYLEPKRRYHGRGMVDTSRPEPPIGHAMVRRSGTDVTVVTYGNLVSTALSSADTAEQQHDWSLEVIDLRSLAPLDFDTIAASIQRTGRCVVMHEGPRSLGYGAGLAARIQEEMFYQLEAPVLRACGFDTPYPPARLEKLWLPGPDRLLDCVERVLRQP bkdB curated SwissProt::Q5SLR3 2-oxoisovalerate dehydrogenase subunit beta; Branched-chain alpha-keto acid dehydrogenase E1 component beta chain; BCKDH E1-beta; EC 1.2.4.4 MALMTMVQALNRALDEEMAKDPRVVVLGEDVGKRGGVFLVTEGLLQKYGPDRVMDTPLSEAAIVGAALGMAAHGLRPVAEIQFADYIFPGFDQLVSQVAKLRYRSGGQFTAPLVVRMPSGGGVRGGHHHSQSPEAHFVHTAGLKVVAVSTPYDAKGLLKAAIRDEDPVVFLEPKRLYRSVKEEVPEEDYTLPIGKAALRREGKDLTLIGYGTVMPEVLQAAAELAKAGVSAEVLDLRTLMPWDYEAVMNSVAKTGRVVLVSDAPRHASFVSEVAATIAEDLLDMLLAPPIRVTGFDTPYPYAQDKLYLPTVTRILNAAKRALDY bkdB curated SwissProt::Q9LDY2 2-oxoisovalerate dehydrogenase subunit beta 2, mitochondrial; Branched-chain alpha-keto acid dehydrogenase E1 component beta chain; BCKDE1B; BCKDH E1-beta; Protein DARK INDUCIBLE 4; EC 1.2.4.4 MAAALVRRFCRGSSFPVSGHGYRMLSTVENVSESGKSMNLYSAINQALHIALETDPRSYVFGEDVGFGGVFRCTTGLAERFGKSRVFNTPLCEQGIVGFGIGLAAMGNRVIAEIQFADYIFPAFDQIVNEAAKFRYRSGNQFNCGGLTIRAPYGAVGHGGHYHSQSPEAFFCHVPGIKVVIPRSPREAKGLLLSSIRDPNPVVFFEPKWLYRQAVEDVPEDDYMIPLSEAEVMREGSDITLVGWGAQLTIMEQACLDAENEGISCELIDLKTLIPWDKEIVETSVRKTGRLLISHEAPVTGGFGAEIAATIVERCFLRLEAPVSRVCGLDTPFPLVFEPFYMPTKNKILDAIRSTVNY bkdB curated metacyc::MONOMER-11684 2-keto-isovalerate dehydrogenase component β subunit (EC 1.2.4.4) MSVMSYIDAINLAMKEEMERDSRVFVLGEDVGRKGGVFKATAGLYEQFGEERVMDTPLAESAIAGVGIGAAMYGMRPIAEMQFADFIMPAVNQIISEAAKIRYRSNNDWSCPIVVRAPYGGGVHGALYHSQSVEAIFANQPGLKIVMPSTPYDAKGLLKAAVRDEDPVLFFEHKRAYRLIKGEVPADDYVLPIGKADVKREGDDITVITYGLCVHFALQAAERLEKDGISAHVVDLRTVYPLDKEAIIEAASKTGKVLLVTEDTKEGSIMSEVAAIISEHCLFDLDAPIKRLAGPDIPAMPYAPTMEKYFMVNPDKVEAAMRELAEF bkdB curated reanno::Smeli:SMc03202 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) (EC 1.2.4.4) MARMTMIEAVRSAMDVSMARDDNVVVFGEDVGYFGGVFRCTQGLQAKYGKTRCFDTPISESGIVGTAIGMAAYGLKPCVEIQFADYMYPAYDQLTQEAARIRYRSNGDFTCPIVVRMPTGGGIFGGQTHSQSPEALFTHVCGLKVVVPSNPYDAKGLLISAIEDPDPVMFLEPKRLYNGPFDGHHERPVTAWSKHELGDVPDGHYTIPIGKAEIRRKGSGVTVIAYGTMVHVALAAAEETGIDAEVIDLRSLLPLDLETIVQSAKKTGRCVVVHEATLTSGFGAELAALVQEHCFYHLESPVVRLTGWDTPYPHAQEWDYFPGPARVGRALAEAMEG bkdB curated reanno::WCS417:GFF3430 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) (EC 1.2.4.4) MNDHNNSIEVETAMTTTTMTMIQALRSAMDVMLERDDNVVVFGQDVGYFGGVFRCTEGLQTKYGSSRVFDAPISESGIVGVAVGMGAYGLRPVAEIQFADYVYPATDQIISEAARLRYRSAGQFTAPLTMRMPCGGGIYGGQTHSQSIEAVFTQVCGLRTVMPSNPYDAKGLLIASIENDDPVIFLEPKRLYNGPFDGHHDRPVTPWSKHPQAQVPDGYYTVPLDVAAIVRPGSAVTVLTYGTTVYVSQVAAEETGIDAEVIDLRSLWPLDLETIVKSVKKTGRCVVVHEATRTCGFGAELVSLVQEHCFHHLEAPIERVTGWDTPYPHAQEWAYFPGPSRVGAALKRVMEV bkdB curated reanno::pseudo13_GW456_L13:PfGW456L13_3541 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) (EC 1.2.4.4) MNDHNNNIELETAMTTTTMTMIQALRSAMDVMLERDDNVVVFGQDVGYFGGVFRCTEGLQAKYGTSRVFDAPISESGIVGTAVGMGAYGLRPVVEIQFADYVYPAYDQIISEAARLRYRSAGEFTAPMTLRMPCGGGIYGGQTHSQSIEALFTQVCGLRTVMPSNPYDAKGLLIASIENDDPVIFLEPKRLYNGPFDGHHERPVTPWSKHPAAQVPDGYYTVPLDVAAIARPGKDVTVLTYGTTVYVSQVAAEESGVDAEVIDLRSLWPLDLETITKSVKKTGRCVIVHEATRTCGFGAELTALVQEHCFHYLEAPIERVTGWDTPYPHAQEWAYFPGPSRVGAALKRVMEV bkdB curated reanno::pseudo5_N2C3_1:AO356_22985 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) (EC 1.2.4.4) MNDHNNNIALDTAMTTTTMTMIQALRSAMDVMLERDDNVVVFGQDVGYFGGVFRCTEGLQNKYGTSRVFDAPISESGIVGVAVGMGAYGLRPVAEIQFADYVYPASDQIISEAARLRYRSAGEFTAPMTLRMPCGGGIYGGQTHSQSIEAMFTQVCGLRTVMPSNPYDAKGLLIASIENDDPVIFLEPKRLYNGPFDGHHDRPVTPWSKHPSAQVPDGYYTVPLDVAAITRPGKDVTILTYGTTVYVSQVAAEETGIDAEVIDLRSLWPLDLETIVKSVKKTGRCVVVHEATRTCGFGAELVSLVQEHCFHHLEAPIERVTGWDTPYPHAQEWAYFPGPSRVGAALKRVMEV bkdB curated reanno::pseudo6_N2E2:Pf6N2E2_480 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) (EC 1.2.4.4) MNDHNTNIALDTAMTTTTMTMIQALRSAMDVMLERDDNVVVFGQDVGYFGGVFRCTEGLQNKYGTSRVFDAPISESGIVGVAVGMGAYGLRPVAEIQFADYVYPASDQIISEAARLRYRSAGEFTAPMTLRMPCGGGIYGGQTHSQSIEAMFTQVCGLRTVMPSNPYDAKGLLIASIENDDPVIFLEPKRLYNGPFDGHHDRPVTPWSKHPSAQVPDGYYTVPLDVAAITRPGKDVTVLTYGTTVYVSQVAAEETGIDAEVIDLRSLWPLDLETIVKSVKKTGRCVVVHEATRTCGFGAELVALVQEHCFHHLEAPIERVTGWDTPYPHAQEWAYFPGPSRVGAALKRVMEV bkdC curated BRENDA::P11182,SwissProt::P11182,metacyc::MONOMER-12007 dihydrolipoyllysine-residue (2-methylpropanoyl)transferase (EC 2.3.1.168);; Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial; 52 kDa mitochondrial autoantigen of primary biliary cirrhosis; Branched chain 2-oxo-acid dehydrogenase complex component E2; BCOADC-E2; Branched-chain alpha-keto acid dehydrogenase complex component E2; BCKAD-E2; BCKADE2; Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex; Dihydrolipoamide branched chain transacylase; Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase; EC 2.3.1.168;; branched-chain α-keto acid dehydrogenase complex E2 component subunit (EC 2.3.1.168) MAAVRMLRTWSRNAGKLICVRYFQTCGNVHVLKPNYVCFFGYPSFKYSHPHHFLKTTAALRGQVVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALKDSEEDVVETPAVSHDEHTHQEIKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYLEKQTGAILPPSPKVEIMPPPPKPKDMTVPILVSKPPVFTGKDKTEPIKGFQKAMVKTMSAALKIPHFGYCDEIDLTELVKLREELKPIAFARGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTFAKPVIMPPEVAIGALGSIKAIPRFNQKGEVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLLDLK bkdC curated BRENDA::Q8QHL7 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) (EC 1.2.4.4); dihydrolipoyllysine-residue (2-methylpropanoyl)transferase (EC 2.3.1.168) MAAVTRGSFTFIRRLLLAHRYKLCCSRVQTGRPDYTRHPHTVFIPQLCSSRFFHTSYVTSGPILPFKLSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKKLYYEVDATALVGTPLVDIETEPGPEVVHEEDVVETPAMSNDEHTHQEIKGHKTQATPAVRRLAMENNIKLSEVVGTGRDGRILKEDILNFLAKQTGAILPPTPFHEIQPPPPAASAPSSASMPKMKPTPSVQLPVVSRPVFTGKDSTEPLKGFHKAMVKTMTAALKIPHFGYKDEVDLTRLVQLRKELKGLSEARGVKLSYMPFFIKAASLGLLHFPILNASVDEAVQNITYKASHNIGLAMDTSQGLLVPNVKNVQLLSVFEIAVELNRMQTLGATGQLGTADLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPRFNSRDEVVKAHVMNVSWSADHRIIDGATMARFSNLWRDYLENPASMVLDLK bkdC curated BRENDA::Q98UJ6 dihydrolipoyllysine-residue (2-methylpropanoyl)transferase (EC 2.3.1.168) MAAVTTLRSSCRTAGRLVCVHHIRSCSSIRFIKSKYACVFDKSAFNFSHQQRLFRTSAVSHGQIVQFKLSDIGEGITEVTVKEWYIKEGDSVSQFDSICEVQSDKASVTITSRYDGIIRKLHYNLDEIAYVGKPLVDIEIDASKGVAPEEDVVETPAMSHEEHTHQEIKGHKTLATPAVRRLAMENNIKLSEVIGTGKDNRILKEDILSFLAKQTGAILPPSPKAEIIAPLSKSETVPTAPKDKARKIPIPISRPVVFSGKDKTEPITGFHKAMVKTMSAALKIPHFGYCDEIDLTHLVQLREELKPLAQSRGVKLSFMPFFIKAASLGLLQYPILNASLDEGCQNVTYKASHNIGVAMDTEQGLIVPNVKNVQVSSIFEIASELNRLQALGSASQLGTNDLTGGTFTLSNIGTIGGTYAKAVILPPEVAIGALGKIQVLPRFNGKGEVFKAQIMNVSWSADHRIIDGATMARFSNLWKSYLENPALMLLDLK bkdC curated SwissProt::O06159 Dihydrolipoyllysine-residue acyltransferase component of branched-chain alpha-ketoacid dehydrogenase complex; Branched-chain alpha-ketoacid dehydrogenase complex component E2; BCKADH E2; Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase; EC 2.3.1.168 MSGEDSIRSFPVPDLGEGLQEVTVTCWSVAVGDDVEINQTLCSVETAKAEVEIPSPYAGRIVELGGAEGDVLKVGAELVRIDTGPTAVAQPNGEGAVPTLVGYGADTAIETSRRTSRPLAAPVVRKLAKELAVDLAALQRGSGAGGVITRADVLAAARGGVGAGPDVRPVHGVHARMAEKMTLSHKEIPTAKASVEVICAELLRLRDRFVSAAPEITPFALTLRLLVIALKHNVILNSTWVDSGEGPQVHVHRGVHLGFGAATERGLLVPVVTDAQDKNTRELASRVAELITGAREGTLTPAELRGSTFTVSNFGALGVDDGVPVINHPEAAILGLGAIKPRPVVVGGEVVARPTMTLTCVFDHRVVDGAQVAQFMCELRDLIESPETALLDL bkdC curated SwissProt::P11181 Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial; Branched-chain alpha-keto acid dehydrogenase complex component E2; BCKAD-E2; BCKADE2; Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex; Dihydrolipoamide branched chain transacylase; Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase; EC 2.3.1.168 MAAALVLRTWSRAAGQLICVRYFQTCGNVHVLKPKYVCFFGYPPFKYSHPYQWLKTTAALQGQIVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDTAYVGKPLVDIETEALKDSEEDVVETPAVSHDEHTHQEIKGQKTLATPAVRRLAMENNIKLSEVIGSGKDGRILKEDILNYLEKQTGAILPPSPKAEIMPPPPKPKDRTIPIPISKPPVFIGKDRTEPVKGFHKAMVKTMSAALKIPHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQIRSIFEIATELNRLQKLGSAGQLSTNDLIGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGTIKALPRFNEKGEVCKAQIMNVSWSADHRIIDGATVSRFSNLWKSYLENPAFMLLDLK bkdC curated SwissProt::Q23571 Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial; Branched-chain alpha-keto acid dehydrogenase complex component E2; Dihydrolipoamide branched-chain transacylase E2; EC 2.3.1.168 MMAARLLGTSSRIFKLNKHLHTSKVAFMPVVQFKLSDIGEGIAEVQVKEWYVKEGDTISQFDKVCEVQSDKAAVTISCRYDGIVKKLYHEVDGMARVGQALIDVEIEGNVEEPEQPKKEAASSSPEAPKSSAPKAPESAHSEGKVLATPAVRRIAIENKIKLAEVRGTGKDGRVLKEDVLKFLGQVPADHTSGSTNIRTTHQAPQPSSKSYEPLKEDVAVPIRGYTRAMVKTMTEALKIPHFGYNDEINVDSLVKYRAELKEFAKERHIKLSYMPFFIKAASLALLEYPSLNSTTDEKMENVIHKASHNICLAMDTPGGLVVPNIKNCEQRSIFEIAQELNRLLEAGKKQQIKREDLIDGTFSLSNIGNIGGTYASPVVFPPQVAIGAIGKIEKLPRFDKHDNVIPVNIMKVSWCADHRVVDGATMARFSNRWKFYLEHPSAMLAQLK bkdC curated SwissProt::Q9M7Z1 Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial; Branched-chain alpha-keto acid dehydrogenase complex component E2; BCE2; BCKAD-E2; BCKADE2; Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex; Dihydrolipoamide branched chain transacylase; Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase; Protein DARK INDUCIBLE 3; EC 2.3.1.168 MIARRIWRSHRFLRPFSSSSVCSPPFRVPEYLSQSSSSPASRPFFVHPPTLMKWGGGSRSWFSNEAMATDSNSGLIDVPLAQTGEGIAECELLKWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPGDIIKVGETLVRLAVEDSQDSLLTTDSSEIVTLGGSKQGTENLLGALSTPAVRNLAKDLGIDINVITGTGKDGRVLKEDVLRFSDQKGFVTDSVSSEHAVIGGDSVSTKASSNFEDKTVPLRGFSRAMVKTMTMATSVPHFHFVEEINCDSLVELKQFFKENNTDSTIKHTFLPTLIKSLSMALTKYPFVNSCFNAESLEIILKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAANNKLNPEDVTGGTITLSNIGAIGGKFGSPLLNLPEVAIIALGRIEKVPKFSKEGTVYPASIMMVNIAADHRVLDGATVARFCCQWKEYVEKPELLMLQMR bkdC curated reanno::Marino:GFF1672 Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase (EC 2.3.1.168) MTDKAMVEITAPKAGRVTKLYHQQQAMAKVHAPLFAFIPRDREEPEEARTKPEPAAQLSTATASPVAAASRQRIPASPAVRRLVREHELNLSDIQGSGKDGRVLKADVLAYIEEGPKQAQNQAPADDAQTATTRSARRAPAADQEARVEPIRGIKAAMAKSMVKSATTIPHFIYSEDIDVTDLLKLREQLKPEAEARGSRLTLMPFFMKAMALAVQEFPVLNSQLNDDVTEIHYLPQCNIGMAVDGKAGLTVPNIKGVESLSLLGIADEVARLTEAARSGRVSQEDLKGGTITISNIGALGGTYTAPIINAPEVAIVALGRTQKLPRFDANGQVVERAIMTVSWAGDHRIIDGGTIARFCNRWKGYLESPQTMLLHMG bkdC curated reanno::Smeli:SMc03203 Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase (EC 2.3.1.168) MGEFIIKMPDVGEGVAEAELVEWHVKPGDPVREDMVLAAVMTDKATVEIPSPVTGKVLWLGAEVGDTVAVKAPLVRIETAGEAGEAAPDSIPEALAEQVLDEPVAVSSRLEAKAPPQPEKPAPKPAPAPREAPDLSAKPLASPAVRLRARESGIDLRQVAGTGPAGRITHEDLDLFISRGAEPLPAQTGLVRKTAVEEVRMIGLRRRIAEKMSLSTSRIPHITYVEEVDMTALEDLRATMNRDRKPEQAKLTILPFLMRALVKTVAEQPGVNATFDDHAGVIHRHAAVHIGIATQTPAGLTVPVVRHAEARGIWDCAAELNRLADAARTGTATRDELTGSTITISSLGAIGGIASTPVINHPEVAIVGVNKIAVRPVWDGAQFVPRKIMNLSSSFDHRVIDGWDAAVFVQRLKTLLETPALIFVEG bkdC curated reanno::pseudo13_GW456_L13:PfGW456L13_3542 Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase (EC 2.3.1.168) MGTHVIKMPDIGEGIAEVELSVWHVKVGDMVVEDQVLADVMTDKAMVDIPSPVHGKVIALGGQPGEVMAVGSVLISIEVEGAGNVKESAQPAPVVKEAPVAATKVETVVESKPVAAPAPKAAVCQGPMVAREADERPLASPAVRKHALDLGIQLRLVRGTGPAGRVLHEDLDAYLAQGQSNASAPVAAAYAQRTDEQQIPVIGMRRKIAQRMQDATQRAAHFSYVEEIDVTAVEELRAHLNEKHGATRGKLTLLPFLVRALVVALRDFPQINARYDDEAQVITRLGAVHVGIATQADIGLMVPVVRHAEARSLWDSAAEISRLATAARNGKASRDELSGSTITLTSLGALGGIVSTPVLNLPEVAIVGVNKIVERPMVIKGQIVIRKMMNLSSSFDHRVVDGMDAALFIQAIRGLLEQPATLFVE bkdC curated reanno::pseudo6_N2E2:Pf6N2E2_479 Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase (EC 2.3.1.168) MGTHVIKMPDIGEGIAEVELSVWHVKVGDMVVEDQVLADVMTDKAMVDIPSPVHGRVIALGGEPGEVMAVGSELIRIEVEGAGNLKESAQQAPTPTPAAQAPKPAPVATPEPVLEKTAAPRCAPQAPVARDPDERPLASPAVRKHALDLGIQLRLVQGSGPAGRVLHEDLEAYLAQGPSVQAKGGSGYAERHDEQQIPVIGMRRKIAQRMQEATQRAAHFSYVEEIDITALEELRVHLNEKHGASRGKLTLLPFLVRALVVALRDFPQMNARYDDEAQVIHRSGAVHVGVATQSDVGLMVPVVRHAEARSLWDNAAEISRLATAARTGKASRDELSGSTITLTSLGALGGIVSTPVLNLPEVAIVGVNKIVERPVVIKGQIVIRKMMNLSSSFDHRVVDGMDAAQFIQALRGLLEQPATLFVE bkdC curated2 O06159 Dihydrolipoyllysine-residue acyltransferase component of branched-chain alpha-ketoacid dehydrogenase complex; EC 2.3.1.168; Branched-chain alpha-ketoacid dehydrogenase complex component E2; BCKADH E2; Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase MSGEDSIRSFPVPDLGEGLQEVTVTCWSVAVGDDVEINQTLCSVETAKAEVEIPSPYAGRIVELGGAEGDVLKVGAELVRIDTGPTAVAQPNGEGAVPTLVGYGADTAIETSRRTSRPLAAPVVRKLAKELAVDLAALQRGSGAGGVITRADVLAAARGGVGAGPDVRPVHGVHARMAEKMTLSHKEIPTAKASVEVICAELLRLRDRFVSAAPEITPFALTLRLLVIALKHNVILNSTWVDSGEGPQVHVHRGVHLGFGAATERGLLVPVVTDAQDKNTRELASRVAELITGAREGTLTPAELRGSTFTVSNFGALGVDDGVPVINHPEAAILGLGAIKPRPVVVGGEVVARPTMTLTCVFDHRVVDGAQVAQFMCELRDLIESPETALLDL bkdC curated2 P09062 Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex; EC 2.3.1.168; Branched-chain alpha-keto acid dehydrogenase complex component E2; BCKAD-E2; BCKADE2; Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex; Dihydrolipoamide branched chain transacylase; Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase MGTHVIKMPDIGEGIAQVELVEWFVKVGDIIAEDQVVADVMTDKATVEIPSPVSGKVLALGGQPGEVMAVGSELIRIEVEGSGNHVDVPQAKPAEVPAAPVAAKPEPQKDVKPAAYQASASHEAAPIVPRQPGDKPLASPAVRKRALDAGIELRYVHGSGPAGRILHEDLDAFMSKPQSAAGQTPNGYARRTDSEQVPVIGLRRKIAQRMQDAKRRVAHFSYVEEIDVTALEALRQQLNSKHGDSRGKLTLLPFLVRALVVALRDFPQINATYDDEAQIITRHGAVHVGIATQGDNGLMVPVLRHAEAGSLWANAGEISRLANAARNNKASREELSGSTITLTSLGALGGIVSTPVVNTPEVAIVGVNRMVERPVVIDGQIVVRKMMNLSSSFDHRVVDGMDAALFIQAVRGLLEQPACLFVE bkdC curated2 P37942 Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex; EC 2.3.1.168; Branched-chain alpha-keto acid dehydrogenase complex component E2; BCKAD-E2; BCKADE2; Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex; Dihydrolipoamide branched chain transacylase; Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase MAIEQMTMPQLGESVTEGTISKWLVAPGDKVNKYDPIAEVMTDKVNAEVPSSFTGTITELVGEEGQTLQVGEMICKIETEGANPAEQKQEQPAASEAAENPVAKSAGAADQPNKKRYSPAVLRLAGEHGIDLDQVTGTGAGGRITRKDIQRLIETGGVQEQNPEELKTAAPAPKSASKPEPKEETSYPASAAGDKEIPVTGVRKAIASNMKRSKTEIPHAWTMMEVDVTNMVAYRNSIKDSFKKTEGFNLTFFAFFVKAVAQALKEFPQMNSMWAGDKIIQKKDINISIAVATEDSLFVPVIKNADEKTIKGIAKDITGLAKKVRDGKLTADDMQGGTFTVNNTGSFGSVQSMGIINYPQAAILQVESIVKRPVVMDNGMIAVRDMVNLCLSLDHRVLDGLVCGRFLGRVKQILESIDEKTSVY brnQ curated TCDB::P0AD99,ecocyc::BRNQ-MONOMER,metacyc::BRNQ-MONOMER Branched chain amino acid transporter 2 of 439 aas and 12 TMSs, BrnQ;; branched chain amino acid transporter BrnQ;; branched chain amino acid transporter BrnQ MTHQLRSRDIIALGFMTFALFVGAGNIIFPPMVGLQAGEHVWTAAFGFLITAVGLPVLTVVALAKVGGGVDSLSTPIGKVAGVLLATVCYLAVGPLFATPRTATVSFEVGIAPLTGDSALPLFIYSLVYFAIVILVSLYPGKLLDTVGNFLAPLKIIALVILSVAAIVWPAGSISTATEAYQNAAFSNGFVNGYLTMDTLGAMVFGIVIVNAARSRGVTEARLLTRYTVWAGLMAGVGLTLLYLALFRLGSDSASLVDQSANGAAILHAYVQHTFGGGGSFLLAALIFIACLVTAVGLTCACAEFFAQYVPLSYRTLVFILGGFSMVVSNLGLSQLIQISVPVLTAIYPPCIALVVLSFTRSWWHNSSRVIAPPMFISLLFGILDGIKASAFSDILPSWAQRLPLAEQGLAWLMPTVVMVVLAIIWDRAAGRQVTSSAH brnQ curated TCDB::P19072 Branched chain amino acid: Na+ symporter MTHLKGFDLLALGFMTFALFLGAGNIIFPPSAGMAAGEHVWSAAFGFLLTGVGLPLLTVVALARVGGGIGRLTQPIGRRAGVAFAIAVYLAIGPLFATPRTAVVSFEMGVAPFTGDGGVPLLIYTVAYFSVVLFLVLNPGRLVDRVGKVITPVLLSALLVLGGAAIFAPAGEIGSSSGEYQSAPLVQGFLQGYLTMDTLGALVFGIVIATAIRDRGISDSRLVTRYSMIAGVIAATGLSLVYLALFYLGATSQGIAGDAQNGVQILTAYVQQTFGVSGSLLLAVVITLACLTTAVGLITACGEFFSDLLPVSYKTVVIVFSLFSLLVANQGLTQLISLSVPVLVGLYPLAIVLIALSLFDRLWVSAPRVFVPVMIVALLFGIVDGLGAAKLNGWVPDVFAKLPLADQSLGWLLPVSIALVLAVVCDRLLGKPREAVA ilvE hmm TIGR01122 ilvE: branched-chain amino acid aminotransferase (EC 2.6.1.42) TIGR01122.hmm ilvE hmm TIGR01123 ilvE: branched-chain amino acid aminotransferase (EC 2.6.1.42) TIGR01123.hmm ilvE curated BRENDA::A0A060PQX5 branched-chain-amino-acid transaminase (EC 2.6.1.42) MELEKRLKEKLEAPTLDYEKYFSKKALGMKASEVRELLKLVESSDVISLAGGLPAPETFPVEIIAEITKEVLEKHAAQALQYGTTKGFTPLRLALAEWMRKRYDIPISKVDIMITSGSQQALDLIGRVFINPGDIVVVEAPTYLAALQAFKYYEPEFVQIPLDDEGMRVDLLEEKLQELEKEGKKVKLVYTIPTFQNPAGVTMSEKRRKRLLELASEYDFLIVEDNPYGELRYSGEPVKPIKAWDDEGRVMYLGTFSKILAPGFRIGWIAAEPHLIRKLEIAKQSVDLCTNPFSQVIAWKYVEGGHLDNHIPNIIEFYKPRRDAMLKALEEFMPEGVRWTKPEGGMFVWVTLPEGIDTKLMLEKAVAKGVAYVPGEAFFAHRDVKNTMRLNFTYVPEEKIREGIKRLAETIKEEMKK ilvE curated BRENDA::A0R066,SwissProt::A0R066 branched-chain-amino-acid transaminase (EC 2.6.1.42);; Branched-chain-amino-acid aminotransferase; BCAT; EC 2.6.1.42 MNSGPLEFTVSANTNPATDAVRESILANPGFGKYYTDHMVSIDYTVDEGWHNAQVIPYGPIQLDPSAIVLHYGQEIFEGLKAYRWADGSIVSFRPEANAARLQSSARRLAIPELPEEVFIESLRQLIAVDEKWVPPAGGEESLYLRPFVIATEPGLGVRPSNEYRYLLIASPAGAYFKGGIKPVSVWLSHEYVRASPGGTGAAKFGGNYAASLLAQAQAAEMGCDQVVWLDAIERRYVEEMGGMNLFFVFGSGGSARLVTPELSGSLLPGITRDSLLQLATDAGFAVEERKIDVDEWQKKAGAGEITEVFACGTAAVITPVSHVKHHDGEFTIADGQPGEITMALRDTLTGIQRGTFADTHGWMARLN ilvE curated BRENDA::B6RFK8 branched-chain-amino-acid transaminase (EC 2.6.1.42) MESAAVFAGLQPNPGHYHQLLAPSRSAIKLLPPPLTDKHNFCPLPLKLQKQSHYASYINNNTINNGNTLRVASPASNITSELADIDWDNLGFGFMPTDYMYVMKCSQGENFSKGELQRFGNIELSPSAGILNYGQGLFEGLKAYRKHDGNILLFRPEENAMRLKMGAERMCMPLPSVEQFVEAVKATVLANERWIPPSGKGSLYIRPLLMGSGAVLGLAPAPEYTFLIYVSPVGNYFKEGLAPINLVVETEMHRATPGGTGGVKTVGNYAAVLKAQSAAKAKGYSDVLYLDSVQKRYLEEVSSCNVFIVKGNLIVTPAIKGTILPGITRKSIIDVALSQGFEVEERLVSVDELLDADEVFCTGTAVVVSPVGSITHQGKRVTYGNNGVGIVSQQLYSALTSLQMGLAKDKMGWIVELK ilvE curated BRENDA::F2L0W0 branched-chain-amino-acid transaminase (EC 2.6.1.42) MKVWLDGRLVDEEEAKVTVLSPSLNYGFGVFEGIRAYWNGENLYVFRLRDHMERLLRSAKIIGLDVPYTAEELSKAVVETVRANGFKEDLYIRPVAYISKPQISLDVRGLQASVAIAAIPFGKYLKVEGVRAAVVSWRRVHTSMMPVMAKATGIYLNSIMAAVEARARGYDEAIMLNAEGKVVEGSGENIFIVRRGVLMTPPLEDGILEGITRETVISIAGDLGIPLLEKSITREELYAADEAFFVGTAAEITPIIEIDGRVLQRGPITQKIAETYRRIVLGKEEKYLPWLTPVY ilvE curated BRENDA::O15382,SwissProt::O15382 branched-chain-amino-acid transaminase (EC 2.6.1.42);; Branched-chain-amino-acid aminotransferase, mitochondrial; BCAT(m); Placental protein 18; PP18; EC 2.6.1.42 MAAAALGQIWARKLLSVPWLLCGPRRYASSSFKAADLQLEMTQKPHKKPGPGEPLVFGKTFTDHMLMVEWNDKGWGQPRIQPFQNLTLHPASSSLHYSLQLFEGMKAFKGKDQQVRLFRPWLNMDRMLRSAMRLCLPSFDKLELLECIRRLIEVDKDWVPDAAGTSLYVRPVLIGNEPSLGVSQPTRALLFVILCPVGAYFPGGSVTPVSLLADPAFIRAWVGGVGNYKLGGNYGPTVLVQQEALKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGVLELVTPPLNGVILPGVVRQSLLDMAQTWGEFRVVERTITMKQLLRALEEGRVREVFGSGTACQVCPVHRILYKDRNLHIPTMENGPELILRFQKELKEIQYGIRAHEWMFPV ilvE curated BRENDA::O35855 branched-chain-amino-acid transaminase (EC 2.6.1.42) MAAATLGQVWARKLLPVPWLLCGSKRCVSSIFKAADLQIQMTKEPQKKPAPSQALLFGKTFTDHMLMVEWNNKAGWGPPRIQPFQNLTLHPACSGLHYSLQLFEGLKAYKGGDQQVRLFRPWLNMDRMLRSARRLCLPDFDKQELLECIRQLIEVDKDWVPDGNGTSLYVRPVLIGNEPSLGVGMVTQALLYVILCPVGSYFPGDSMTPVSLLADPSFVRAWIGGVGDCKLGGNYGPTVAVQREAQKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGVLELVTPPLNGVILPGVVRQSLLDLARTWGEFRVAERKVTMKELKRALEEGRVREVFGSGTACQVCPVHQILYEGKQLHIPTMENGPELILRFQKELKAIQYGASAHDWMFRV ilvE curated BRENDA::P0AB80,CharProtDB::CH_024500,ecocyc::BRANCHED-CHAINAMINOTRANSFER-MONOMER,metacyc::BRANCHED-CHAINAMINOTRANSFER-MONOMER branched-chain-amino-acid transaminase (EC 2.6.1.42);; branched-chain-amino-acid aminotransferase; EC 2.6.1.42;; branched-chain-amino-acid aminotransferase (EC 2.6.1.1; EC 2.6.1.57; EC 2.6.1.27; EC 2.6.1.42; EC 2.6.1.6);; branched-chain-amino-acid aminotransferase (EC 2.6.1.1; EC 2.6.1.42; EC 2.6.1.6) MTTKKADYIWFNGEMVRWEDAKVHVMSHALHYGTSVFEGIRCYDSHKGPVVFRHREHMQRLHDSAKIYRFPVSQSIDELMEACRDVIRKNNLTSAYIRPLIFVGDVGMGVNPPAGYSTDVIIAAFPWGAYLGAEALEQGIDAMVSSWNRAAPNTIPTAAKAGGNYLSSLLVGSEARRHGYQEGIALDVNGYISEGAGENLFEVKDGVLFTPPFTSSALPGITRDAIIKLAKELGIEVREQVLSRESLYLADEVFMSGTAAEITPVRSVDGIQVGEGRCGPVTKRIQQAFFGLFTGETEDKWGWLDQVNQ ilvE curated BRENDA::P38891,SwissProt::P38891,metacyc::YHR208W-MONOMER branched-chain-amino-acid transaminase (EC 2.6.1.42);; Branched-chain-amino-acid aminotransferase, mitochondrial; BCAT; Protein ECA39; Protein TWT1; EC 2.6.1.42;; branched-chain amino acid aminotransferase subunit (EC 2.6.1.42; EC 2.6.1.6) MLQRHSLKLGKFSIRTLATGAPLDASKLKITRNPNPSKPRPNEELVFGQTFTDHMLTIPWSAKEGWGTPHIKPYGNLSLDPSACVFHYAFELFEGLKAYRTPQNTITMFRPDKNMARMNKSAARICLPTFESEELIKLTGKLIEQDKHLVPQGNGYSLYIRPTMIGTSKGLGVGTPSEALLYVITSPVGPYYKTGFKAVRLEATDYATRAWPGGVGDKKLGANYAPCILPQLQAAKRGYQQNLWLFGPEKNITEVGTMNVFFVFLNKVTGKKELVTAPLDGTILEGVTRDSVLTLARDKLDPQEWDINERYYTITEVATRAKQGELLEAFGSGTAAVVSPIKEIGWNNEDIHVPLLPGEQCGALTKQVAQWIADIQYGRVNYGNWSKTVADLN ilvE curated BRENDA::P47176,SwissProt::P47176 branched-chain-amino-acid transaminase (EC 2.6.1.42);; Branched-chain-amino-acid aminotransferase, cytosolic; BCAT; Protein TWT2; EC 2.6.1.42 MTLAPLDASKVKITTTQHASKPKPNSELVFGKSFTDHMLTAEWTAEKGWGTPEIKPYQNLSLDPSAVVFHYAFELFEGMKAYRTVDNKITMFRPDMNMKRMNKSAQRICLPTFDPEELITLIGKLIQQDKCLVPEGKGYSLYIRPTLIGTTAGLGVSTPDRALLYVICCPVGPYYKTGFKAVRLEATDYATRAWPGGCGDKKLGANYAPCVLPQLQAASRGYQQNLWLFGPNNNITEVGTMNAFFVFKDSKTGKKELVTAPLDGTILEGVTRDSILNLAKERLEPSEWTISERYFTIGEVTERSKNGELLEAFGSGTAAIVSPIKEIGWKGEQINIPLLPGEQTGPLAKEVAQWINGIQYGETEHGNWSRVVTDLN ilvE curated BRENDA::P54687 branched-chain-amino-acid transaminase (EC 2.6.1.42) MKDCSNGCSAECTGEGGSKEVVGTFKAKDLIVTPATILKEKPDPNNLVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRMYRSAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGTFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYGEDHQITEVGTMNLFLYWINEDGEEELATPPLDGIILPGVTRRCILDLAHQWGEFKVSERYLTMDDLTTALEGNRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPKLASRILSKLTDIQYGREESDWTIVLS ilvE curated BRENDA::P54691 branched-chain-amino-acid transaminase (EC 2.6.1.42); glutamate-prephenate aminotransferase (EC 2.6.1.79) MHKFLPIAYFEDKFVPFEDAKISVATHALHYGTAAFGGLRGIPDPEDPGTILLFRLDRHGDRLSKSAKFLHYDISAEKIKEVIVDFVKKNQPDKSFYIRPLVYSSGLGIAPRLHNLEKDFLVYGLEMGDYLAADGVSCRISSWYRQEDRSFPLRGKISAAYITSALAKTEAVESGFDEAILMNSQGKVCEATGMNVFMVRNGQIVTPGNEQDILEGITRDSILTIAADLGIPTCQRPIDKSELMIADEVFLSGTAAKITPVKRIENFTLGGDRPITEKLRSVLTAVTENREPKYQDWVFKIPLNG ilvE curated BRENDA::P9WQ75,SwissProt::P9WQ75 branched-chain-amino-acid transaminase (EC 2.6.1.42);; Branched-chain-amino-acid aminotransferase; BCAT; EC 2.6.1.42 MTSGSLQFTVLRAVNPATDAQRESMLREPGFGKYHTDHMVSIDYAEGRGWHNARVIPYGPIELDPSAIVLHYAQEVFEGLKAYRWADGSIVSFRADANAARLRSSARRLAIPELPDAVFIESLRQLIAVDKAWVPGAGGEEALYLRPFIFATEPGLGVRPATQYRYLLIASPAGAYFKGGIAPVSVWVSTEYVRACPGGTGAAKFGGNYAASLLAQAEAAENGCDQVVWLDAVERRYIEEMGGMNIFFVLGSGGSARLVTPELSGSLLPGITRDSLLQLAIDAGFAVEERRIDIDEWQKKAAAGEITEVFACGTAAVITPVARVRHGASEFRIADGQPGEVTMALRDTLTGIQRGTFADTHGWMARLG ilvE curated BRENDA::Q0E9S8 branched-chain-amino-acid transaminase (EC 2.6.1.42) MADLENLDWKNLGFSYIKTDFRFIATYKNGSWSQGELVSENVLQLSEGSPVLHYGQACFEGLKAYRSQKGKALLFRPLENAKRLQTSCERLLMPKVSEELFLKACAEVVKANQKWLAPYKSGASLYLRPFVIGVGDNLGVKPANEYLFIVFCAPVGAYFKGGIEKGGARFITTIFDRAAPKGTGGVKVGGNYAASLLAHKMAIEQGYDDCIYLDPATHTKIEEVGAANFFGITHDDAFITPHSPSILPSITKKSLMVLAKEHLELKVEEREILMDELGAFKEAGACGTAAIITPIKEIAHNNKSYFFEAPGHITKRLYDLLLSIQQGEQEAPKDWIFEVG ilvE curated BRENDA::Q70KX9 branched-chain-amino-acid transaminase (EC 2.6.1.42) MAVLSSAKRVLPCASAGGVSGGLRALLGTDGGGRSLLPSRWKSSLPQLDPVDRSDEESGGDIDWDNLGFGLTPTDYMYVMRCSREEGGFSRGELARYGNIELSPSSGVLNYGQGLFEGLKAYRRSDGAGYMLFRPEENARRMQHGAGRMCMPSPSVEQFVHAVKQTVLANRRWVPPQGKGALYIRPLLIGSGAILGLAPAPEYTFMIYAAPVGTYFKEGMAAINLLVEEEIHRAMPGGTGGVKTISNYAPVLKPQMDAKSKGFADVLYLDAVHKRYVEEASSCNLFVVKGGAVATPATTAGTILPGVTRRSIIELARDDGYQVEERLVSIDDLVGADEVFCTGTAVGVTPVSTITYQGTRHEFRTGEDTLSRKLYTTLTSIQMGLAEDKKGWTVAID ilvE curated BRENDA::Q7BPX6 branched-chain-amino-acid transaminase (EC 2.6.1.42) MAINLDWENLGFSYRNLPFRYIARFKDGKWSAGELTGDNQLHISESSPALHYGQQGFEGLKAYRTKDGSIQLFRPDQNAARLQKTARRLCMAEVSTEMFIDAVKQVVKANKDFVPPYGTGATLYLRPLLIGVGDVIGVKPADEYIFKVFAMPVGSYFKGGLAPSKFVISREYDRAAPLGTGGAKVGGNYAASLQAEVGAKASGYADAIYLDPSTHTKIEEVGAANFFGITADNEFITPLSPSILPSITKYSLLYLAEHRLGLKAIEGEVYAKDLGKFVEAGACGTAAIISPIGRIDDGEDSYIFHSETEVGPTVKRLYDELVGIQFGDVEAPEGWIVKVD ilvE curated BRENDA::Q8DTW7 branched-chain-amino-acid transaminase (EC 2.6.1.42) MTVDLDWKNLGFEYHKLPFRYISYYKDGKWDDGKLTEDATLHISESSPALHYGQEAFEGLKAYRTKDGSVQLFRPNMNAERLQRTADRLLMPQVPTDKFIDAAKQVVRANEEYVPPYGTGATLYLRPLLIGVGDVIGVHPADEYIFTIFAMPVGNYFKGGLAPTNFLIQDDYDRAAPHGTGAAKVGGNYAASLLPGKVAHERQFSDVIYLDPATHTKIEEVGSANFFGITKDNEFITPLSPSILPSVTKYSLLYLAEHRFGMKAIEGDVCVDELDKFVEAGACGTAAVISPIGGVQHGDDFHVFYSETEVGPVTHKLYDELTGIQFGDVKAPEGWIYKVDD ilvE curated BRENDA::Q93Y32 branched-chain-amino-acid transaminase (EC 2.6.1.42) MALRRCLPQYSTTSSYLSKIWGFRMHGTKAAASVVEEHVSGAEREDEEYADVDWDNLGFSLVRTDFMFATKSCRDGNFEQGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEDGRVLLFRPELNAMRMKIGAERMCMHSPSVHQFIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAASEYTFLVFGSPVQNYFKEGTAALNLYVEEVIPRAYLGGTGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTGKNIEEVSAANIFLVKGNTIVTPATSGTILGGITRKSIIEIALDLGYKVEERSVPVEELKEAEEVFCTGTAAGVASVGSITFKNTRTEYKVGDGIVTQQLRSILVGIQTGSIQDTKDWVLQIA ilvE curated BRENDA::Q9FYA6 branched-chain-amino-acid transaminase (EC 2.6.1.42) MERSAVASGFHRNYILCASRAATSTTRLHSLSSLRNFPSSSLRIRHCPSPISSNFIVSEVSRNRRCDAVSSSTTDVTELAEIDWDKIDFGLKPTDYMYAMKCSRDGEFSQGQLQPFGNIDINPAAGVLNYGQGLFEGLKAYRKQDGNILLFRPEENAIRMRNGAERMCMPSPTVEQFVEAVKTTVLANKRWIPPPGKGSLYIRPLLMGTGAVLGLAPAPEYTFLIFVSPVGNYFKEGVAPINLIVETEFHRATPGGTGGVKTIGNYAAVLKAQSIAKAKGYSDVLYLDCLHKRYLEEVSSCNIFIVKDNVISTPEIKGTILPGITRKSIIEVARSQGFKVEERNVTVDELVEADEVFCTGTAVVLSPVGSITYKSQRFSYGEDGFGTVSKQLYTSLTSLQMGLSEDNMNWTVQLS ilvE curated BRENDA::Q9LE06,SwissProt::Q9LE06,metacyc::AT3G19710-MONOMER branched-chain-amino-acid transaminase (EC 2.6.1.42); methionine transaminase (EC 2.6.1.88);; Methionine aminotransferase BCAT4; Branched-chain-amino-acid aminotransferase 4; Atbcat-4; Methionine-oxo-acid transaminase BCAT4; EC 2.6.1.88;; methionine transaminase (EC 2.6.1.88) MAPSAQPLPVSVSDEKYANVKWEELAFKFVRTDYMYVAKCNHGESFQEGKILPFADLQLNPCAAVLQYGQGLYEGLKAYRTEDGRILLFRPDQNGLRLQAGADRLYMPYPSVDQFVSAIKQVALANKKWIPPPGKGTLYIRPILFGSGPILGSFPIPETTFTAFACPVGRYHKDNSGLNLKIEDQFRRAFPSGTGGVKSITNYCPVWIPLAEAKKQGFSDILFLDAATGKNIEELFAANVFMLKGNVVSTPTIAGTILPGVTRNCVMELCRDFGYQVEERTIPLVDFLDADEAFCTGTASIVTSIASVTFKDKKTGFKTGEETLAAKLYETLSDIQTGRVEDTKGWTVEIDRQG ilvE curated BRENDA::Q9LPM9 branched-chain-amino-acid transaminase (EC 2.6.1.42) MAPSSSPLRTTSETDEKYANVKWEELGFALTPIDYMYVAKCRQGESFTQGKIVPYGDISISPCSPILNYGQGLFEGLKAYRTEDDRIRIFRPDQNALRMQTGAERLCMTPPTLEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLLGSGATLGVAPAPEYTFLIYASPVGDYHKVSSGLNLKVDHKYHRAHSGGTGGVKSCTNYSPVVKSLLEAKSAGFSDVLFLDAATGRNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVFCTGTAVVVKAVETVTFHDKKVKYRTGEAALSTKLHSMLTNIQMGVVEDKKGWMVDIDPCQG ilvE curated BRENDA::Q9M401,SwissProt::Q9M401,metacyc::AT3G49680-MONOMER branched-chain-amino-acid transaminase (EC 2.6.1.42);; Branched-chain-amino-acid aminotransferase 3, chloroplastic; Atbcat-3; EC 2.6.1.42; EC 2.6.1.88;; branched-chain aminotransferase MERAAILPSVNQNYLLCPSRAFSTRLHSSTRNLSPPSFASIKLQHSSSSVSSNGGISLTRCNAVSSNSSSTLVTELADIDWDTVGFGLKPADYMYVMKCNIDGEFSKGELQRFGNIEISPSAGVLNYGQGLFEGLKAYRKKDGNNILLFRPEENAKRMRNGAERMCMPAPTVEQFVEAVTETVLANKRWVPPPGKGSLYVRPLLMGTGAVLGLAPAPEYTFIIYVSPVGNYFKEGVAPINLIVENEFHRATPGGTGGVKTIGNYAAVLKAQSIAKAKGYSDVLYLDCIYKRYLEEVSSCNIFIVKDNVISTPEIKGTILPGITRKSMIDVARTQGFQVEERNVTVDELLEADEVFCTGTAVVVSPVGSVTYKGKRVSYGEGTFGTVSKQLYTVLTSLQMGLIEDNMKWTVNLS ilvE curated BRENDA::Q9M439,SwissProt::Q9M439 branched-chain-amino-acid transaminase (EC 2.6.1.42);; Branched-chain-amino-acid aminotransferase 2, chloroplastic; Atbcat-2; EC 2.6.1.42 MIKTITSLRKTLVLPLHLHIRTLQTFAKYNAQAASALREERKKPLYQNGDDVYADLDWDNLGFGLNPADYMYVMKCSKDGEFTQGELSPYGNIQLSPSAGVLNYGQAIYEGTKAYRKENGKLLLFRPDHNAIRMKLGAERMLMPSPSVDQFVNAVKQTALANKRWVPPAGKGTLYIRPLLMGSGPILGLGPAPEYTFIVYASPVGNYFKEGMAALNLYVEEEYVRAAPGGAGGVKSITNYAPVLKALSRAKSRGFSDVLYLDSVKKKYLEEASSCNVFVVKGRTISTPATNGTILEGITRKSVMEIASDQGYQVVEKAVHVDEVMDADEVFCTGTAVVVAPVGTITYQEKRVEYKTGDESVCQKLRSVLVGIQTGLIEDNKGWVTDIN ilvE curated BRENDA::Q9RTX5 branched-chain-amino-acid transaminase (EC 2.6.1.42) MRLTILGMTAHDSRPEQAKKLADIDWSTLGFSYIRTDLRYLAHWKDGEWDAGTLTEDNQIHLAEGSTALHYGQQCFEGLKAYRCADGSINLFRPDQNAARMRMSCRRLLMPELSDEQFIDACLQVVRANEHFLPPYGTGGSLYLRPFVIGVGDNIGVRTAPEFIFSVFCVPVGPYFKGGLTPTNFITSDYDRAAPHGTGAAKVGGNYAASLLPGYEAKKRDFADVIYLDPATHTTIEEAGAANFFAITQDGQKFVTPQSPSILPSITKYSLLWLAEHRLGLEVEEGDIRIDELGKFSEAGACGTAAVITPIGGIQHGDDFHVFYSESEPGPVTRRLYDELVGIQYGDKEAPEGWIVKV ilvE curated BRENDA::Q9S7N2,SwissProt::Q9S7N2,metacyc::AT1G70560-MONOMER tryptophan transaminase (EC 2.6.1.27); L-tryptophan-pyruvate aminotransferase (EC 2.6.1.99);; L-tryptophan--pyruvate aminotransferase 1; Protein CYTOKININ INDUCED ROOT CURLING 1; Protein SHADE AVOIDANCE 3; Protein TRANSPORT INHIBITOR RESPONSE 2; Protein TRYPTOPHAN AMINOTRANSFERASE OF ARABIDOPSIS 1; Protein WEAK ETHYLENE INSENSITIVE 8; Tryptophan transaminase; EC 2.6.1.27; EC 2.6.1.99;; tryptophan aminotransferase (EC 2.6.1.1; EC 2.6.1.58; EC 2.6.1.2; EC 2.6.1.6; EC 2.6.1.27; EC 2.6.1.99) MVKLENSRKPEKISNKNIPMSDFVVNLDHGDPTAYEEYWRKMGDRCTVTIRGCDLMSYFSDMTNLCWFLEPELEDAIKDLHGVVGNAATEDRYIVVGTGSTQLCQAAVHALSSLARSQPVSVVAAAPFYSTYVEETTYVRSGMYKWEGDAWGFDKKGPYIELVTSPNNPDGTIRETVVNRPDDDEAKVIHDFAYYWPHYTPITRRQDHDIMLFTFSKITGHAGSRIGWALVKDKEVAKKMVEYIIVNSIGVSKESQVRTAKILNVLKETCKSESESENFFKYGREMMKNRWEKLREVVKESDAFTLPKYPEAFCNYFGKSLESYPAFAWLGTKEETDLVSELRRHKVMSRAGERCGSDKKHVRVSMLSREDVFNVFLERLANMKLIKSIDL ilvE curated CharProtDB::CH_004054,SwissProt::P04693,ecocyc::TYRB-MONOMER,metacyc::TYRB-MONOMER aromatic-amino-acid transaminase TyrB; EC 2.6.1.57;; Aromatic-amino-acid aminotransferase; ARAT; AROAT; Beta-methylphenylalanine transaminase; EC 2.6.1.57; EC 2.6.1.107;; tyrosine aminotransferase (EC 2.6.1.57; EC 2.6.1.6; EC 2.6.1.42; EC 2.6.1.27; EC 2.6.1.5; EC 2.6.1.1);; tyrosine aminotransferase (EC 2.6.1.57; EC 2.6.1.6; EC 2.6.1.27; EC 2.6.1.1) MFQKVDAYAGDPILTLMERFKEDPRSDKVNLSIGLYYNEDGIIPQLQAVAEAEARLNAQPHGASLYLPMEGLNCYRHAIAPLLFGADHPVLKQQRVATIQTLGGSGALKVGADFLKRYFPESGVWVSDPTWENHVAIFAGAGFEVSTYPWYDEATNGVRFNDLLATLKTLPARSIVLLHPCCHNPTGADLTNDQWDAVIEILKARELIPFLDIAYQGFGAGMEEDAYAIRAIASAGLPALVSNSFSKIFSLYGERVGGLSVMCEDAEAAGRVLGQLKATVRRNYSSPPNFGAQVVAAVLNDEALKASWLAEVEEMRTRILAMRQELVKVLSTEMPERNFDYLLNQRGMFSYTGLSAAQVDRLREEFGVYLIASGRMCVAGLNTANVQRVAKAFAAVM ilvE curated CharProtDB::CH_012531 branched-chain amino acid aminotransferase 2; EC 2.6.1.42 MNEQWIFLNGEFVPKDEAKVSVYDHGYLYGDGVFEGIRVYSGNVFRLREHLVRLYESAKSIMLEIPYSLDEITNIVVETIRQNKLSNGYIRLVVSRGAGNLGLDPDSCTKPNVVVIAEQLSLFPQEYYEKGIPVVTVATRRNRPDVLSPQVKSLNYLNNILVRIEAKLAGVQEALMLNDQGYVAEGSGDNVFIVKGNKLITPPSSAGALEGITRNAILEIGEKLGYDVREELFTRHDVYVADEVFLTGTAAEVIAVTTVDGRTIGLGQTGPHTNRLLEEFRKLVIEDGEKIYEENKVG ilvE curated CharProtDB::CH_124663 branched chain amino acid aminotransferase Eca39; EC 2.6.1.42 MVQTAALHGPKPMDSSHIKVTNVKELKPLPEWKSLKFGENFTDHMLIMKWNREKGWSTPEIVPFGKLCFHPASSVFHYGFECFEGMKAFRDEKGVPRLFRPIKNAERMLSTGTRISLPSFDPAELAEIIRKFVAHENRWVPDQRGYSLYIRPTFIGTDEALGVHHCDNAMLYVIASPVGPYYSSGFKAVKLCCSEESVRAWPGGTGHYKLGGNYAPSVLPQKEAAKKGYAQILWLYGDEDYITEVGTMNCFTVWINKNGEKEIITAPLDGMILPGVTRDSILEICRERLAPKGWKITEGKYSMKEVAQASKEGRLLEVFGAGTAALVSPVKAINYKGTEYEIPMPEGQEAGPITSEISKWILDIQYGKEPNNPWSVPALP ilvE curated SwissProt::K7QHS5 Branched-chain amino acid aminotransferase 2, chloroplastic; HlBCAT2; EC 2.6.1.42 MDCAAALLPGFHPNYLLCPSRHFSSLLPKTDLSSPLKFQLQNKQLSLASSHGFSPVICNATLSDTYSETVELADIDWDNLGFGFLPTDYMYNMKCAQGESFSNGELQRFGNIELSPSAGVLNYGQGLFEGLKAYRKEDGNILLFRPEENALRMRLGAERMCMPSPTVDQFVDAVKATVLANKRWIPPVGKGSLYIRPLLMGSGAVLGLAPAPEYTFLIYVSPVGNYFKEGVAPIHLIVEDNLHRATPGGTGGVKTIGNYAAVLKAQSAAKEQGYSDVLYLDCVHKKYLEEVSSCNIFVVKGNLIFTPAIKGTILPGITRKSIIDVARTLGFQVEERLVHVDELLDADEVFCTGTAVVVSPVGSITYHGERVPYNEGGVGAVSQQLYSALTRLQMGFIKDNMNWTVELS ilvE curated SwissProt::K7QKH1 Branched-chain amino acid aminotransferase 1, mitochondrial; HlBCAT1; EC 2.6.1.42 MIHRGLWLHNLVQSYRVGSSSSSSTLFKLVYRYNSSTSLAKSSLKQSCELSCKSNTEPSNMDWDKLGFKLMPTDYVYSMKCSNEGNFEQGRLELHGNIELSPAAAVLNYGQGIFEGTKAYRKEDGSLLLFRPDQNGVRMRIGAERMCMPSPSVDQFVDAVKQTAIANRRWVPPSGKGSLYIRPLLMGTGAVLGVAPAPQYTFLAYASPVGNYFKEGLAPLRLYVEDEFDRASPGGTGFVKTIGNYSRCLAALSRAKNKGFSDVLFLDSVHKKYVEELSSCNIFIVQGNQISTPAANGTILSGVTRSSIIEIARDHGFKVEERKIAVDELMEAEEVFCTGTAVGVASVGSITYHNKRVEFKTGSQSVSQKFYSTLIGIQTGVVEDKKGWIVEID ilvE curated SwissProt::O14370,BRENDA::O14370 Branched-chain-amino-acid aminotransferase, mitochondrial; BCAT; EC 2.6.1.42;; branched-chain-amino-acid transaminase (EC 2.6.1.42) MSLMFLRRAGNIKGRNIRFALQRGSVGYSQQSSEACKNFLNTTQLRTMVQTAALHGPKPMDSSHIKVTNVKELKPLPEWKSLKFGENFTDHMLIMKWNREKGWSTPEIVPFGKLCFHPASSVFHYGFECFEGMKAFRDEKGVPRLFRPIKNAERMLSTGTRISLPSFDPAELAEIIRKFVAHENRWVPDQRGYSLYIRPTFIGTDEALGVHHCDNAMLYVIASPVGPYYSSGFKAVKLCCSEESVRAWPGGTGHYKLGGNYAPSVLPQKEAAKKGYAQILWLYGDEDYITEVGTMNCFTVWINKNGEKEIITAPLDGMILPGVTRDSILEICRERLAPKGWKITEGKYSMKEVAQASKEGRLLEVFGAGTAALVSPVKAINYKGTEYEIPMPEGQEAGPITSEISKWILDIQYGKEPNNPWSVPALP ilvE curated SwissProt::O31461 Branched-chain-amino-acid transaminase 1; BCAT 1; EC 2.6.1.42 MNKLIEREKTVYYKEKPDPSSLGFGQYFTDYMFVMDYEEGIGWHHPRIAPYAPLTLDPSSSVFHYGQAVFEGLKAYRTDDGRVLLFRPDQNIKRLNRSCERMSMPPLDEELVLEALTQLVELEKDWVPKEKGTSLYIRPFVIATEPSLGVKASRSYTFMIVLSPVGSYYGDDQLKPVRIYVEDEYVRAVNGGVGFAKTAGNYAASLQAQRKANELGYDQVLWLDAIEKKYVEEVGSMNIFFVINGEAVTPALSGSILSGVTRASAIELIRSWGIPVREERISIDEVYAASARGELTEVFGTGTAAVVTPVGELNIHGKTVIVGDGQIGDLSKKLYETITDIQLGKVKGPFNWTVEV ilvE curated SwissProt::O35854 Branched-chain-amino-acid aminotransferase, mitochondrial; BCAT(m); EC 2.6.1.42 MSAAILGQVWTRKLLPIPWRLCVPGRCVSSNFKAADLQVQVTREPQKKPAPSQPLLFGKTFTDHMLMVEWNSKTGWGPPRIQPFQNLTLHPACSGLHYSLQLFEGLKAYKGRDKQVRLFRPWLNMDRMLRSARRLCLPDFDKQELLECIRQLIEVDKDWVPDGNGTSLYVRPVLIGNEPSLGVGMVTQALLFVILCPVGSYFPGDSMTPVSLLADPSFVRAWIGGVGDCKLGGNYGPTVAVQQEAQKKGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGELELATPPLDGIILPGVVRQSLLDLARTWGEFRVAERKVTMKELKRALEEGRVREVFGSGTACQVCPVHQILYEGKQLHIPTMENGPELILRFQKELKAIQYGTSAHDWMLRV ilvE curated SwissProt::P39576 Branched-chain-amino-acid aminotransferase 2; BCAT 2; Vegetative protein 85; VEG85; EC 2.6.1.42 MTKQTIRVELTSTKKPKPDPNQLSFGRVFTDHMFVMDYAADKGWYDPRIIPYQPLSMDPAAMVYHYGQTVFEGLKAYVSEDDHVLLFRPEKNMERLNQSNDRLCIPQIDEEQVLEGLKQLVAIDKDWIPNAEGTSLYIRPFIIATEPFLGVAASHTYKLLIILSPVGSYYKEGIKPVKIAVESEFVRAVKGGTGNAKTAGNYASSLKAQQVAEEKGFSQVLWLDGIEKKYIEEVGSMNIFFKINGEIVTPMLNGSILEGITRNSVIALLKHWGLQVSERKIAIDEVIQAHKDGILEEAFGTGTAAVISPVGELIWQDETLSINNGETGEIAKKLYDTITGIQKGAVADEFGWTTEVAALTESK ilvE curated SwissProt::Q9GKM4,BRENDA::Q9GKM4 Branched-chain-amino-acid aminotransferase, cytosolic; BCAT(c); EC 2.6.1.42;; branched-chain-amino-acid transaminase (EC 2.6.1.42) MDCNNGCSAEGTGEGGSKEPVETFKAEDLIITRATILKEKPDPSTLVFGTVFTDHMLTVEWSLELGWEKPRIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFRPNLNMDRMYRSAMRATLPAFDKKELLECIQQLVKLDEEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVILSPVGPYFSSGSFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVENACQQVLWLYGEENQITEVGTMNLFLYWINEDGEEELATPPLDGIILPGVMRQSILDLAHKWGEFKVSERYLTMDDLTTAVEENRVREMFGSGTACVVCPVSTILYKDETIHIPTMENGPKLASRILEKLTDIQYGREESDWTITVA ilvE curated SwissProt::Q9Y885 Putative branched-chain-amino-acid aminotransferase TOXF; EC 2.6.1.42 MAIPLPAFYKWDVYDSKLNNVHGHVECRYTAQTGYWSDPCFVQSPFLSVHGLAPGLNYGQQVYEGIQARRTARNEILIFRPGASADRMAKSATAVSMPPVPYELFVRSVHMAVALNADYVPPHDFHGSMYIRPCQFGSSCQIGLQPPDEFIFCVFVQPHIALHGHGSLRALIAEDFDRAATRGTGHVKIGGNYAPVIRWTQSAKKEENGGWDVLLHVDSKTQTRIDEFSTSAFIGTKYAEEQNEPPQIILPESAAAIQSITSDSVAWLAKSFGWNIVKQPVTIDELASLSEVMAVGTAAGLVPVSCIRHNSTNRTFEFPSAGPMYRQLKETLDNIQRGRSSDSFGWCEKLRYAEFVQ ilvE curated SwissProt::S3DQP8 Branched-chain amino acid aminotransferase gloG; L-homotyrosine biosynthesis sub-cluster protein gloG; Pneumocandin biosynthesis cluster protein G; EC 2.6.1.42 MTENFPLPPLLGVDWDHLGFEPLEVNGHVECTFSTTTSCWTEPVFVTNPYLPVHGLAPGLNYGQQIFEGMKAFRNPSGDVQLFRPDQNALRFARSALRVAIPPVPTDLFLRAVNTAVGMNTDFVPPHGTGASLYIRPMAFASSPTVGLFLASQFKFCVYVLPVSPLHGKATQEGASVLVIEDFDRAAPLGTGNVKVGGNYGPVLGLIDEAKKQGFNLTLHLDSLSHSLIDEFSTSGFIGVLNDGEVPTIVVSDSQQVVSSITVDSICELARAFDWHVQKRPISFLEVARFSEVYAAGTAAVLVPVESILRRSTGEHVVYSVEYSSPTSCFSRLSTALRDIQQGLVPDDRSWIKLVTKP ilvE curated metacyc::MONOMER-11691 branched-chain-amino-acid aminotransferase subunit (EC 2.6.1.6; EC 2.6.1.42) MSMADRDGVIWYDGELVQWRDATTHVLTHTLHYGMGVFEGVRAYDTPQGTAIFRLQAHTDRLFDSAHIMNMQIPYSRDEINEATRAAVRENNLESAYIRPMVFYGSEGMGLRASGLKVHVIIAAWSWGAYMGEEALQQGIKVRTSSFTRHHVNISMTRAKSNGAYINSMLALQEAISGGADEAMMLDPEGYVAEGSGENIFIIKDGVIYTPEVTACLNGITRNTILTLAAEHGFKLVEKRITRDEVYIADEAFFTGTAAEVTPIREVDGRKIGAGRRGPVTEKLQKAYFDLVSGKTEAHAEWRTLVK ilvE curated metacyc::MONOMER-11904 branched-chain amino acid aminotransferase subunit (EC 2.6.1.6; EC 2.6.1.42) MKIYLNGEFVEKEQAKISVYDHGLLYGDGVFEGIRVYDGVIFKLKEHIDRLFDSATSLQMDIQTSKDEISKIVIDTIRINELNNAYIRLVITRGVGDLGLDPRKCPKPTIFCIAEPMNPLLGEDGIKVITSSIRRLPVDVLNPAVKSLNYLNSILAKIQANYAGCDEAFLLDSEGYVAEGTGDNIFVIKNGKIKTPPVSSSVLKGITRDAVVDLAKEQGYEIIEEKLTLHDLYVADELFITGTAAELAHVVEIDGRVINNREMGVITKKLSEEFKKIRKIMGTKVY ilvE curated metacyc::MONOMER-11914 branched-chain-amino-acid aminotransferase subunit (EC 2.6.1.42) MSCEASGKIWLNGEMVEWEEATVHVLSHVVHYGSSVFEGIRCYRNSKGSAIFRLREHVKRLFDSAKIYRMDIPYTQEQICDAIVETVRENGLEECYIRPVVFRGYGEMGVHPVNCPVDVAVAAWEWGAYLGAEALEVGVDAGVSTWRRMAPNTMPNMAKAGGNYLNSQLAKMEAVRHGYDEAIMLDYHGYISEGSGENIFLVSEGEIYTPPVSSSLLRGITRDSVIKIARTEGVTVHEEPITREMLYIADEAFFTGTAAEITPIRSVDGIEIGAGRRGPVTKLLQDEFFRIIRAETEDSFGWLTYI ilvE curated reanno::BFirm:BPHYT_RS16285 Branched-chain amino acid aminotransferase (EC 2.6.1.42) MSMADRDGKIWMDGKLIDWRDAKIHVLTHTLHYGMGVFEGVRAYKTADGGTAIFRLQEHTKRLLNSAKIFQMDVPFDHETLAAAQCEVVRENKLESCYLRPIIWVGSEKLGVSAKGNTIHVAIAAWPWGAYLGEDGIAKGIRVKTSSFTRHHVNVSMVRAKASGWYVNSILANQEAIADGYDEALLLDVDGYVSEGSGENFFLVNNGKLYTPDLSSCLDGITRDTVITLARDAGIQVIEKRITRDEVYTCDEAFFTGTAAEVTPIRELDNRTIGSGARGPITEKLQSGFFDIVNGKSDKYANWLTKI ilvE curated reanno::Cup4G11:RR42_RS25890 Branched-chain amino acid aminotransferase (EC 2.6.1.42) MTQQTTFSLEPNPNALDAATRDALMRDPAFGRVFTDHMVTITWREGQGWQDAKVTARKPFSIDPACSVLHYGQEIFEGMKAYRGADGAVTLFRPLENARRFQASAKRMAMPALPESLFLEAIEQLVRIDQAWVPHGSGSLYLRPFMFANEVFLGIKPASEFIFCVIACPVGPYFKGGDKAVSVWVSENYTRAAPGGTGEAKCGGNYAGSLVAQNEATANGCDQVVFLDAAEHRWVEELGGMNIFFVMDDGTLVTPPLSGSILPGITRASVIELAREMGMVVEERRYSYPEWEADAKSGRLAEAFVCGTAATLVAIGEVRSARTRFAIGNGTAGNTVKVLRDRLVEIQRNQAAGPAGWVHHVAL ilvE curated reanno::Dyella79:N515DRAFT_2015 Branched-chain amino acid aminotransferase (EC 2.6.1.42) MAQQYPEWIWQNGQIKPWREATTHVMSHALHYGSSVFEGIRSYATPDGAAIFRLTDHLKRLYQSAKIYDMVLPYSQDQIAAACRDVIKQNGLGAAYLRPVAYRGLGGFGLSAETPIDVAVAAWPMGPYLGPEALESGIDACVSSWQRFAPNTIPAGAKAGGNYLSGQLIAREARRLGFGEGIALANTGLLSEGAGENLFLVFDGVLHTTPASASILTGITRHTLITLAREDGIEVIERDIPREYLYLCDELLMCGTAAEITPIRSVDGKKIGSGKAGRVTRRMQELFFGLFNGKTNDQWGWLEPV ilvE curated reanno::Koxy:BWI76_RS24235 Branched-chain-amino-acid transaminase (EC 2.6.1.42) MHDRRLAARAGELKPSAVRELLKHSKLPGVISLGGGIPAPELFDTEGLNLAVQQVMNGRFNDAFQYGLTEGYPPLRQAVSELCQARGVACPASHVYITSGSQQSLDIVARTLLDPGDAIVVERPTYLAALQVFQLAQANILSVDTDDDGMLVEQLADLLETTRVKAVYLVPTFGNPGGKTLSEARRRRLVELAKKHDFVIIEDDPYGEISFTDEVRRPLYQYAVELGCEDQVVYTSTFSKILAPGMRIGWIVMPDWLAQQTVIVKQAADLHTNMLSQVITAEYLSMNRLESQIALIREDYRKKCVALADALESQLGEHLEFSRPKGGMFLWARFRYPFDTMEWMKKTLENGVVYVPGEAFYNDNPDTRTLRLSYSTVSADGLMTAVERLAKSL ilvE curated reanno::acidovorax_3H11:Ac3H11_1358 L-leucine transaminase; L-isoleucine transaminase (EC 2.6.1.42) VKLNDLPQNSTWTLARRAERMNPSVIREILKVTEKPGIISLAGGLPSPKTFPVSAFAAASAAVLANDGPAALQYAASEGYAPLRQAIADFLPWDVDADQILITTGSQQALDLIAKVLIDENSRVLVETPTYLGALQAFTPMEPSVVAVASDDEGVLIDDLKAKVGTGADKARFLYVLPNFQNPTGRTMTEARRAALVKAAAELNLPLVEDNPYGDLWFDNPPPAPLTARNPEGCIYMGSFSKVLAPGLRLGFVVAPKAVYPKLLQAKQAADLHTPGYNQRLVAEVMKGNFLDRHVPTIRALYKQQCEAMLAALTQEMAGLGVEWNRPDGGMFLWVRLPEGMSAIELLPQAVERNVAFVPGAAFYADNADPRTLRLSFVTSTVEQIATGIAALAAAIRSHKG ilvE curated reanno::azobra:AZOBR_RS06555 Branched-chain-amino-acid transaminase (EC 2.6.1.42) VTVDWGNVFAGRVAGMGASEIRELLKLLERPEIISFAGGIPDPDFFPTAAIARAYEKIFQSNSGAGGALQYTISEGFTPLREWICAYLGRRGIQAGLDEVLVTSGSQQALEFVGKLLIGPGEKILVTRPTYLGALQAFSPYEPQYLSVPGDAEGPDLAAVEAALEQKPKFFYLVPDFQNPNGTTISLARREALLDLCAKHGVPIVEDAAYTELRYEGEPIPSMVALDAARNGGKITNVLFCGSFSKTMVPALRVGWINGPAEVINRLVLMKQAGDLHTSTINQIVLHDVVSQNFDSHIRRLRAGYKERRDAMLTALSEFAPAGVTWTKPEGGMFVWIELPEGTDGVDLLARAIKDANVAFVPGSAFHADRSGKNTLRLSFSNNNPERIREGIRRLCGLLQTVAA ilvE curated reanno::psRCH2:GFF445 Branched-chain amino acid aminotransferase (EC 2.6.1.42) MSMADRDGVIWYDGELVQWRDATTHVLTHTLHYGMGVFEGVRAYNTPDGTAIFRLQAHTDRLFDSAHIMNMPMPYSKEEINEATRAAVRENNLESAYIRPMVFYGSEGMGLRASGLKVHVIVAAWHWGAYMGDEALELGIKVRTSSFTRHHVNITMTRAKSNGAYINSMLALQEAISGGADEALMLDPEGYVAEGSGENIFIIKDGVIYTPEVTACLNGITRGTVLTLAAEHGLKIVEKRITRDEVYIADEAFFTGTAAEVTPIREVDGRAIGIGRRGPITEKLQKAYFDLVTGKTDAHAEWRTLVK ilvE curated reanno::pseudo5_N2C3_1:AO356_22970 Branched-chain amino acid aminotransferase (EC 2.6.1.42) MGNESINWDKLGFDYIKTDKRYLSHWRDGAWDAGTLTDDNVLHISEGSTALHYGQQCFEGLKAYRCKDGSINLFRPDQNAARMQRSCARLLMPQVETEQFVEACKQVVRANERFIPPYGTGGALYLRPFVIGVGDNIGVRTAPEFIFSIFCIPVGAYFKGGLTPHNFLISSFDRAAPQGTGAAKVGGNYAASLMPGSQAKKASFADCIYLDPMTHSKIEEVGSANFFGITHDNTFVTPRSPSVLPGITRLSLIELAKSRLGLEVIEGDVFIDKLSDFKEAGACGTAAVITPIGGISYKDKLHVFHSETEVGPITQKLYKELTGVQTGDVEAPAGWIVKV ilvE curated2 O26004 Branched-chain-amino-acid aminotransferase; BCAT; EC 2.6.1.42 MANLENLDWKNLGFSYIKTDFRFIATYKNGSWSQGGLVSENMLQLSEGSPVLHYGQACFEGLKAYRSQKGKALLFRPLENAKRLQTSCERLLMPKVSEELFLRACAEVVKANQKWLAPYKSGASLYLRPFVIGVGDNLGVKPANEYLFIVFCAPVGAYFKGGIEKGGARFITTIFDRAAPKGTGGVKVGGNYAASLLAHKMATEQGYDDCIYLDPTTHTKIEEVGAANFFGITHDDAFITPHSPSILPSITKKSLMVLAKEYLNLKVEEREILMDELDAFKEAGACGTAAIITPIKEIVHNNKSYFFEAPGHITKRLYDLLLSIQQGEQEAPKDWIFEVG ilvE curated2 O27481 Putative branched-chain-amino-acid aminotransferase; BCAT; EC 2.6.1.42; Transaminase B MSCEASGKIWLNGEMVEWEEATVHVLSHVVHYGSSVFEGIRCYRNSKGSAIFRLREHVKRLFDSAKIYRMDIPYTQEQICDAIVETVRENGLEECYIRPVVFRGYGEMGVHPVNCPVDVAVAAWEWGAYLGAEALEVGVDAGVSTWRRMAPNTMPNMAKAGGNYLNSQLAKMEAVRHGYDEAIMLDYHGYISEGSGENIFLVSEGEIYTPPVSSSLLRGITRDSVIKIARTEGVTVHEEPITREMLYIADEAFFTGTAAEITPIRSVDGIEIGAGRRGPVTKLLQDEFFRIIRAETEDSFGWLTYI ilvE curated2 O29329 Putative branched-chain-amino-acid aminotransferase; BCAT; EC 2.6.1.42; Transaminase B MLYVYMDGEFVPENEAKVSIFDHGFLYGDGVFEGIRAYNGRVFRLKEHIDRLYDSAKAIDLEIPITKEEFMEIILETLRKNNLRDAYIRPIVTRGIGDLGLDPRKCQNPSIIVITKPWGKLYGDLYEKGLTAITVAVRRNSFDALPPNIKSLNYLNNILAKIEANAKGGDEAIFLDRNGYVSEGSGDNIFVVKNGAITTPPTINNLRGITREAVIEIINRLGIPFKETNIGLYDLYTADEVFVTGTAAEIAPIVVIDGRKIGDGKPGEITRKLMEEFSKLTESEGVPIYE ilvE curated2 O31461 Branched-chain-amino-acid transaminase 1; BCAT 1; EC 2.6.1.42 MNKLIEREKTVYYKEKPDPSSLGFGQYFTDYMFVMDYEEGIGWHHPRIAPYAPLTLDPSSSVFHYGQAVFEGLKAYRTDDGRVLLFRPDQNIKRLNRSCERMSMPPLDEELVLEALTQLVELEKDWVPKEKGTSLYIRPFVIATEPSLGVKASRSYTFMIVLSPVGSYYGDDQLKPVRIYVEDEYVRAVNGGVGFAKTAGNYAASLQAQRKANELGYDQVLWLDAIEKKYVEEVGSMNIFFVINGEAVTPALSGSILSGVTRASAIELIRSWGIPVREERISIDEVYAASARGELTEVFGTGTAAVVTPVGELNIHGKTVIVGDGQIGDLSKKLYETITDIQLGKVKGPFNWTVEV ilvE curated2 O67733 Probable branched-chain-amino-acid aminotransferase; BCAT; EC 2.6.1.42 MLKSFSMDFAFFEGKIVPVEEAKISIMTNSFHYGTAIFEGIRAYWNEEEEQLYILFAKEHYERLLTNARCLFMELNYSAEELVEITKEILRKSEIREDVYIRPIAYFKDLKLTPKLIDYTPEIAIYLYRFGRYLDTSKGIRAKVSSWRRNDDNSIPSRWKVAGAYVNSALAKTEALMSGYDEAILLNSQGYVAEGSGENIFIIKNGKAITPSPNEHILEGITRNAVITLLKKELVVEVEERPIARSELYTADEVFLTGTAAEVTPVVEIDNRKIGNGEIGPITKQLQEFYFNAVRGKIQRYKKWLTPVYDK ilvE curated2 O86428 Branched-chain-amino-acid aminotransferase; BCAT; EC 2.6.1.42 MSMADRDGVIWYDGELVQWRDATTHVLTHTLHYGMGVFEGVRAYDTPQGTAIFRLQAHTDRLFDSAHIMNMQIPYSRDEINEATRAAVRENNLESAYIRPMVFYGSEGMGLRASGLKVHVIIAAWSWGAYMGEEALQQGIKVRTSSFTRHHVNISMTRAKSNGAYINSMLALQEAISGGADEAMMLDPEGYVAEGSGENIFIIKDGVIYTPEVTACLNGITRNTILTLAAEHGFKLVEKRITRDEVYIADEAFFTGTAAEVTPIREVDGRKIGAGRRGPVTEKLQKAYFDLVSGKTEAHAEWRTLVK ilvE curated2 O86505 Probable branched-chain-amino-acid aminotransferase; BCAT; EC 2.6.1.42 MTTPTIELKPSAHPLSDSERAAILANPGFGRHFTDHMVTIKWTEGRGWHDGQLVPYAPLSLDPATMVLHYAQEIFEGLKAYRRPDGSVATFRPEKNGARFQASSRRLGMPELPVDTFIEACDALVAQDEKWVPAHGGEESLYLRPFMIATEVGLGVRPANEYLFIVIASPAGAYFPGGVKPVSIWVSEDRVRAVPGGMGDAKTGGNYAASLLAQAEAAAKGCDQVCYLDAIERKWVEELGGMNLYFVYGNKIVTPSLTGSILEGVTRDSLLTVARDLGYEAEEGRVSVDQWQRDSENGTLTEVFACGTAAVITPVGTVKRAGAQWQQSGGETGEVTQRLRDALLDIQRGTVADPHGWMHTLA ilvE curated2 P0A1A6 Branched-chain-amino-acid aminotransferase; BCAT; EC 2.6.1.42; Transaminase B MTTKKADYIWFNGEMVRWEDAKVHVMSHALHYGTSVFEGIRCYDSHKGPVVFRHREHMQRLRDSAKIYRFPVSQSIDELMEACRDVIRKNNLTSAYIRPLVFVGDVGMGVNPPPGYTTDVIIAAFPWGAYLGAEALDQGIDAMVSSWNRAAPNTIPTAAKAGGNYLSSLLVGSEARRHGYQEGIALDVNGYISEGAGENLFEVKDGVLFTPPFTSSALPGITRDAIIKLAKELGIEVREQVLSRESLYLADEVFMSGTAAEITPVRSVDGIQVGEGRCGPVTKRIQQAFFGLFTGETEDKWGWLDPVNS ilvE curated2 P39576 Branched-chain-amino-acid aminotransferase 2; BCAT 2; EC 2.6.1.42; Vegetative protein 85; VEG85 MTKQTIRVELTSTKKPKPDPNQLSFGRVFTDHMFVMDYAADKGWYDPRIIPYQPLSMDPAAMVYHYGQTVFEGLKAYVSEDDHVLLFRPEKNMERLNQSNDRLCIPQIDEEQVLEGLKQLVAIDKDWIPNAEGTSLYIRPFIIATEPFLGVAASHTYKLLIILSPVGSYYKEGIKPVKIAVESEFVRAVKGGTGNAKTAGNYASSLKAQQVAEEKGFSQVLWLDGIEKKYIEEVGSMNIFFKINGEIVTPMLNGSILEGITRNSVIALLKHWGLQVSERKIAIDEVIQAHKDGILEEAFGTGTAAVISPVGELIWQDETLSINNGETGEIAKKLYDTITGIQKGAVADEFGWTTEVAALTESK ilvE curated2 P54691 Probable branched-chain-amino-acid aminotransferase; BCAT; EC 2.6.1.42 MHKFLPIAYFEDKFVPFEDAKISVATHALHYGTAAFGGLRGIPDPEDPGTILLFRLDRHGDRLSKSAKFLHYDISAEKIKEVIVDFVKKNQPDKSFYIRPLVYSSGLGIAPRLHNLEKDFLVYGLEMGDYLAADGVSCRISSWYRQEDRSFPLRGKISAAYITSALAKTEAVESGFDEAILMNSQGKVCEATGMNVFMVRNGQIVTPGNEQDILEGITRDSILTIAADLGIPTCQRPIDKSELMIADEVFLSGTAAKITPVKRIENFTLGGDRPITEKLRSVLTAVTENREPKYQDWVFKIPLNG ilvE curated2 P74921 Probable branched-chain-amino-acid aminotransferase; BCAT; EC 2.6.1.42 MLIWWRGKFRRADEISLDFSLFEKSLQGAVYETLRTYSRAPFAAYKHYTRLKRSADFFNLPLSLSFDEFTKVLKAGADEFKQEVRIKVYLFPDSGEVLFVFSPLNIPDLETGVEVKISNVRRIPDLSTPPALKITGRTDIVLARREIVDCYDVILLGLNGQVCEGSFSNVFLVKEGKLITPSLDSGILDGITRENVIKLAKSLEIPVEERVVWVWELFEADEMFLTHTSAGVVPVRRLNEHSFFEEEPGPVTATLMENFEPFVLNLEENWVGI ilvE curated2 P9WQ74 Branched-chain-amino-acid aminotransferase; BCAT; EC 2.6.1.42 MTSGSLQFTVLRAVNPATDAQRESMLREPGFGKYHTDHMVSIDYAEGRGWHNARVIPYGPIELDPSAIVLHYAQEVFEGLKAYRWADGSIVSFRADANAARLRSSARRLAIPELPDAVFIESLRQLIAVDKAWVPGAGGEEALYLRPFIFATEPGLGVRPATQYRYLLIASPAGAYFKGGIAPVSVWVSTEYVRACPGGTGAAKFGGNYAASLLAQAEAAENGCDQVVWLDAVERRYIEEMGGMNIFFVLGSGGSARLVTPELSGSLLPGITRDSLLQLAIDAGFAVEERRIDIDEWQKKAAAGEITEVFACGTAAVITPVARVRHGASEFRIADGQPGEVTMALRDTLTGIQRGTFADTHGWMARLG ilvE curated2 Q1RIJ2 Probable branched-chain-amino-acid aminotransferase; BCAT; EC 2.6.1.42 MTKNSENNLWYIWINGELVPYELATVHALTHSLHYSGSVFEGERAYNGKVFKLKEHTERLVKSAEVLGLKVPYNVEEIIKAHELLIEKNKIQDAYIRPLVWCGSESLNIINPKLSTNVLIAAVPSMPRAFAAGFNLYVSRWRKAAPNMMPVQSKSAAHYNMAITSKKEAKDLGYDDALLLDYEGYIAECTTTNIFFVKDNVLYTPIADRFLDGITRQTIIEIAKNLGLEVKEERLKLEQIEDFISCFATGTAIEVQNINSIDIGNKKVIFNDHKIADVLKEEYGKIVRG ilvE curated2 Q58414 Putative branched-chain-amino-acid aminotransferase; BCAT; EC 2.6.1.42; Transaminase B MKIYLNGKFVDEKDAKVSVFDHGLLYGDGVFEGIRAYDGVVFMLKEHIDRLYDSAKSLCIDIPLTKEEMIDVVLETLRVNNLRDAYIRLVVTRGVGDLGLDPRKCGKPTIFCIAIPMPPLLGEDGIRAITVSVRRLPVDVLNPAVKSLNYLNSVLAKIQANYAGVDEAFLLDDKGFVVEGTGDNIFIVKNGVLKTPPVYQSILKGITRDVVIKLAKEEGIEVVEEPLTLHDLYTADELFITGTAAEIVPVFEIDGRVINNKQVGEITKKLKEKFKDIRTKWGIKVYDE ilvE curated2 Q6GJB4 Probable branched-chain-amino-acid aminotransferase; BCAT; EC 2.6.1.42 MSQAVKIELRETLKEKPDTSQLGFGKYFTDYMLSYDYDADKGWHDLKIVPYGPIEISPAAQGVHYGQSVFEGLKAYKKDGEVALFRPDENFKRLNNSLARLEMPQVNEGELLEGLKQLVDLEREWVPEGEGQSLYIRPFVFATEGVLGVGASHQYKLLIILSPSGAYYGGETLKPTKIYVEDEYVRAVRGGVGFAKVAGNYAASLLAQTNANKLGYDQVLWLDGVEQKYIEEVGSMNIFFVENGKVITPELNGSILPGITRKSIIELAKNLGYEVEERRVSIDELFESYDKGELTEVFGSGTAAVISPVGTLRYEDREIVINNNETGEITQKLYDVYTGIQNGTLEDKNGWRVVVPKY leuT curated TCDB::O67854 The amino acid (leucine):2 Na+ symporter, LeuTAa (Yamashita et al., 2005). LeuT possesses two ion binding sites, NA1 and NA2, both highly specific for Na+ but with differing mechanisms of binding (Noskov and Roux, 2008). X-ray structures have been determined for LeuT in substrate-free outward-open and apo inward-open states MEVKREHWATRLGLILAMAGNAVGLGNFLRFPVQAAENGGGAFMIPYIIAFLLVGIPLMWIEWAMGRYGGAQGHGTTPAIFYLLWRNRFAKILGVFGLWIPLVVAIYYVYIESWTLGFAIKFLVGLVPEPPPNATDPDSILRPFKEFLYSYIGVPKGDEPILKPSLFAYIVFLITMFINVSILIRGISKGIERFAKIAMPTLFILAVFLVIRVFLLETPNGTAADGLNFLWTPDFEKLKDPGVWIAAVGQIFFTLSLGFGAIITYASYVRKDQDIVLSGLTAATLNEKAEVILGGSISIPAAVAFFGVANAVAIAKAGAFNLGFITLPAIFSQTAGGTFLGFLWFFLLFFAGLTSSIAIMQPMIAFLEDELKLSRKHAVLWTAAIVFFSAHLVMFLNKSLDEMDFWAGTIGVVFFGLTELIIFFWIFGADKAWEEINRGGIIKVPRIYYYVMRYITPAFLAVLLVVWAREYIPKIMEETHWTVWITRFYIIGLFLFLTFLVFLAERRRNHESA liuA curated BRENDA::B5UB85 isovaleryl-CoA dehydrogenase (EC 1.3.8.4) MVVRLCVRRLLRKTANKTGHRCISHYPIDDHVFGLSEEQQQLRKMVFDFAQKELAPKAAEIDKENNFKELRPFWKKLGDLGLLGITASSDYGGTGGKYSDHCVIMEELSRASGGIALSYGAHSNLCVNQINRNGTEEQKSKYLPKLCSGEHIGALAMSEPGSGSDVVSMKLRAEKKGDYYVLNGNKFWITNGPDADVLVVYAKTNWSTSKQQHGISAFLIEKDYPGFSTAQKLDKLGMRGSNTGELVFEDCKVPAANLLGQENKGVYVLMSGLDLERLVLAAGPVGLMQAAIDTAFLYAHTRKQFGKNIGEFQLIQGKMADMYTTLSACRSYLYNVAKACDNGHVNSKDCAGVILYCAEKATQVALDAIQILGGNGYINDYPTGRILRDAKLYEIGAGTSEVRRMLIGRALNNEYK liuA curated BRENDA::P12007,SwissProt::P12007 isovaleryl-CoA dehydrogenase (EC 1.3.8.4);; Isovaleryl-CoA dehydrogenase, mitochondrial; IVD; EC 1.3.8.4 MATAVRLLGRRVSSWRLRPLPSPLAVPQRAHSMLPVDDDINGLNEEQKQLRHTISKFVQENLAPKAQEIDQSNDFKNLREFWKQLGSLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASAAVGLSYGAHSNLCINQIVRNGNEAQKEKYLPKLISGEFIGALAMSEPNAGSDVVSMRLKAEKKGDHYVLNGNKFWITNGPDADVLVVYAKTDLTAVPASRGITAFIVEKDMPGFSTSKKLDKLGMRGSNTCELVFEDCKVPAANILSQESKGVYVLMSGLDLERLVLAGGPLGIMQAVLDHTIPYLHVREAFGQKIGQFQLMQGKMADMYTRLMACRQYVYNVARACDEGHITAKDCAGVILYTAECATQVALDGIQCLGGNGYINDFPMGRFLRDAKLYEIGGGTSEVRRLVIGRAFNADFR liuA curated BRENDA::P26440,SwissProt::P26440 isovaleryl-CoA dehydrogenase (EC 1.3.8.4);; Isovaleryl-CoA dehydrogenase, mitochondrial; IVD; EC 1.3.8.4 MAEMATATRLLGWRVASWRLRPPLAGFVSQRAHSLLPVDDAINGLSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKNLREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAVPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRAFNADFH liuA curated BRENDA::Q75N94 isovaleryl-CoA dehydrogenase (EC 1.3.8.4) MAAASRLPFLFRSTSRSLGSIRKPLIQIPASRTFASKHPKGFVPPTEDELLELRERVQEFTRREITEEVAAKTDAQNEFPAEMWKKLGDAGFLGITANEDYGGLGMGYQAHCIVMEELSRASGSIALSYAAHSQLCVNQLSLNGSPEQKERFLPGLLSGDKIGALAMSEHSAGSDVVSMKTTAKEVDGGYVLNGTKMWITNGPDADFIVVYAKTEPQKGSKGITAFVVEKTFDGFSCARKLDKLGMRGSNTGELIFEDVFVPKENVLGEVNRGVKVLMEGLDLERLVLSAGPLGIMQAALDLVLPYTHVRKQFGTPIAHNQLIQGKLADMYTKLQASRAYTYSTARHIDNSASLSEVSIRTQDCAGAILYAAERATECALDAIQLMGGNGYINELPAGRLLRDAKLYEIGAGTSEIRRMVIGRAFNKEYA liuA curated BRENDA::Q9SWG0,SwissProt::Q9SWG0 isovaleryl-CoA dehydrogenase (EC 1.3.8.4);; Isovaleryl-CoA dehydrogenase, mitochondrial; IVD; EC 1.3.8.4 MQRFFSARSILGYAVKTRRRSFSSRSSSLLFDDTQLQFKESVSKFAQDNIAPHAERIDKTNSFPKDVNLWKLMGEFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVALSYGAHSNLCINQLVRNGTAAQKEKYLPKLISGEHVGALAMSEPNAGSDVVGMKCKAEKVDGGYILNGNKMWCTNGPSAETLVVYAKTDTKAGSKGITAFIIEKGMTGFSTAQKLDKLGMRGSDTCELVFENCFVPEENILDKEGKGVYVLMSGLDLERLVLAAGPLGIMQACLDNVLPYIRQREQFGRPVGEFQFIQGKVADMYTALQSSRSYVYSVARDCDNGKVDPKDCAGTILCAAERATQVALQAIQCLGGNGYINEYATGRLLRDAKLYEIGAGTSEIRRIVIGRELFKEE liuA curated CharProtDB::CH_122627 isovaleryl-coenzyme A dehydrogenase; EC 1.3.99.10 MATIRLPLLIRRSLPTRAPARFTRPLIPCVRTLATTKHPRGFVPPTEDDLLELRESVQEFTSRISTVVAARTDAQNEFPAEMWKKLGNAGFLGVTADEEYGGLGMGYQAHCVVMEEISRASGSIALSYAAHSQLCVNQLSLNGTPEQKARFLPGLLSGEKIGALAMSEHSAGSDVVSMKTSAKEVDGGWVLNGTKMWITNGPDADYIVVYAKTEPEKGSKGITAFVVEKTFKGFSCARKLDKLGMRGSNTGELIFEDVFVPRENLLGEVNRGVKVLMEGLDLERLVLSAGPLGIMQAALDLVLPYTHVRKQFGAPIAHNQLIQGKLADMHTKLAASRAYTYATARHIDSHASLGSAAIRTQDCAGAILYAAERATECALDAIQLMGGNGYINEIPAGRLLRDAKLYEIGAGTSEIRRMVIGRAFNKEYAQ liuA curated SwissProt::P33224,metacyc::EG11811-MONOMER Putative acyl-CoA dehydrogenase AidB; EC 1.3.99.-;; putative acyl-CoA dehydrogenase AidB (EC 1.3.8.4) MHWQTHTVFNQPIPLNNSNLYLSDGALCEAVTREGAGWDSDFLASIGQQLGTAESLELGRLANVNPPELLRYDAQGRRLDDVRFHPAWHLLMQALCTNRVHNLAWEEDARSGAFVARAARFMLHAQVEAGSLCPITMTFAATPLLLQMLPAPFQDWTTPLLSDRYDSHLLPGGQKRGLLIGMGMTEKQGGSDVMSNTTRAERLEDGSYRLVGHKWFFSVPQSDAHLVLAQTAGGLSCFFVPRFLPDGQRNAIRLERLKDKLGNRSNASCEVEFQDAIGWLLGLEGEGIRLILKMGGMTRFDCALGSHAMMRRAFSLAIYHAHQRHVFGNPLIQQPLMRHVLSRMALQLEGQTALLFRLARAWDRRADAKEALWARLFTPAAKFVICKRGMPFVAEAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLNKQAGVYDLLSEAFVEVKGQDRYFDRAVRRLQQQLRKPAEELGREITHQLFLLGCGAQMLKYASPPMAQAWCQVMLDTRGGVRLSEQIQNDLLLRATGGVCV liuA curated SwissProt::Q9FS87,BRENDA::Q9FS87 Isovaleryl-CoA dehydrogenase, mitochondrial; IVD; Isovaleryl-CoA dehydrogenase 2; St-IVD2; EC 1.3.8.4;; isovaleryl-CoA dehydrogenase (EC 1.3.8.4) MHKLFVARSVKSALFRIKNHQKPQFAAFSTSLLFDDTQKQFKESVAQFAQENIAPHAEKIDRTNYFPQDVNLWKLMGNFNLLGITVPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHTNLCINQLVRNGTHEQKQKYLPKLISGEHVGALAMSEPNAGSDVVSMKCKADRVEGGYVLNGNKMWCTNGPTAQTLVVYAKTDVTAGSKGITAFIIEKGMTGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQVGRGVYVLMSGLDLERLVLASGPVGIMQACLDVVLPYVKQREQFGRPIGEFQFVQGKVADMYTSMQSSRSYLYSVARECDSGTINTKDCAGVILSAAERATQVALQAIQCLGGNGYVNEYPTGRFLRDAKLYEIGAGTSEIRRMIIGRELFKEQ liuA curated metacyc::MONOMER-11693 acyl-CoA dehydrogenase subunit (EC 1.3.8.4; EC 1.3.8.5) MDHRLTPELEELRRTVEEFAHDVVAPKIGDFYERHEFPYEIVREMGRMGLFGLPFPEEYGGMGGDYLALGIALEELARVDSSVAITLEAGVSLGAMPIHLFGTDAQKAEWLPRLCSGEILGAFGLTEPDGGSDAGATRTTARLDESTNEWVINGTKCFITNSGTDITGLVTVTAVTGRKPDGKPLISSIIVPSGTPGFTVAAPYSKVGWNASDTRELSFADVRVPAANLLGEQGRGYAQFLRILDEGRIAISALATGLAQGCVDESVKYAGERHAFGRNIGAYQAIQFKIADMEMKAHMARVGWRDAASRLVAGEPFKKEAAIAKLYSSTVAVDNAREATQIHGGYGFMNEYPVARMWRDSKILEIGEGTSEVQRMLIARELGLVG liuA curated metacyc::MONOMER-16063 isovaleryl-CoA dehydrogenase subunit (EC 1.3.8.4) MTYPSLNFALGETIDMLRDQVRGFVAAELQPRAAQIDQDNQFPMDMWRKFGEMGLLGITVDEEYGGSALGYLAHAVVMEEISRASASVALSYGAHSNLCVNQIKRNGNAEQKARYLPALVSGEHIGALAMSEPNAGSDVVSMKLRADRVGDRFVLNGSKMWITNGPDAHTYVIYAKTDADKGAHGITAFIVERDWKGFSRGPKLDKLGMRGSNTCELIFQDVEVPEENVLGAVNGGVKVLMSGLDYERVVLSGGPVGIMQACMDVVVPYIHDRRQFGQSIGEFQLVQGKVADMYTALNASRAYLYAVAAACDRGETTRKDAAGVILYSAERATQMALDAIQILGGNGYINEFPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFNETR liuA curated reanno::ANA3:7024494 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) MNSLYTSLNFGLGEEVDMLRDAVQDFAKHEIAPIAAKVDHDNAFPNEIWPVLGGMGLLGVTVPEEYGGANMGYLAHVVAMEEISRASASIGLSYGAHSNLCVNQINRNGNAEQKAKYLPKLVSGEHIGALAMSEPNAGSDVVSMKLHARKEGDRYILNGNKMWITNGPDANTYVIYAKTDLTKGAHGITAFIVERGFKGFSQAQKLDKLGMRGSNTCELVFEDVEVPEENILGGLNNGVKVLMSGLDYERVVLSGGPLGIMNACMDIVVPYIHEREQFGKSIGEFQLVQGKLADMYTGMNAAKAYVYSVAKSCDRGETTRKDAAGAILYSAELATKMALDAIQLLGGNGYVNEYATGRLLRDAKLYEIGAGTSEIRRMLIGRELFNESK liuA curated reanno::Phaeo:GFF1011 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) MFNASMTFDLGEDVNALRDMVHRWAQERVRPMAQEIDQKNEFPAELWQEMGELGLLGITVPEEFGGAGMSYLAHTVAVEEIARASASVSLSYGAHSNLCVNQIKLNGNAEQKAKYLPRLVSGEHVGALAMSEAGAGSDVVSMSLRAEKRNDHYRLNGNKYWITNGPDADTLVVYAKTDPDAGSKGMTAFLIEKEFKGFSTSQHFDKLGMRGSNTAELVFEDVEVPFENVLGEEGKGVRVLMSGLDYERVVLAGIGTGIMAACMDEMMPYMKERKQFGQPIGNFQLMQGKIADMYTAMNTARAYVYEVAKACDKGTVTRQDAAACCLYASEVAMTQAHQAVQAFGGAGYLSDNPVGRIFRDAKLMEIGAGTSEIRRMLIGRELMSQM liuA curated reanno::SB2B:6937192 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) MSHLYSTLNFGLGEDVDMLRDAVYEFAKGEIAPLAEKVDRDNAFPNELWAKFGDMGLLGVTVAEEYGGVNMGYLAHVVAMEEISRASASIGLSYGAHSNLCVNQIYRNGNEAQRAKYLPKLISGEHIGALAMSEPNAGSDVVSMKLHARKEGDRYILNGNKMWITNGPDAHTYVIYAKTDLDKGPHGITAFIVERGFKGFSQAQKLDKLGMRGSNTCELVFEDCEVPEENILGGLNNGVKVLMSGLDYERVVLSGGPLGIMTACMDIVVPYVHERVQFGKSIGEFQLVQGKLADMYTGMNAAKSYVYNVARACDRGETTRKDAAGVILYAAELATKMALDAIQLLGGNGYVNEYATGRLLRDAKLYEIGAGTSEIRRMLIGRELFNETK liuA curated reanno::Smeli:SM_b21121 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) MFEAGLNFALGEEIDALRASVRRFASERIAPLADDADRSNAFPMSLWREMGELGLLGITADEAHGGAGLGYLAHCVAMEEISRASASVGLSYGAHSNLCVNQINRNGKPAQKSRYLPKLISGEHVGALAMSEPGAGSDVVSMKLKADKRGDRYVLNGSKMWITNGPDADVLVVYAKTDPAAGPRGITAFLVEKAFPGFSAGQKLDKLGMRGSNTSELIFTDCEVPEENVLGGVGEGVKVLMSGLDYERVVLSAGPLGIMAACLDVVVPYLHERKQFGQPIGEFQLMQGKLADMYVTMNAARAYVYAVAAACDRGETARKDAAGCILYAAEKATAMALEAIQALGGNGYTNDYPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFAETK liuA curated reanno::WCS417:GFF3325 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) MSYPSLNFALGETIDMLRDQVQSFVSKEIAPRAAQIDRDNLFPADLWQKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSASVALSYGAHSNLCVNQINRNGNHSQKLKYLPKLISGEHVGALAMSEPNAGSDVVSMKLRADKRGDHYVLNGSKTWITNGPDASTYVIYAKTDLEKGPHGITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVEVPEENILGTLNGGVKVLMSGLDYERVVLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGVILYSAERATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFNETR liuA curated reanno::acidovorax_3H11:Ac3H11_2991 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) MSIPANLPGLNFQLGEDIDALRDAVRDFAQAEIAPRAADIDKSDQFPMDLWRKMGDLGVLGITVPEQYGGAAMGYLAHMVAMEEISRASASVGLSYGAHSNLCVNQINRNGNEAQKAKYLSKLISGEHVGALAMSEPGAGSDVISMKLKAEDKGGYYLLNGSKMWITNGPDADTLVVYAKTEPELGARGVTAFLIEKGMKGFSIAQKLDKLGMRGSHTGELVFQDVEVPAENVLGGLNQGAKVLMSGLDYERAVLTGGPLGIMQSVMDNVIPYIHDRKQFGQSIGEFQLIQGKVADMYTVLQAGRSFAYTVAKNLDMLGTDHVRQVRKDCASVILWCAEKATWMAGEGVQIYGGNGYINEYPLGRLWRDAKLYEIGAGTSEIRRMLIGRELFAETC liuA curated reanno::psRCH2:GFF1051 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) MNYSSLNFALGETIDMLREQVQAFVAAEIAPRAEAIDQENLFPADMWRKFGEMGLLGVTVSEEYGGAGLGYLAHVVAMEEISRGSASVALSYGAHSNLCVNQINRNGNPEQKARYLPKLISGEHVGALAMSEPNAGSDVVSMKLRAEKRGDRYVLNGSKTWITNGPDANTYVIYAKTDLDKGAHGITAFIVERDWKGFSRGNKFDKLGMRGSNTCELFFDDVEVPQENVLGAENGGVKVLMSGLDYERVVLAGGPTGIMQSCLDVVVPYIHDRKQFGQSIGEFQFIQGKVADMYTQLNASRAYLYAVAQACDRGETTRKDAAGVILYTAENATQMALQAIQILGGNGYINEFPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFNESR liuA curated reanno::pseudo3_N2E3:AO353_20350 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) MSYPTLNFALGETIDMLRDQVRAFVSKEIAPRAAQIDIDNLFPADLWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSASVALSYGAHSNLCVNQINRNGTHEQKAKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRADKRGDHYVLNGSKTWITNGPDANTYVIYAKTDLEKGPHGITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVEVPEENILGVLNGGVKVLMSGLDYERVVLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGVILYSAERATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFNETR liuA curated reanno::pseudo5_N2C3_1:AO356_01580 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) MSYPSLNFALGETIDMLRDQVQAFVKAELAPRAAQIDIDNLFPADMWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSASVALSYGAHSNLCVNQINRNGNHEQKTKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRADKRGDHYVLNGSKTWITNGPDANTYVIYAKTDLEKGPHGITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVEVPEENILGALNGGVKVLMSGLDYERVVLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGVILYSAERATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFNETR liuA curated reanno::pseudo6_N2E2:Pf6N2E2_2191 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) MSYPSLNFALGETIDMLRDQVQAFVNAELAPRAAQIDIDNLFPADMWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSASVALSYGAHSNLCVNQINRNGNHEQKTKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRADKRGDKYVLNGSKTWITNGPDANTYVIYAKTDLEKGPHGITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVEVPEDNILGALNGGVKVLMSGLDYERVVLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGVILYSAERATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFNETR liuB curated BRENDA::Q42523,SwissProt::Q42523 methylcrotonoyl-CoA carboxylase (EC 6.4.1.4);; Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial; MCCase subunit alpha; 3-methylcrotonyl-CoA carboxylase 1; 3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha; EC 6.4.1.4 MSMMTVWALRRNVRRKNHSMLVRYISGSASMKPKEQCIEKILVANRGEIACRIMRTAKRLGIQTVAVYSDADRDSLHVKSADEAVRIGPPSARLSYLSGVTIMEAAARTGAQAIHPGYGFLSESSDFAQLCEDSGLTFIGPPASAIRDMGDKSASKRIMGAAGVPLVPGYHGHEQDIDHMKSEAEKIGYPIIIKPTHGGGGKGMRIVQSGKDFADSFLGAQREAAASFGVNTILLEKYITRPRHIEVQIFGDKHGNVLHLYERDCSVQRRHQKIIEEAPAPNISEKFRANLGQAAVSAARAVGYYNAGTVEFIVDTESDQFYFMEMNTRLQVEHPVTEMIVGQDLVEWQIRVANGEPLPLSQSEVPMSGHAFEARIYAENVPKGFLPATGVLNHYRPVAVSPSVRVETGVEQGDTVSMHYDPMIAKLVVWGGNRGEALVKLKDCLSNFQVAGVPTNINFLQKLASHKEFAVGNVETHFIEHHKSDLFADESNPAATEVAYKAVKHSAALVAACISTIEHSTWNESNHGKVPSIWYSNPPFRVHHEAKQTIELEWNNECEGTGSNLISLGVRYQPDGSYLIEEGNDSPSLELRVTRAGKCDFRVEAAGLSMNVSLAAYLKDGYKHIHIWHGSEHHQFKQKVGIEFSEDEEGVQHRTSSETSSHPPGTIVAPMAGLVVKVLVENEAKVDQGQPILVLEAMKMEHVVKAPSSGSIQDLKVKAGQQVSDGSALFRIKG liuB curated BRENDA::Q9I299,metacyc::MONOMER-16075 methylcrotonoyl-CoA carboxylase (subunit 2/2) (EC 6.4.1.4);; methylcrotonyl-CoA carboxylase α-subunit (EC 6.4.1.4) MNPDYRSIQRLLVANRGEIACRVMRSARALGIGSVAVHSDIDRHARHVAEADIAVDLGGAKPADSYLRGDRIIAAALASGAQAIHPGYGFLSENADFARACEEAGLLFLGPPAAAIDAMGSKSAAKALMEEAGVPLVPGYHGEAQDLETFRREAGRIGYPVLLKAAAGGGGKGMKVVEREAELAEALSSAQREAKAAFGDARMLVEKYLLKPRHVEIQVFADRHGHCLYLNERDCSIQRRHQKVVEEAPAPGLGAELRRAMGEAAVRAAQAIGYVGAGTVEFLLDERGQFFFMEMNTRLQVEHPVTEAITGLDLVAWQIRVARGEALPLTQEQVPLNGHAIEVRLYAEDPEGDFLPASGRLMLYREAAAGPGRRVDSGVREGDEVSPFYDPMLAKLIAWGETREEARQRLLAMLAETSVGGLRTNLAFLRRILGHPAFAAAELDTGFIARHQDDLLPAPQALPEHFWQAAAEAWLQSEPGHRRDDDPHSPWSRNDGWRSALARESDLMLRCRDERRCVRLRHASPSQYRLDGDDLVSRVDGVTRRSAALRRGRQLFLEWEGELLAIEAVDPIAEAEAAHAHQGGLSAPMNGSIVRVLVEPGQTVEAGATLVVLEAMKMEHSIRAPHAGVVKALYCSEGELVEEGTPLVELDENQA liuB curated CharProtDB::CH_122249 3-methylcrotonyl-CoA carboxylase biotin-containig subunit; EC 6.4.1.4 MPLSSLLRTSARLGQTVVARRSRRTASTVTSNSSSNFRALDSILIANRGEIALRVGRTAAQHGIRVTTLYTDPDSQAQHALSTPYAFNLGSVSAYLDGDRIIEIAKAQGCQGIHPGYGFLSENSEFARKCTEAGLVFIGPPWKAIEDMGDKRCSKHIMTAAGVPCVPSYHGENQDPNFLEAEADKIKYPVLIKAIKGGGGKGMRIARSKEEFQAQLQSAKSEAMNSFGDDHVLVEKYITTPRHIEVQVFADKHGNCVALGERDCSIQRRHQKILEESPAPHLPDATRKDIWAKARSAALAVRYEGAGTVEFIFDNDTGEFFFMEMNTRLQVEHPVTEMVTGQDLVHWQLKVAEGAELPLTQEEVEANIATHGHAIEARIYAENPAQGFIPDSGALLHVRTPATTEDVRIDAGFVQGDEVSAHYDPMIAKLIVRGADRQEAIRKLACSIGRVEVAGPATNIEFLKSVCKSADFISGKVETGYIEKHHDELFAQSPIEPEVLAQVALACLHDDARLAAQKATNFQGSAVGFGPGFQQHHMTFTNSASANNEAFDVKVQQTGENVFNVKIGEHTFEQVTSHPNADFRIITSFFPHTRLDTTVIRDGDSIVVFQRGRQYRLTTPRAKWMEKALGMKDVTNSVLAPMPCKVLRVEVQAGDTVEKDQPLVVIESMKMETVIRSPQRGKLPKSSIKKETNAKAGHRLWSLLVKTKRRRNRYGRIEAMLHQ liuB curated SwissProt::Q2QMG2 Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial; MCCase subunit alpha; 3-methylcrotonyl-CoA carboxylase 1; 3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha; EC 6.4.1.4 MASRLLLLPRRRSRHGGASLLLARLLSSSSSEAGGGGAVEKVLVANRGEIACRVMRTARRLGIPTVAVYSDADRGALHVRAADEAVRLGPPPARESYLNASAIVDAALRTGAKAIHPGYGFLSESADFAQLCKAEGLTFIGPPPSAIRDMGDKSASKRIMGAAGVPLVPGYHGAEQDIELLKLEANKIGYPVLIKPTHGGGGKGMRIVQRPEDFVDSVLSAQREAAASFGINTLLVEKYITQPRHIEVQIFGDQHGNVIHLYERDCSLQRRHQKIIEEAPAPNVTAQFRSHIGEAAVSAAKAVGYYSAGTVEFIVDTLSGEFYFMEMNTRLQVEHPVTEMIVGQDLVEWQIRIANGECLPLSQEQVPLNGHAFEARIYAENVPRGFLPATGTLHHYRPVPSTATVRVETGVEEGDTVSMHYDPMIAKLVVWGESRNAALVKLKNSLSNFQIAGLPTNVGFLQELAGHSAFEKGLVDTHFIERYQNDLLSTSTQALSGSHEAEELGAILAAACICKKDHVSSEVSLHDKKLSMWYAHPPFRMHHFAKRLMEFELDRELGGSSDDLLKLSVTYRSDGTYFVETEDGSSPGLDVKVDSRGDHDFRVDVGGLQTDVTLAFYSKDNCNHIHIWHGKHHHHYRQTLRAEQSPDDSSQPSASSEARSHPKGSVLAPMAGLVVKVLLKDGARVEEGQPVMVMEAMKMEHVVKAPCAGYVEGLKATAGQQVFDSSVLFTVKENKPN liuB curated SwissProt::Q96RQ3,metacyc::ENSG00000078070-MONOMER Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial; MCCase subunit alpha; 3-methylcrotonyl-CoA carboxylase 1; 3-methylcrotonyl-CoA carboxylase biotin-containing subunit; 3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha; EC 6.4.1.4;; 3-methylcrotonyl-CoA carboxylase α subunit (EC 6.4.1.4) MAAASAVSVLLVAAERNRWHRLPSLLLPPRTWVWRQRTMKYTTATGRNITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTSAAQAIHPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPRADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQHHKQLLLSRKAAAKESLCQAALGLILKEKAMTDTFTLQAHDQFSPFSSSSGRRLNISYTRNMTLKDGKNNVAIAVTYNHDGSYSMQIEDKTFQVLGNLYSEGDCTYLKCSVNGVASKAKLIILENTIYLFSKEGSIEIDIPVPKYLSSVSSQETQGGPLAPMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEFEEEESDKRESE liuB curated SwissProt::Q99MR8 Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial; MCCase subunit alpha; 3-methylcrotonyl-CoA carboxylase 1; 3-methylcrotonyl-CoA carboxylase biotin-containing subunit; 3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha; EC 6.4.1.4 MAAAALLAAVDRNQLRRVPILLLQPREWAWKLRTMKYGTTPGGSITKVLIANRGEIACRVIRTAKKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPGYGFLSENMEFAELCKQEGIIFIGPPSSAIRDMGIKSTSKSIMAAAGVPVVEGYHGKDQSDQCLREHAGKIGYPVMIKAVRGGGGKGMRIVRSEREFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGINPEVRRKLGEAAVRAAKAVKYVGAGTVEFIMDSRHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIPLSQEEIPLQGHAFEARIYAEDPDNNFMPGAGPLVHLSTPSADMSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQSALSKLRYCLHQYNIVGLRSNVDFLLRLSGHPEFEAGNVHTDFIPQHHKDLLPSHSTIAKESVCQAALGLILKEKEMTSAFKLHTQDQFSPFSFSSGRRLNISYTRNMTLRSGKSDIVIAVTYNRDGSYDMQIDNKSFRVLGDLSSEDGCTYLKSSINGVARKSKFILLDNTVHLFSMEGSIEVGIPVPKYLSPVSAEGAQGGTIAPMTGTIEKVFVKAGDRVKAGDSLMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPLVEFEEEESDK liuB curated reanno::SB2B:6937189 Methylcrotonoyl-CoA carboxylase (EC 6.4.1.4) MFNKLLIANRGEIACRVIRTARDMGIKTVAVYSDADRDARHVALADESFYLGESAPASSYLRGELIIDIAKKCGAEAIHPGYGFLSENAAFARACEASGIAFVGPGSDAIDAMGSKSAAKLIMEKAGVPLVPGYHGDDQSDATLLAEAKKIGYPLLIKAAYGGGGKGMRIVESESELKAAIDSARREAASSFGNDKLLMERYLRQPRHVEVQVFADSQGNCVYLSDRDCSIQRRHQKVVEEAPAPGLPDSLRKQMGEAAVAAAKAIDYRGAGTVEFLLDVDMSFFFMEMNTRLQVEHPVTEMVTGQDLVKWQLLVAAGAQLPLEQHEIQIHGHAFEVRIYAEDPNNEFLPASGKLTFLREPEPSRHVRIDSGVRENDVISNYYDPMIAKLIVWDESRPRALARLTRALGDYRVGGLKHNIEFLSNIAEHPAFAQANFSTDFIGRYGDALIGDSRDEADTAFVLAVLTQLRLREAVSQDVAGHDPFSPWSSLKGFRLSSPRRHSVTLLDDAHQSRSAELTESNGRYQLCLNDKLIELSGSIEDSELKCEINGHKMKVTVSLEDGGLTVFLSSGSYHFREVLGQVLEETASSEDKLKAPMNGTVVTHLVAAGDKVSAGQGLLVMEAMKMEYTIEAPFDGVVSEFFFAPGELVSDGTLLLALEMADAAADSKETEA liuB curated reanno::Smeli:SM_b21124 Methylcrotonoyl-CoA carboxylase (EC 6.4.1.4) MFSKLLIANRGEIACRIIRTARRLGIRTVAVYSDADGDALHVALADEAIRIGGAPAAESYLASAPIVQAARSVGAQAIHPGYGFLSENADFAEAVAEAGMIFVGPPPAAIRAMGLKDAAKALMERSGVPVVPGYHGEEQDASFLADRAREIGYPVLIKARAGGGGKGMRRVERQEDFGPALEAARREAESAFGDGSVLLERYLTKPRHIEMQVFGDRHGNIVHLFERDCSLQRRHQKVIEEAPAPGMTAEVRRAMGDAAVRAAQAIGYVGAGTVEFIADVTNGLWPDHFYFMEMNTRLQVEHPVTEAITGIDLVEWQLRVASGEPLPKKQADISMNGWAFEARLYAEDPARGFLPATGRLTELSFPEGTSRVDSGVRQGDTITPYYDPLIAKLIVHGQNRSAALGRLQDALKECRIGGTVTNRDFLIRLTEEHDFRSGHPDTGLIDREIERLTAPVAPGDEALALAAIFSTGALDPNRSTDPWSSLGSWQIWGDAHRMVVIEHADVRATVTLASRGRDQFAVRAGASTLPVLVLDRFEGGARLEVAGQKRLIRFSRDREALTLFHGGRNLVFHVPDGLTGGQSSEIADDELVAPMPGLVKLVRVGAGDAVTKGQALVVMEAMKMELTLSASREGTIANVHVAEGAQVSEGTVLVTLMEEAAQ liuB curated reanno::pseudo1_N1B4:Pf1N1B4_3984 Methylcrotonyl-CoA carboxylase biotin-containing subunit (EC 6.4.1.4) MSAPVLTTLLVANRGEIACRVMRTAKALGLTTVAVHSATDRDARHSREADIRVDLGGSKAADSYLQIDKLIAAAKASGAQAIHPGYGFLSENAGFARAIEAAGLIFLGPPASAIDAMGSKSAAKALMETAGVPLVPGYHGEAQDLETFRDACERIGYPVLLKATAGGGGKGMKVVEDVSQLAEALASAQREALSSFGDSRMLVEKYLLKPRHVEIQVFADQHGNCLYLNERDCSIQRRHQKVVEEAPAPGLSPELRRAMGEAAVRSAQAIGYVGAGTVEFLLDARGEFFFMEMNTRLQVEHPVTEAITGLDLVAWQIRVARGEALPMTQDQVPLIGHAIEVRLYAEDPGNDFLPATGRLALYRESAAGPGRRVDSGVEEGDEISPFYDPMLGKLIAWGEDREQARLRLLSMLDEFAIGGLKTNINFLRRIIGHPAFAAAELDTGFIPRYQEQLLPAPSDLSDEFWQAAAQAFAQSQSSTTRADDLSSPWGIGNGFRAGLPTEITLHLSCEEQDRALTLGDADAHTAQLKGEYLLTEHNGLRRQHRAIRRGDTLYLQWDGELRRIESYDPISAVEASHSHQGGLTAPMNGSIVRVLVEAGQTVEAGAQLVVLEAMKMEHSIRAPHAGIIKALYCQEGEMVSEGSALVELEHA liuB curated reanno::pseudo5_N2C3_1:AO356_01595 Methylcrotonoyl-CoA carboxylase (EC 6.4.1.4) MSAPALTTLLVANRGEIACRVMRTARAMGLTTVAVHSATDRDARHSREADIRVDLGGSKAADSYLQIDKLIAAAKASGAQAIHPGYGFLSENAGFARAIENAGLIFLGPPASAIDAMGSKSAAKTLMETAGVPLVPGYHGEAQDLETFRDAAERIGYPVLLKATAGGGGKGMKVVEDVSQLAEALASAQREAQSSFGDSRMLVEKYLLKPRHVEIQVFADQHGNCLYLNERDCSIQRRHQKVVEEAPAPGLTPQLRRAMGEAAVRAAQAIGYVGAGTVEFLLDARGEFFFMEMNTRLQVEHPVTEAITGLDLVAWQIRVAQGEPLPITQAQVPLLGHAIEVRLYAEDPGNDFLPATGRLALYRESAEGPGRRVDSGVEEGDEISPFYDPMLGKLIAWGEDREQARLRLLSMLDEFVIGGLKTNIGFLRRIVAHPAFAAAELDTGFIPRYQAQLLPEPSELDDAFWFAAAQGVALSLAPHVRGDDAGSPWASTTGMRLGLPRETTLHLSCEGQDRALTLDVTAHCAELEGERLTIEHHGVRRSHRAIRQVDSLYLQWEGDLHRIDLYDPLAAAEASHSHQGGLVAPMNGSIVRVLVGVGQTVEAGAQLVVLEAMKMEHSIRAPKAGVIKALYCQEGEMVSEGSALVAFEE liuB curated reanno::pseudo6_N2E2:Pf6N2E2_2194 Methylcrotonoyl-CoA carboxylase (EC 6.4.1.4) MSAPALTTLLVANRGEIACRVMRTAKAMGLTTVAVHSATDRDARHSREADIRVDLGGSKAADSYLQIDKLIAAAKASGAQAIHPGYGFLSENAGFARAIENAGLIFLGPPASAIDAMGSKSAAKALMETAGVPLVPGYHGEAQDLETFRDAAERIGYPVLLKATAGGGGKGMKVVEDVSQLAEALASAQREAQSSFGDSRMLVEKYLLKPRHVEIQVFADQHGNCLYLNERDCSIQRRHQKVVEEAPAPGLTAQLRQAMGEAAVRAAQAIGYVGAGTVEFLLDARGEFFFMEMNTRLQVEHPVTEAITGLDLVAWQIRVAQGEPLPITQAQVPLLGHAIEVRLYAEDPVNDFLPATGRLALYRESAKGPGRRVDSGVEEGDEISPFYDPMLGKLIAWGENREQARLRLLSMLDEFAIGGLKTNIGFLRRIVAHPAFAAAELDTGFIPRYQAQLLPEPGELDDAFWLAAAQGFALSLAPHIRGDDAGSPWASTTGMRLGLSRETTLHLSCEGQDRALTLDVTAHCAELKGERLTIEHHGVRRSHRAIRQGDSLYLHWAGDLHRIDLYDPLAAAEASHSHQGGLAAPMNGSIVRVLVSVGQPVDAGAQLVVLEAMKMEHSIRAPKAGVIKALYCQEGEMVSEGSALVAFEE liuB ignore BRENDA::Q9I297,metacyc::MONOMER-16074 methylcrotonoyl-CoA carboxylase (EC 6.4.1.4);; methylcrotonyl-CoA carboxylase β-subunit (EC 6.4.1.4) MAILHTQINPRSAEFAANAATMLEQVNALRTLLGRIHEGGGSAAQARHSARGKLLVRERINRLLDPGSPFLELSALAAHEVYGEEVAAAGIVAGIGRVEGVECMIVGNDATVKGGTYYPLTVKKHLRAQAIALENRLPCIYLVDSGGANLPRQDEVFPDREHFGRIFFNQANMSARGIPQIAVVMGSCTAGGAYVPAMSDETVMVREQATIFLAGPPLVKAATGEVVSAEELGGADVHCKVSGVADHYAEDDDHALAIARRCVANLNWRKQGQLQCRAPRAPLYPAEELYGVIPADSKQPYDVREVIARLVDGSEFDEFKALFGTTLVCGFAHLHGYPIAILANNGILFAEAAQKGAHFIELACQRGIPLLFLQNITGFMVGQKYEAGGIAKHGAKLVTAVACARVPKFTVLIGGSFGAGNYGMCGRAYDPRFLWMWPNARIGVMGGEQAAGVLAQVKREQAERAGQQLGVEEEAKIKAPILEQYEHQGHPYYSSARLWDDGVIDPAQTREVLALALSAALNAPIEPTAFGVFRM liuB ignore BRENDA::Q9LDD8 methylcrotonoyl-CoA carboxylase (EC 6.4.1.4) MLRILGRRVVSASKELTSIQQWRIRPGTDSRPDPFRTFRGLQKGFCVGILPDGVDRNSEAFSSNSIAMEGILSELRSHIKKVLAGGGEEAVKRNRSRNKLLPRERIDRLLDPGSSFLELSQLAGHELYEEPLPSGGIITGIGPIHGRICMFMANDPTVKGGTYYPITIKKHLRAQEIAARCRLPCIYLVDSGGAYLPKQAEVFPDKENFGRVFYNESVMSSDGIPQIAIVLGSCTAGGAYIPAMADESVMVKGNGTIFLAGPPLVKAATGEEVSAEDLGGATVHCTVSGVSDYFAQDELHGLAIGRNIVKNLHMAAKQGMEGTFGSKNLVYKEPLYDINELRSIAPVDHKQQFDVRSIIARIVDGSEFDEFKKQYGTTLVTGFARIYGQTVGIIGNNGILFNESALKGAHFIELCSQRKIPLVFLQNITGFMVGSRAEANGIAKAGAKMVMAVSCAKVPKITIITGASFGAGNYAMCGRAYSPDFMFIWPNARIGIMGGAQAAGVLTQIERATKKRQGIKWTEEEEEAFKKKTVDAYEREANPYYSTARLWDDGVIDPCDTRKVLGLCLSAALNRPLEDTRFGVFRM liuB ignore CharProtDB::CH_122289 non-biotin containing subunit of 3-methylcrotonyl-CoA carboxylase; EC 6.4.1.4 MRVSVPLHSIRRSCNSSIANAATRLTPQRLYLSYGRRSSIVQAHLGTQARPIASYTHPHHASAISVLSTAVDTSSPDFRENERQMQEVLNRMNSLHSTISQGGPQKAKDKHVARGKMLPRDRVSALIDPGTSFLELSQLAGHEVYPGEDVPAGGIITGIGTVEGVTCMIVANDSTVKGGTYYPVTVKKHLRAQAIAQENKLPCIYLVDSGGANLPHQADVFPDKEHFGRIFFNQARMSSQGIPQISVVMGPCTAGGAYVPAMSDETIIVENQGTIFLAGPPLVKAATGEVVSAEDLGGGQLHSTISGVTDYLAVDDAHAIVLARRSISNLNYPKAKQPLESNDDIKEPLYDPAELNGIVGTNLRRQIPVHEVIARIVDGSEFAEFKRDYGTTLVTGFARIHGHRVGIVANNGILFSESSLKGAHFIELCAQRNIPLVFLQNISGFMVGADAEKGGIAKNGAKLVTAVACADVPKFTVVFGSSAGAGNYGMCGRAYSPRFLFMWPNAKIGVMGSELSSVMEAVGRTADPELKARIDRESEATFSSARLWDDGIIPPAHTRHVLGLSLAAALGGKSDKDVQTKFGVFRM liuB ignore SwissProt::Q9HCC0,metacyc::ENSG00000131844-MONOMER Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial; MCCase subunit beta; 3-methylcrotonyl-CoA carboxylase 2; 3-methylcrotonyl-CoA carboxylase non-biotin-containing subunit; 3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta; EC 6.4.1.4;; 3-methylcrotonyl-CoA carboxylase β subunit (EC 6.4.1.4) MWAVLRLALRPCARASPAGPRAYHGDSVASLGTQPDLGSALYQENYKQMKALVNQLHERVEHIKLGGGEKARALHISRGKLLPRERIDNLIDPGSPFLELSQFAGYQLYDNEEVPGGGIITGIGRVSGVECMIIANDATVKGGAYYPVTVKKQLRAQEIAMQNRLPCIYLVDSGGAYLPRQADVFPDRDHFGRTFYNQAIMSSKNIAQIAVVMGSCTAGGAYVPAMADENIIVRKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCRKSGVSDHWALDDHHALHLTRKVVRNLNYQKKLDVTIEPSEEPLFPADELYGIVGANLKRSFDVREVIARIVDGSRFTEFKAFYGDTLVTGFARIFGYPVGIVGNNGVLFSESAKKGTHFVQLCCQRNIPLLFLQNITGFMVGREYEAEGIAKDGAKMVAAVACAQVPKITLIIGGSYGAGNYGMCGRAYSPRFLYIWPNARISVMGGEQAANVLATITKDQRAREGKQFSSADEAALKEPIIKKFEEEGNPYYSSARVWDDGIIDPADTRLVLGLSFSAALNAPIEKTDFGIFRM liuB ignore SwissProt::Q9V9A7 Probable methylcrotonoyl-CoA carboxylase beta chain, mitochondrial; MCCase subunit beta; 3-methylcrotonyl-CoA carboxylase 2; 3-methylcrotonyl-CoA carboxylase non-biotin-containing subunit; 3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta; EC 6.4.1.4 MIRLNWLFRSSSVLLRSQVRLLHVGDANVLHSEVDKQSAEYKENAREMASLVGDLRNFTSQVLKGGGQKAIERHTSRGKLLARERINLLLDKGSPFLELSALAGHELYGEEVVNSGGIVTGVGRVCGTECLVVANDATVKGGSYYPITVKKHLRAQEIAQENRLPCIYLVDSGGANLPRQADVFPDKLHFGRIFYNQANMSAQGIPQIAVVMGSCTAGGAYVPAMADESIIVKKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCKTSGVTDHYALDDEHALYLARQIVSNLNLSATNSYNDQLMHSSQVNFQTATPPSAVEEPRYDAEELYGIVGPNLTKSFDVREVIARIVDGSRFTEFKKLYGETLVCGFAKLYGHTVGIVGNNGVLFSESALKGAHFIQLCAQRKIPLVFLQNITGFMVGRDAEANGIAKNGAKMVTAVACANVPKFTVIIGGSYGAGNYGMCGRAYSPRFLYMWPNSRISVMGGTQAANVMAQITEDQRKRAGKEFSEEEAQKLKAPIVEMFEAEGSPYYSTARLWDDGIIDPANTRQILGLSLKAALNNAGQETKFGVFRM liuB ignore reanno::SB2B:6937191 Methylcrotonoyl-CoA carboxylase (EC 6.4.1.4) MTQLTSRVNPRSDEFKQKHDAMAALVADLKDKLAHIEQGGGLVAMERHLSRGKLAPRARVEKLLDPGSPFLELSQFAAFEVYDEDVPAAGIIAGIGRVSGVECMIIANDATVKGGTYYPITVKKHLRAQAIAERCHLPCIYLVDSGGANLPRQDEVFPDRDHFGRIFFNQARMSAKGIPQIAVVMGLCTAGGAYVPAMADESIIVREQGTIFLAGPPLVKAATGEEVSAEELGGGDVHTKISGVADHLAQNDEHALELARKAVSRLNHQKQVELQLSKVKPPKYDINELYGIVGTDLKKPFDVKEVIARIVDDSDFDEFKANYGTTLVCGFARIHGYPVGIVANNGILFSESAQKGAHFIELCCQRKIPLVFLQNITGFMVGKKYEHEGIAKHGAKMVTAVSCATVPKFTVLIGGSYGAGNYGMCGRAFEPTLMWMWPNARISVMGGEQAAGVLATVRKDGLARKGETMSAEEEAKFKAPIIAQYDKEGHPYHASARLWDDGIIDPAQTRDVLGLAISAALNAPIEETRFGVFRM liuB ignore reanno::Smeli:SM_b21122 Methylcrotonoyl-CoA carboxylase (EC 6.4.1.4) MTVLRSHISPSSEEFKANRAAMTEAIATIEDAVRLAAAGGGETARERHVSRGKLLPRDRLATLIDPGTPFLEVGATAAYGMYNDDAPGAGLITGIGRISARECMIVCNDPTVKGGTYYPLTVKKHLRAQEIAAENRLPCVYLVDSGGANLPNQDEVFPDRDHFGRIFYNQANMSAAGIPQIAVVMGSCTAGGAYVPAMSDEAIIVEKQGTIFLAGPPLVRAATGEVVSAEDLGGADVHTRLSGVADHLARDDAHALALARRAVSALNREKPWTVERIEPEPPLYDPEEIAGIVPADLKTPYEIREVIARLVDGSRFDEFKARFGTTLVCGFAHVHGIPVGIVANNGVLFSESAVKGAHFVELCAQRRIPLVFLQNITGFMVGRKYETEGIAKHGAKLVTAVATVKVPKITMLVGGSFGAGNYGMCGRAFSPRFLWTWPNSRISVMGGEQAAGVLSSVRGEALKRSGKPWSEEEEARFRQPVLDLFERQSHPLYASARLWDDGVIDPRKSRDVLALSLSAALNAPIEETRFGLFRM liuB ignore reanno::psRCH2:GFF1050 Methylcrotonyl-CoA carboxylase carboxyl transferase subunit (EC 6.4.1.4) MAILHTQINIRSPEFAANSAAMLEQVNDLRALLGRVSEGGGATAQQRHVSRGKLLVRERIDTLLDAGSAFLELAPLAAHEVYGEDVAAAGVVAGIGRVEGIECMIIANDATVKGGTYYPLTVKKHLRAQTVARENRLPCIYLVDSGGANLPRQDEVFPDREHFGRIFFNQANMSAMGIPQIAVVMGSCTAGGAYVPAMADETIMVRNQATIFLAGPPLVKAATGEVVTAEELGGADVHCKTSGVADHYAENDEHALSIARRCVANLNWRKLGQLQTREPRAPLYAADELYGVIPAQAKQPYDVREVIARLVDGSEFDEFKALFGTTLVCGFAHLHGYPIAILANNGILFAEAAQKGAHFIELACQRGIPLLFLQNITGFMVGQKYEAGGIAKHGAKLVTAVACAQVPKFTVLIGGSFGAGNYGMCGRAYDPRFLWMWPNARIAVMGGEQAAGVLAQVKQEQSERAGKSLGDDEVAAIKQPILEQYERQGHPYYSSARLWDDGVIDPAQTREVLGLALSAALNAPIEPTRFGVFRM liuB ignore reanno::pseudo5_N2C3_1:AO356_01585 Methylcrotonoyl-CoA carboxylase (EC 6.4.1.4) MATLHTQLNPRSPEFIANREAMLGHVEALRTLLAQIRQGGGLKAQERHTSRGKLLPRERINRLLDPGSPFLEISPLAAHDVYGEDVPAAGVIAGIGRVEGVECMIVANDATVKGGSYYPLTVKKHLRAQTIAQQNRLPCIYLVDSGGANLPRQDEVFPDREHFGRIFFNQANMSAQGIPQIAVVMGSCTAGGAYVPAMADEAIMVRQQATIFLAGPPLVKAATGEVVSAEDLGGADVHCKISGVADHYADSDEHALALARRSVANLNWRKLGELQQRQPIAPLYSSDELYGVVSADAKQPFDVREVIARLVDGSVFNEFKALFGTTLVCGFAHLHGYPVAILANNGILFAEAAQKGAHFIELACQRGIPLLFLQNITGFMVGQKYEAGGIAKHGAKLVTAVACAKVPKFTVIIGGSFGAGNYGMCGRAYDPRFLWMWPNARIGVMGAEQAAGVLVQVKREQAERSGHPFSAEQEAEIKQPILDQYEEQGHPYYSSARLWDDGVIDPAQTRDVLGLALSASLNAPIEPSRFGVFRM liuB ignore reanno::pseudo6_N2E2:Pf6N2E2_2192 Methylcrotonoyl-CoA carboxylase (EC 6.4.1.4) MATLHTQLNPRSPEFIANRDAMLGHVEALRTLLAQIRQGGGPKAQERHTSRGKLLPRERINRLLDPGSPFLEISPLAAHEVYGEDVPAAGVIAGIGRVEGVECMIVANDATVKGGSYYPLTVKKHLRAQTIAQQNRLPCIYLVDSGGANLPRQDEVFPDREHFGRIFFNQANMSAQGIPQIAVVMGSCTAGGAYVPAMADEAIMVRQQATIFLAGPPLVKAATGEVVSAEDLGGADVHCKISGVADHYADSDEHALALARRSVANLNWRKQGELQHRLPIAPLYSGEELYGVVSADAKQPFDVREVIARLVDGSVFDEFKALFGTTLVCGFAHLHGYPIAILANNGILFAEAAQKGAHFIELACQRGIPLLFLQNITGFMVGQKYEAGGIAKHGAKLVTAVACAKVPKFTVIIGGSFGAGNYGMCGRAYDPRFLWMWPNARIGVMGAEQAAGVLVQVKREQAERSGHPFSAEQEAEIKQPILDQYEEQGHPYYSSARLWDDGVIDPAQTRDVLGLALSASLNAPIEPSRFGVFRM liuC uniprot Q92VJ6 SubName: Full=Putative enoyl-CoA hydratase protein {ECO:0000313|EMBL:CAC49105.1}; EC=4.2.1.17 {ECO:0000313|EMBL:CAC49105.1}; MTFDTIRCAIDQRGVARVTLARSEKHNALSATMIGELTAVVGRLATDASIRAVILDAEGKSFCAGGDLDWMRQQFSADRPTRIAEATRLAMMLKALNDLPKPLIARVHGNAFGGGVGLISVCDTVIAASGAQFGLTETRLGLIPATISPYVIARTGEARARPLFMSARVFGAEEAKVAGFVTTVVDGTMLDGAVEAAVTAYLVAAPGAAGRAKRLARSLGLPITDAVIAATIEQLADTWETDEAREGVSAFFERRNPSWRQ liuC curated BRENDA::F4JML5 methylglutaconyl-CoA hydratase (EC 4.2.1.18) MSFVKYLRRDNLLQLAGKPSLSRNYILQTCRTLIIETSPPEFVKLNRLSGSDSGIIEVNLDRPVTKNAINKEMLKSLQNAFESIHQDNSARVVMIRSLVPGVFCAGADLKERRTMSPSEVHTYVNSLRYMFSFIEALSIPTIAAIEGAALGGGLEMALACDLRICGENAVFGLPETGLAIIPGAGGTQRLSRLVGRSVSKELIFTGRKIDAIEAANKGLVNICVTAGEAHEKAIEMAQQINEKGPLAIKMAKKAIDEGIETNMASGLEVEEMCYQKLLNTQDRLEGLAAFAEKRKPLYTGN liuC curated BRENDA::Q13825,SwissProt::Q13825,metacyc::HS07490-MONOMER methylglutaconyl-CoA hydratase (EC 4.2.1.18);; Methylglutaconyl-CoA hydratase, mitochondrial; AU-specific RNA-binding enoyl-CoA hydratase; AU-binding protein/enoyl-CoA hydratase; Itaconyl-CoA hydratase; EC 4.2.1.18; EC 4.2.1.56;; methylglutaconyl-CoA hydratase subunit (EC 4.2.1.18) MAAAVAAAPGALGSLHAGGARLVAACSAWLCPGLRLPGSLAGRRAGPAIWAQGWVPAAGGPAPKRGYSSEMKTEDELRVRHLEEENRGIVVLGINRAYGKNSLSKNLIKMLSKAVDALKSDKKVRTIIIRSEVPGIFCAGADLKERAKMSSSEVGPFVSKIRAVINDIANLPVPTIAAIDGLALGGGLELALACDIRVAASSAKMGLVETKLAIIPGGGGTQRLPRAIGMSLAKELIFSARVLDGKEAKAVGLISHVLEQNQEGDAAYRKALDLAREFLPQGPVAMRVAKLAINQGMEVDLVTGLAIEEACYAQTIPTKDRLEGLLAFKEKRPPRYKGE liuC curated BRENDA::Q1D5Y4 methylglutaconyl-CoA hydratase (EC 4.2.1.18) MPEFKVDARGPIEIWTIDGESRRNAISRAMLKELGELVTRVSSSRDVRAVVITGAGDKAFCAGADLKERATMAEDEVRAFLDGLRRTFRAIEKSDCVFIAAINGAALGGGTELALACDLRVAAPAAELGLTEVKLGIIPGGGGTQRLARLVGPGRAKDLILTARRINAAEAFSVGLANRLAPEGHLLAVAYGLAESVVENAPIAVATAKHAIDEGTGLELDDALALELRKYEEILKTEDRLEGLRAFAEKRAPVYKGR liuC curated CharProtDB::CH_122457 3-hydroxy-3-methylglutaryl-coenzyme A lyase/3-methylglutaconyl-coenzyme A hydratase; EC 4.1.3.4; EC 4.2.1.18 MQNSTKTVRIVEVGPRDGLQNIPQSIDSTIKLDLIRRLRDAGLQTIELTSFVSPRAIPQLADAQVVVQNADIQKLLKNPKLRLPVLVPNLKGLERALHNGIKEVAVFISATEGFSRANINCTVDEGLERARQVASRAASAGLSVRGYVSCIFADPYDGPTRPSSVLRCTKALLDAGCYEVSLGDTLGIGTPADVRWLITYLQDNGVPLEMLAGHFHDTYGGAVANVWEAYKCGLRMFDSSVAGLGGCPXALGAKGNVASEDLVYMFERSGIHTGVDLSKLVETGEWISRQLSIAISSRAGAALWAMRKQTAVPKSPKVSVSWKLVKQTEGLQLFRSGVNLRINLNRPKNGNALTAIMAQDLTEAVTNAGRDATISRIILTGSGKFFCTGMDLGKGSTAVGQGGSSSNAQFDRLTNLFEAIDQSPKVTIACLNGPAFGGGVGLAFACDMRFAVRAASVTLSEVKLGLCPATISKYVIREFGIALSREAMLSARPVSAGELKARGLVVELADNAEALPGLLDQFLTQLKAASPEASRMSKELIRLAWAHGGKEEQAKGIRALFDGMMRPDGDGAHGVKEFQAKRSVDWDAYTLRRVDSAKV liuC curated SwissProt::Q9JLZ3 Methylglutaconyl-CoA hydratase, mitochondrial; AU-specific RNA-binding enoyl-CoA hydratase; AU-binding enoyl-CoA hydratase; muAUH; Itaconyl-CoA hydratase; EC 4.2.1.18; EC 4.2.1.56 MAAAAPGALGALRTGRVRLVAACCARLGPAAWARGTAPRRGYSSEVKTEDELRVRHLEEENRGIVVLGINRAYGKNALSKNLLKMLSKAVDALKSDKKVRTIIIRSEVPGIFCAGADLKERAKMHSSEVGPFVSKIRSVINDIANLPVPTIAAIDGLALGGGLELALACDIRVAASSAKMGLVETKLAIIPGGGGTQRLPRAIGMSLAKELIFSARVLDGQEAKAVGLISHVLEQNQEGDAAYRKALDLAREFLPQGPVAMRVAKLAINQGMEVDLVTGLAIEEACYAQTISTKDRLEGLLAFKEKRPPRYKGE liuC curated metacyc::MONOMER-16071 3-methylglutaconyl-CoA hydratase (EC 4.2.1.18) MSDFSTLEVIRDPRGFATLWLSREDKNNAFNAQMIRELIVAIDQLAEDASLRFVLLRGRGRHFSAGADLAWMQQSAQLDFNTNLDDAHELGELMYALHRLKAPTLAVVQGAAFGGALGLISCCDMAIGAEDAQLCLSEVRIGLAPAVISPFVVKAIGERAARRYALTAERFTGVRARELGLLAEVYPASELDDHVEAWVSNLLQNSPQALRATKDLLREVDDGELSPALRRYCENTIARIRVSAEGQEGLRAFLEKRRPAWQTVDKKEPRP liuC curated reanno::Pedo557:CA265_RS09125 Methylglutaconyl-CoA hydratase (EC 4.2.1.18) MENLVLYQVAERIATITINRPEKKNALNPQLIAELTAAFIKASEDDLVKVVILNANGDAFSAGADLAYLQQLQYNTFEENVADSNHLKKLFTTIYYLPKVVIAQVEGHAIAGGCGLATICDIVFATPESNFGYTEVKIGFVPAIVSCFLKEKVSESIAKEILLTGKIFSAEEALKYNLINFVTNSSDIHQIVREFALSLCSGSSGNSLMITKQLITQTTNPLLEKCLETAVQINARVRESEDFKKGISSFLNKEKINW liuC curated reanno::pseudo5_N2C3_1:AO356_01590 Methylglutaconyl-CoA hydratase (EC 4.2.1.18) MDNFNTLELHSDPRGVATLWLSRESKNNAFNAEMIRELILALDHVSSDPNLRFLLIRGRGKHFSAGADLAWMQQSAELDYHTNLDDARELAELMYNLAKLKIPTLAVVQGAAFGGALGLISACDMAIGADEAQFCLSEVRIGLAPAVISPFVVQAIGERAARRYALTAERFDGQRAKEIGLLSESYPVETLDQQVEQWIDNLLLNSPAAMRASKELLREVGNGALTPALRRYTENAIARIRVSPEGQEGLRAFLQKRAPNWQAESNNNKEPRR liuC curated reanno::pseudo6_N2E2:Pf6N2E2_2193 Methylglutaconyl-CoA hydratase (EC 4.2.1.18) MDNFNTLELHSDPRGVATLWLSRESKNNAFNAEMIRELILALDHVSSDPNLRFLLIRGRGKHFSAGADLAWMQQSAELDYHTNLDDARELAELMYNLAKLKIPTLAVVQGAAFGGALGLISACDMAIGADEAQFCLSEVRIGLAPAVISPFVVQAIGERAARRYALTAERFDGQRAKEIGLLSESYPAEVLDQQVEQWIDNLLLNSPAAMRASKELLREVGNGALTPALRRYTENAIARIRVSPEGQEGLRAFLQKRAPNWQAESNNKEPRR liuD curated BRENDA::Q9I297,metacyc::MONOMER-16074 methylcrotonoyl-CoA carboxylase (EC 6.4.1.4);; methylcrotonyl-CoA carboxylase β-subunit (EC 6.4.1.4) MAILHTQINPRSAEFAANAATMLEQVNALRTLLGRIHEGGGSAAQARHSARGKLLVRERINRLLDPGSPFLELSALAAHEVYGEEVAAAGIVAGIGRVEGVECMIVGNDATVKGGTYYPLTVKKHLRAQAIALENRLPCIYLVDSGGANLPRQDEVFPDREHFGRIFFNQANMSARGIPQIAVVMGSCTAGGAYVPAMSDETVMVREQATIFLAGPPLVKAATGEVVSAEELGGADVHCKVSGVADHYAEDDDHALAIARRCVANLNWRKQGQLQCRAPRAPLYPAEELYGVIPADSKQPYDVREVIARLVDGSEFDEFKALFGTTLVCGFAHLHGYPIAILANNGILFAEAAQKGAHFIELACQRGIPLLFLQNITGFMVGQKYEAGGIAKHGAKLVTAVACARVPKFTVLIGGSFGAGNYGMCGRAYDPRFLWMWPNARIGVMGGEQAAGVLAQVKREQAERAGQQLGVEEEAKIKAPILEQYEHQGHPYYSSARLWDDGVIDPAQTREVLALALSAALNAPIEPTAFGVFRM liuD curated BRENDA::Q9LDD8 methylcrotonoyl-CoA carboxylase (EC 6.4.1.4) MLRILGRRVVSASKELTSIQQWRIRPGTDSRPDPFRTFRGLQKGFCVGILPDGVDRNSEAFSSNSIAMEGILSELRSHIKKVLAGGGEEAVKRNRSRNKLLPRERIDRLLDPGSSFLELSQLAGHELYEEPLPSGGIITGIGPIHGRICMFMANDPTVKGGTYYPITIKKHLRAQEIAARCRLPCIYLVDSGGAYLPKQAEVFPDKENFGRVFYNESVMSSDGIPQIAIVLGSCTAGGAYIPAMADESVMVKGNGTIFLAGPPLVKAATGEEVSAEDLGGATVHCTVSGVSDYFAQDELHGLAIGRNIVKNLHMAAKQGMEGTFGSKNLVYKEPLYDINELRSIAPVDHKQQFDVRSIIARIVDGSEFDEFKKQYGTTLVTGFARIYGQTVGIIGNNGILFNESALKGAHFIELCSQRKIPLVFLQNITGFMVGSRAEANGIAKAGAKMVMAVSCAKVPKITIITGASFGAGNYAMCGRAYSPDFMFIWPNARIGIMGGAQAAGVLTQIERATKKRQGIKWTEEEEEAFKKKTVDAYEREANPYYSTARLWDDGVIDPCDTRKVLGLCLSAALNRPLEDTRFGVFRM liuD curated CharProtDB::CH_122289 non-biotin containing subunit of 3-methylcrotonyl-CoA carboxylase; EC 6.4.1.4 MRVSVPLHSIRRSCNSSIANAATRLTPQRLYLSYGRRSSIVQAHLGTQARPIASYTHPHHASAISVLSTAVDTSSPDFRENERQMQEVLNRMNSLHSTISQGGPQKAKDKHVARGKMLPRDRVSALIDPGTSFLELSQLAGHEVYPGEDVPAGGIITGIGTVEGVTCMIVANDSTVKGGTYYPVTVKKHLRAQAIAQENKLPCIYLVDSGGANLPHQADVFPDKEHFGRIFFNQARMSSQGIPQISVVMGPCTAGGAYVPAMSDETIIVENQGTIFLAGPPLVKAATGEVVSAEDLGGGQLHSTISGVTDYLAVDDAHAIVLARRSISNLNYPKAKQPLESNDDIKEPLYDPAELNGIVGTNLRRQIPVHEVIARIVDGSEFAEFKRDYGTTLVTGFARIHGHRVGIVANNGILFSESSLKGAHFIELCAQRNIPLVFLQNISGFMVGADAEKGGIAKNGAKLVTAVACADVPKFTVVFGSSAGAGNYGMCGRAYSPRFLFMWPNAKIGVMGSELSSVMEAVGRTADPELKARIDRESEATFSSARLWDDGIIPPAHTRHVLGLSLAAALGGKSDKDVQTKFGVFRM liuD curated SwissProt::Q9HCC0,metacyc::ENSG00000131844-MONOMER Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial; MCCase subunit beta; 3-methylcrotonyl-CoA carboxylase 2; 3-methylcrotonyl-CoA carboxylase non-biotin-containing subunit; 3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta; EC 6.4.1.4;; 3-methylcrotonyl-CoA carboxylase β subunit (EC 6.4.1.4) MWAVLRLALRPCARASPAGPRAYHGDSVASLGTQPDLGSALYQENYKQMKALVNQLHERVEHIKLGGGEKARALHISRGKLLPRERIDNLIDPGSPFLELSQFAGYQLYDNEEVPGGGIITGIGRVSGVECMIIANDATVKGGAYYPVTVKKQLRAQEIAMQNRLPCIYLVDSGGAYLPRQADVFPDRDHFGRTFYNQAIMSSKNIAQIAVVMGSCTAGGAYVPAMADENIIVRKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCRKSGVSDHWALDDHHALHLTRKVVRNLNYQKKLDVTIEPSEEPLFPADELYGIVGANLKRSFDVREVIARIVDGSRFTEFKAFYGDTLVTGFARIFGYPVGIVGNNGVLFSESAKKGTHFVQLCCQRNIPLLFLQNITGFMVGREYEAEGIAKDGAKMVAAVACAQVPKITLIIGGSYGAGNYGMCGRAYSPRFLYIWPNARISVMGGEQAANVLATITKDQRAREGKQFSSADEAALKEPIIKKFEEEGNPYYSSARVWDDGIIDPADTRLVLGLSFSAALNAPIEKTDFGIFRM liuD curated SwissProt::Q9V9A7 Probable methylcrotonoyl-CoA carboxylase beta chain, mitochondrial; MCCase subunit beta; 3-methylcrotonyl-CoA carboxylase 2; 3-methylcrotonyl-CoA carboxylase non-biotin-containing subunit; 3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta; EC 6.4.1.4 MIRLNWLFRSSSVLLRSQVRLLHVGDANVLHSEVDKQSAEYKENAREMASLVGDLRNFTSQVLKGGGQKAIERHTSRGKLLARERINLLLDKGSPFLELSALAGHELYGEEVVNSGGIVTGVGRVCGTECLVVANDATVKGGSYYPITVKKHLRAQEIAQENRLPCIYLVDSGGANLPRQADVFPDKLHFGRIFYNQANMSAQGIPQIAVVMGSCTAGGAYVPAMADESIIVKKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCKTSGVTDHYALDDEHALYLARQIVSNLNLSATNSYNDQLMHSSQVNFQTATPPSAVEEPRYDAEELYGIVGPNLTKSFDVREVIARIVDGSRFTEFKKLYGETLVCGFAKLYGHTVGIVGNNGVLFSESALKGAHFIQLCAQRKIPLVFLQNITGFMVGRDAEANGIAKNGAKMVTAVACANVPKFTVIIGGSYGAGNYGMCGRAYSPRFLYMWPNSRISVMGGTQAANVMAQITEDQRKRAGKEFSEEEAQKLKAPIVEMFEAEGSPYYSTARLWDDGIIDPANTRQILGLSLKAALNNAGQETKFGVFRM liuD curated reanno::SB2B:6937191 Methylcrotonoyl-CoA carboxylase (EC 6.4.1.4) MTQLTSRVNPRSDEFKQKHDAMAALVADLKDKLAHIEQGGGLVAMERHLSRGKLAPRARVEKLLDPGSPFLELSQFAAFEVYDEDVPAAGIIAGIGRVSGVECMIIANDATVKGGTYYPITVKKHLRAQAIAERCHLPCIYLVDSGGANLPRQDEVFPDRDHFGRIFFNQARMSAKGIPQIAVVMGLCTAGGAYVPAMADESIIVREQGTIFLAGPPLVKAATGEEVSAEELGGGDVHTKISGVADHLAQNDEHALELARKAVSRLNHQKQVELQLSKVKPPKYDINELYGIVGTDLKKPFDVKEVIARIVDDSDFDEFKANYGTTLVCGFARIHGYPVGIVANNGILFSESAQKGAHFIELCCQRKIPLVFLQNITGFMVGKKYEHEGIAKHGAKMVTAVSCATVPKFTVLIGGSYGAGNYGMCGRAFEPTLMWMWPNARISVMGGEQAAGVLATVRKDGLARKGETMSAEEEAKFKAPIIAQYDKEGHPYHASARLWDDGIIDPAQTRDVLGLAISAALNAPIEETRFGVFRM liuD curated reanno::Smeli:SM_b21122 Methylcrotonoyl-CoA carboxylase (EC 6.4.1.4) MTVLRSHISPSSEEFKANRAAMTEAIATIEDAVRLAAAGGGETARERHVSRGKLLPRDRLATLIDPGTPFLEVGATAAYGMYNDDAPGAGLITGIGRISARECMIVCNDPTVKGGTYYPLTVKKHLRAQEIAAENRLPCVYLVDSGGANLPNQDEVFPDRDHFGRIFYNQANMSAAGIPQIAVVMGSCTAGGAYVPAMSDEAIIVEKQGTIFLAGPPLVRAATGEVVSAEDLGGADVHTRLSGVADHLARDDAHALALARRAVSALNREKPWTVERIEPEPPLYDPEEIAGIVPADLKTPYEIREVIARLVDGSRFDEFKARFGTTLVCGFAHVHGIPVGIVANNGVLFSESAVKGAHFVELCAQRRIPLVFLQNITGFMVGRKYETEGIAKHGAKLVTAVATVKVPKITMLVGGSFGAGNYGMCGRAFSPRFLWTWPNSRISVMGGEQAAGVLSSVRGEALKRSGKPWSEEEEARFRQPVLDLFERQSHPLYASARLWDDGVIDPRKSRDVLALSLSAALNAPIEETRFGLFRM liuD curated reanno::psRCH2:GFF1050 Methylcrotonyl-CoA carboxylase carboxyl transferase subunit (EC 6.4.1.4) MAILHTQINIRSPEFAANSAAMLEQVNDLRALLGRVSEGGGATAQQRHVSRGKLLVRERIDTLLDAGSAFLELAPLAAHEVYGEDVAAAGVVAGIGRVEGIECMIIANDATVKGGTYYPLTVKKHLRAQTVARENRLPCIYLVDSGGANLPRQDEVFPDREHFGRIFFNQANMSAMGIPQIAVVMGSCTAGGAYVPAMADETIMVRNQATIFLAGPPLVKAATGEVVTAEELGGADVHCKTSGVADHYAENDEHALSIARRCVANLNWRKLGQLQTREPRAPLYAADELYGVIPAQAKQPYDVREVIARLVDGSEFDEFKALFGTTLVCGFAHLHGYPIAILANNGILFAEAAQKGAHFIELACQRGIPLLFLQNITGFMVGQKYEAGGIAKHGAKLVTAVACAQVPKFTVLIGGSFGAGNYGMCGRAYDPRFLWMWPNARIAVMGGEQAAGVLAQVKQEQSERAGKSLGDDEVAAIKQPILEQYERQGHPYYSSARLWDDGVIDPAQTREVLGLALSAALNAPIEPTRFGVFRM liuD curated reanno::pseudo5_N2C3_1:AO356_01585 Methylcrotonoyl-CoA carboxylase (EC 6.4.1.4) MATLHTQLNPRSPEFIANREAMLGHVEALRTLLAQIRQGGGLKAQERHTSRGKLLPRERINRLLDPGSPFLEISPLAAHDVYGEDVPAAGVIAGIGRVEGVECMIVANDATVKGGSYYPLTVKKHLRAQTIAQQNRLPCIYLVDSGGANLPRQDEVFPDREHFGRIFFNQANMSAQGIPQIAVVMGSCTAGGAYVPAMADEAIMVRQQATIFLAGPPLVKAATGEVVSAEDLGGADVHCKISGVADHYADSDEHALALARRSVANLNWRKLGELQQRQPIAPLYSSDELYGVVSADAKQPFDVREVIARLVDGSVFNEFKALFGTTLVCGFAHLHGYPVAILANNGILFAEAAQKGAHFIELACQRGIPLLFLQNITGFMVGQKYEAGGIAKHGAKLVTAVACAKVPKFTVIIGGSFGAGNYGMCGRAYDPRFLWMWPNARIGVMGAEQAAGVLVQVKREQAERSGHPFSAEQEAEIKQPILDQYEEQGHPYYSSARLWDDGVIDPAQTRDVLGLALSASLNAPIEPSRFGVFRM liuD curated reanno::pseudo6_N2E2:Pf6N2E2_2192 Methylcrotonoyl-CoA carboxylase (EC 6.4.1.4) MATLHTQLNPRSPEFIANRDAMLGHVEALRTLLAQIRQGGGPKAQERHTSRGKLLPRERINRLLDPGSPFLEISPLAAHEVYGEDVPAAGVIAGIGRVEGVECMIVANDATVKGGSYYPLTVKKHLRAQTIAQQNRLPCIYLVDSGGANLPRQDEVFPDREHFGRIFFNQANMSAQGIPQIAVVMGSCTAGGAYVPAMADEAIMVRQQATIFLAGPPLVKAATGEVVSAEDLGGADVHCKISGVADHYADSDEHALALARRSVANLNWRKQGELQHRLPIAPLYSGEELYGVVSADAKQPFDVREVIARLVDGSVFDEFKALFGTTLVCGFAHLHGYPIAILANNGILFAEAAQKGAHFIELACQRGIPLLFLQNITGFMVGQKYEAGGIAKHGAKLVTAVACAKVPKFTVIIGGSFGAGNYGMCGRAYDPRFLWMWPNARIGVMGAEQAAGVLVQVKREQAERSGHPFSAEQEAEIKQPILDQYEEQGHPYYSSARLWDDGVIDPAQTRDVLGLALSASLNAPIEPSRFGVFRM liuD ignore BRENDA::Q42523,SwissProt::Q42523 methylcrotonoyl-CoA carboxylase (EC 6.4.1.4);; Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial; MCCase subunit alpha; 3-methylcrotonyl-CoA carboxylase 1; 3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha; EC 6.4.1.4 MSMMTVWALRRNVRRKNHSMLVRYISGSASMKPKEQCIEKILVANRGEIACRIMRTAKRLGIQTVAVYSDADRDSLHVKSADEAVRIGPPSARLSYLSGVTIMEAAARTGAQAIHPGYGFLSESSDFAQLCEDSGLTFIGPPASAIRDMGDKSASKRIMGAAGVPLVPGYHGHEQDIDHMKSEAEKIGYPIIIKPTHGGGGKGMRIVQSGKDFADSFLGAQREAAASFGVNTILLEKYITRPRHIEVQIFGDKHGNVLHLYERDCSVQRRHQKIIEEAPAPNISEKFRANLGQAAVSAARAVGYYNAGTVEFIVDTESDQFYFMEMNTRLQVEHPVTEMIVGQDLVEWQIRVANGEPLPLSQSEVPMSGHAFEARIYAENVPKGFLPATGVLNHYRPVAVSPSVRVETGVEQGDTVSMHYDPMIAKLVVWGGNRGEALVKLKDCLSNFQVAGVPTNINFLQKLASHKEFAVGNVETHFIEHHKSDLFADESNPAATEVAYKAVKHSAALVAACISTIEHSTWNESNHGKVPSIWYSNPPFRVHHEAKQTIELEWNNECEGTGSNLISLGVRYQPDGSYLIEEGNDSPSLELRVTRAGKCDFRVEAAGLSMNVSLAAYLKDGYKHIHIWHGSEHHQFKQKVGIEFSEDEEGVQHRTSSETSSHPPGTIVAPMAGLVVKVLVENEAKVDQGQPILVLEAMKMEHVVKAPSSGSIQDLKVKAGQQVSDGSALFRIKG liuD ignore BRENDA::Q9I299,metacyc::MONOMER-16075 methylcrotonoyl-CoA carboxylase (subunit 2/2) (EC 6.4.1.4);; methylcrotonyl-CoA carboxylase α-subunit (EC 6.4.1.4) MNPDYRSIQRLLVANRGEIACRVMRSARALGIGSVAVHSDIDRHARHVAEADIAVDLGGAKPADSYLRGDRIIAAALASGAQAIHPGYGFLSENADFARACEEAGLLFLGPPAAAIDAMGSKSAAKALMEEAGVPLVPGYHGEAQDLETFRREAGRIGYPVLLKAAAGGGGKGMKVVEREAELAEALSSAQREAKAAFGDARMLVEKYLLKPRHVEIQVFADRHGHCLYLNERDCSIQRRHQKVVEEAPAPGLGAELRRAMGEAAVRAAQAIGYVGAGTVEFLLDERGQFFFMEMNTRLQVEHPVTEAITGLDLVAWQIRVARGEALPLTQEQVPLNGHAIEVRLYAEDPEGDFLPASGRLMLYREAAAGPGRRVDSGVREGDEVSPFYDPMLAKLIAWGETREEARQRLLAMLAETSVGGLRTNLAFLRRILGHPAFAAAELDTGFIARHQDDLLPAPQALPEHFWQAAAEAWLQSEPGHRRDDDPHSPWSRNDGWRSALARESDLMLRCRDERRCVRLRHASPSQYRLDGDDLVSRVDGVTRRSAALRRGRQLFLEWEGELLAIEAVDPIAEAEAAHAHQGGLSAPMNGSIVRVLVEPGQTVEAGATLVVLEAMKMEHSIRAPHAGVVKALYCSEGELVEEGTPLVELDENQA liuD ignore CharProtDB::CH_122249 3-methylcrotonyl-CoA carboxylase biotin-containig subunit; EC 6.4.1.4 MPLSSLLRTSARLGQTVVARRSRRTASTVTSNSSSNFRALDSILIANRGEIALRVGRTAAQHGIRVTTLYTDPDSQAQHALSTPYAFNLGSVSAYLDGDRIIEIAKAQGCQGIHPGYGFLSENSEFARKCTEAGLVFIGPPWKAIEDMGDKRCSKHIMTAAGVPCVPSYHGENQDPNFLEAEADKIKYPVLIKAIKGGGGKGMRIARSKEEFQAQLQSAKSEAMNSFGDDHVLVEKYITTPRHIEVQVFADKHGNCVALGERDCSIQRRHQKILEESPAPHLPDATRKDIWAKARSAALAVRYEGAGTVEFIFDNDTGEFFFMEMNTRLQVEHPVTEMVTGQDLVHWQLKVAEGAELPLTQEEVEANIATHGHAIEARIYAENPAQGFIPDSGALLHVRTPATTEDVRIDAGFVQGDEVSAHYDPMIAKLIVRGADRQEAIRKLACSIGRVEVAGPATNIEFLKSVCKSADFISGKVETGYIEKHHDELFAQSPIEPEVLAQVALACLHDDARLAAQKATNFQGSAVGFGPGFQQHHMTFTNSASANNEAFDVKVQQTGENVFNVKIGEHTFEQVTSHPNADFRIITSFFPHTRLDTTVIRDGDSIVVFQRGRQYRLTTPRAKWMEKALGMKDVTNSVLAPMPCKVLRVEVQAGDTVEKDQPLVVIESMKMETVIRSPQRGKLPKSSIKKETNAKAGHRLWSLLVKTKRRRNRYGRIEAMLHQ liuD ignore SwissProt::Q2QMG2 Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial; MCCase subunit alpha; 3-methylcrotonyl-CoA carboxylase 1; 3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha; EC 6.4.1.4 MASRLLLLPRRRSRHGGASLLLARLLSSSSSEAGGGGAVEKVLVANRGEIACRVMRTARRLGIPTVAVYSDADRGALHVRAADEAVRLGPPPARESYLNASAIVDAALRTGAKAIHPGYGFLSESADFAQLCKAEGLTFIGPPPSAIRDMGDKSASKRIMGAAGVPLVPGYHGAEQDIELLKLEANKIGYPVLIKPTHGGGGKGMRIVQRPEDFVDSVLSAQREAAASFGINTLLVEKYITQPRHIEVQIFGDQHGNVIHLYERDCSLQRRHQKIIEEAPAPNVTAQFRSHIGEAAVSAAKAVGYYSAGTVEFIVDTLSGEFYFMEMNTRLQVEHPVTEMIVGQDLVEWQIRIANGECLPLSQEQVPLNGHAFEARIYAENVPRGFLPATGTLHHYRPVPSTATVRVETGVEEGDTVSMHYDPMIAKLVVWGESRNAALVKLKNSLSNFQIAGLPTNVGFLQELAGHSAFEKGLVDTHFIERYQNDLLSTSTQALSGSHEAEELGAILAAACICKKDHVSSEVSLHDKKLSMWYAHPPFRMHHFAKRLMEFELDRELGGSSDDLLKLSVTYRSDGTYFVETEDGSSPGLDVKVDSRGDHDFRVDVGGLQTDVTLAFYSKDNCNHIHIWHGKHHHHYRQTLRAEQSPDDSSQPSASSEARSHPKGSVLAPMAGLVVKVLLKDGARVEEGQPVMVMEAMKMEHVVKAPCAGYVEGLKATAGQQVFDSSVLFTVKENKPN liuD ignore SwissProt::Q96RQ3,metacyc::ENSG00000078070-MONOMER Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial; MCCase subunit alpha; 3-methylcrotonyl-CoA carboxylase 1; 3-methylcrotonyl-CoA carboxylase biotin-containing subunit; 3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha; EC 6.4.1.4;; 3-methylcrotonyl-CoA carboxylase α subunit (EC 6.4.1.4) MAAASAVSVLLVAAERNRWHRLPSLLLPPRTWVWRQRTMKYTTATGRNITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTSAAQAIHPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPRADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQHHKQLLLSRKAAAKESLCQAALGLILKEKAMTDTFTLQAHDQFSPFSSSSGRRLNISYTRNMTLKDGKNNVAIAVTYNHDGSYSMQIEDKTFQVLGNLYSEGDCTYLKCSVNGVASKAKLIILENTIYLFSKEGSIEIDIPVPKYLSSVSSQETQGGPLAPMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEFEEEESDKRESE liuD ignore SwissProt::Q99MR8 Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial; MCCase subunit alpha; 3-methylcrotonyl-CoA carboxylase 1; 3-methylcrotonyl-CoA carboxylase biotin-containing subunit; 3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha; EC 6.4.1.4 MAAAALLAAVDRNQLRRVPILLLQPREWAWKLRTMKYGTTPGGSITKVLIANRGEIACRVIRTAKKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPGYGFLSENMEFAELCKQEGIIFIGPPSSAIRDMGIKSTSKSIMAAAGVPVVEGYHGKDQSDQCLREHAGKIGYPVMIKAVRGGGGKGMRIVRSEREFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGINPEVRRKLGEAAVRAAKAVKYVGAGTVEFIMDSRHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIPLSQEEIPLQGHAFEARIYAEDPDNNFMPGAGPLVHLSTPSADMSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQSALSKLRYCLHQYNIVGLRSNVDFLLRLSGHPEFEAGNVHTDFIPQHHKDLLPSHSTIAKESVCQAALGLILKEKEMTSAFKLHTQDQFSPFSFSSGRRLNISYTRNMTLRSGKSDIVIAVTYNRDGSYDMQIDNKSFRVLGDLSSEDGCTYLKSSINGVARKSKFILLDNTVHLFSMEGSIEVGIPVPKYLSPVSAEGAQGGTIAPMTGTIEKVFVKAGDRVKAGDSLMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPLVEFEEEESDK liuD ignore reanno::SB2B:6937189 Methylcrotonoyl-CoA carboxylase (EC 6.4.1.4) MFNKLLIANRGEIACRVIRTARDMGIKTVAVYSDADRDARHVALADESFYLGESAPASSYLRGELIIDIAKKCGAEAIHPGYGFLSENAAFARACEASGIAFVGPGSDAIDAMGSKSAAKLIMEKAGVPLVPGYHGDDQSDATLLAEAKKIGYPLLIKAAYGGGGKGMRIVESESELKAAIDSARREAASSFGNDKLLMERYLRQPRHVEVQVFADSQGNCVYLSDRDCSIQRRHQKVVEEAPAPGLPDSLRKQMGEAAVAAAKAIDYRGAGTVEFLLDVDMSFFFMEMNTRLQVEHPVTEMVTGQDLVKWQLLVAAGAQLPLEQHEIQIHGHAFEVRIYAEDPNNEFLPASGKLTFLREPEPSRHVRIDSGVRENDVISNYYDPMIAKLIVWDESRPRALARLTRALGDYRVGGLKHNIEFLSNIAEHPAFAQANFSTDFIGRYGDALIGDSRDEADTAFVLAVLTQLRLREAVSQDVAGHDPFSPWSSLKGFRLSSPRRHSVTLLDDAHQSRSAELTESNGRYQLCLNDKLIELSGSIEDSELKCEINGHKMKVTVSLEDGGLTVFLSSGSYHFREVLGQVLEETASSEDKLKAPMNGTVVTHLVAAGDKVSAGQGLLVMEAMKMEYTIEAPFDGVVSEFFFAPGELVSDGTLLLALEMADAAADSKETEA liuD ignore reanno::Smeli:SM_b21124 Methylcrotonoyl-CoA carboxylase (EC 6.4.1.4) MFSKLLIANRGEIACRIIRTARRLGIRTVAVYSDADGDALHVALADEAIRIGGAPAAESYLASAPIVQAARSVGAQAIHPGYGFLSENADFAEAVAEAGMIFVGPPPAAIRAMGLKDAAKALMERSGVPVVPGYHGEEQDASFLADRAREIGYPVLIKARAGGGGKGMRRVERQEDFGPALEAARREAESAFGDGSVLLERYLTKPRHIEMQVFGDRHGNIVHLFERDCSLQRRHQKVIEEAPAPGMTAEVRRAMGDAAVRAAQAIGYVGAGTVEFIADVTNGLWPDHFYFMEMNTRLQVEHPVTEAITGIDLVEWQLRVASGEPLPKKQADISMNGWAFEARLYAEDPARGFLPATGRLTELSFPEGTSRVDSGVRQGDTITPYYDPLIAKLIVHGQNRSAALGRLQDALKECRIGGTVTNRDFLIRLTEEHDFRSGHPDTGLIDREIERLTAPVAPGDEALALAAIFSTGALDPNRSTDPWSSLGSWQIWGDAHRMVVIEHADVRATVTLASRGRDQFAVRAGASTLPVLVLDRFEGGARLEVAGQKRLIRFSRDREALTLFHGGRNLVFHVPDGLTGGQSSEIADDELVAPMPGLVKLVRVGAGDAVTKGQALVVMEAMKMELTLSASREGTIANVHVAEGAQVSEGTVLVTLMEEAAQ liuD ignore reanno::pseudo1_N1B4:Pf1N1B4_3984 Methylcrotonyl-CoA carboxylase biotin-containing subunit (EC 6.4.1.4) MSAPVLTTLLVANRGEIACRVMRTAKALGLTTVAVHSATDRDARHSREADIRVDLGGSKAADSYLQIDKLIAAAKASGAQAIHPGYGFLSENAGFARAIEAAGLIFLGPPASAIDAMGSKSAAKALMETAGVPLVPGYHGEAQDLETFRDACERIGYPVLLKATAGGGGKGMKVVEDVSQLAEALASAQREALSSFGDSRMLVEKYLLKPRHVEIQVFADQHGNCLYLNERDCSIQRRHQKVVEEAPAPGLSPELRRAMGEAAVRSAQAIGYVGAGTVEFLLDARGEFFFMEMNTRLQVEHPVTEAITGLDLVAWQIRVARGEALPMTQDQVPLIGHAIEVRLYAEDPGNDFLPATGRLALYRESAAGPGRRVDSGVEEGDEISPFYDPMLGKLIAWGEDREQARLRLLSMLDEFAIGGLKTNINFLRRIIGHPAFAAAELDTGFIPRYQEQLLPAPSDLSDEFWQAAAQAFAQSQSSTTRADDLSSPWGIGNGFRAGLPTEITLHLSCEEQDRALTLGDADAHTAQLKGEYLLTEHNGLRRQHRAIRRGDTLYLQWDGELRRIESYDPISAVEASHSHQGGLTAPMNGSIVRVLVEAGQTVEAGAQLVVLEAMKMEHSIRAPHAGIIKALYCQEGEMVSEGSALVELEHA liuD ignore reanno::pseudo5_N2C3_1:AO356_01595 Methylcrotonoyl-CoA carboxylase (EC 6.4.1.4) MSAPALTTLLVANRGEIACRVMRTARAMGLTTVAVHSATDRDARHSREADIRVDLGGSKAADSYLQIDKLIAAAKASGAQAIHPGYGFLSENAGFARAIENAGLIFLGPPASAIDAMGSKSAAKTLMETAGVPLVPGYHGEAQDLETFRDAAERIGYPVLLKATAGGGGKGMKVVEDVSQLAEALASAQREAQSSFGDSRMLVEKYLLKPRHVEIQVFADQHGNCLYLNERDCSIQRRHQKVVEEAPAPGLTPQLRRAMGEAAVRAAQAIGYVGAGTVEFLLDARGEFFFMEMNTRLQVEHPVTEAITGLDLVAWQIRVAQGEPLPITQAQVPLLGHAIEVRLYAEDPGNDFLPATGRLALYRESAEGPGRRVDSGVEEGDEISPFYDPMLGKLIAWGEDREQARLRLLSMLDEFVIGGLKTNIGFLRRIVAHPAFAAAELDTGFIPRYQAQLLPEPSELDDAFWFAAAQGVALSLAPHVRGDDAGSPWASTTGMRLGLPRETTLHLSCEGQDRALTLDVTAHCAELEGERLTIEHHGVRRSHRAIRQVDSLYLQWEGDLHRIDLYDPLAAAEASHSHQGGLVAPMNGSIVRVLVGVGQTVEAGAQLVVLEAMKMEHSIRAPKAGVIKALYCQEGEMVSEGSALVAFEE liuD ignore reanno::pseudo6_N2E2:Pf6N2E2_2194 Methylcrotonoyl-CoA carboxylase (EC 6.4.1.4) MSAPALTTLLVANRGEIACRVMRTAKAMGLTTVAVHSATDRDARHSREADIRVDLGGSKAADSYLQIDKLIAAAKASGAQAIHPGYGFLSENAGFARAIENAGLIFLGPPASAIDAMGSKSAAKALMETAGVPLVPGYHGEAQDLETFRDAAERIGYPVLLKATAGGGGKGMKVVEDVSQLAEALASAQREAQSSFGDSRMLVEKYLLKPRHVEIQVFADQHGNCLYLNERDCSIQRRHQKVVEEAPAPGLTAQLRQAMGEAAVRAAQAIGYVGAGTVEFLLDARGEFFFMEMNTRLQVEHPVTEAITGLDLVAWQIRVAQGEPLPITQAQVPLLGHAIEVRLYAEDPVNDFLPATGRLALYRESAKGPGRRVDSGVEEGDEISPFYDPMLGKLIAWGENREQARLRLLSMLDEFAIGGLKTNIGFLRRIVAHPAFAAAELDTGFIPRYQAQLLPEPGELDDAFWLAAAQGFALSLAPHIRGDDAGSPWASTTGMRLGLSRETTLHLSCEGQDRALTLDVTAHCAELKGERLTIEHHGVRRSHRAIRQGDSLYLHWAGDLHRIDLYDPLAAAEASHSHQGGLAAPMNGSIVRVLVSVGQPVDAGAQLVVLEAMKMEHSIRAPKAGVIKALYCQEGEMVSEGSALVAFEE liuE curated BRENDA::P35914,SwissProt::P35914,metacyc::HS04116-MONOMER hydroxymethylglutaryl-CoA lyase (EC 4.1.3.4);; Hydroxymethylglutaryl-CoA lyase, mitochondrial; HL; HMG-CoA lyase; 3-hydroxy-3-methylglutarate-CoA lyase; EC 4.1.3.4;; Hydroxymethylglutaryl-CoA lyase, mitochondrial (EC 4.1.3.4) MAAMRKALPRRLVGLASLRAVSTSSMGTLPKRVKIVEVGPRDGLQNEKNIVSTPVKIKLIDMLSEAGLSVIETTSFVSPKWVPQMGDHTEVLKGIQKFPGINYPVLTPNLKGFEAAVAAGAKEVVIFGAASELFTKKNINCSIEESFQRFDAILKAAQSANISVRGYVSCALGCPYEGKISPAKVAEVTKKFYSMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPLAALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLGGCPYAQGASGNLATEDLVYMLEGLGIHTGVNLQKLLEAGNFICQALNRKTSSKVAQATCKL liuE curated BRENDA::P97519,SwissProt::P97519 hydroxymethylglutaryl-CoA lyase (EC 4.1.3.4);; Hydroxymethylglutaryl-CoA lyase, mitochondrial; HL; HMG-CoA lyase; 3-hydroxy-3-methylglutarate-CoA lyase; EC 4.1.3.4 MATVRKAFPQRLVGLASLRAASTSSMGTLPKRVKIVEVGPRDGLQNEKSIVPTPVKIKLIDMLSEAGLPVIEATSFVSPKWVPQMADHSDVLKGIQKFPGINYPVLTPNMKGFEEAVAAGAKEVSIFGAASELFTRKNVNCSIEESFQRFDGVMQAARAASISVRGYVSCALGCPYEGKVSPAKVAEVAKKLYSMGCYEISLGDTIGVGTPGLMKDMLTAVLHEVPVAALAVHCHDTYGQALANTLVALQMGVSVVDSSVAGLGGCPYAKGASGNLATEDLVYMLTGLGIHTGVNLQKLLEAGDFICQALNRKTSSKVAQATCKL liuE curated BRENDA::Q9I2A0,SwissProt::Q9I2A0,metacyc::MONOMER-16069 3-Hydroxy-3-isohexenylglutaryl-CoA lyase (EC 4.1.3.26);; 3-hydroxy-3-isohexenylglutaryl-CoA/hydroxy-methylglutaryl-CoA lyase; HIHG-CoA lyase; HMG-CoA lyase; (S)-3-hydroxy-3-methylglutaryl-CoA acetoacetate-lyase; 3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA acetate-lyase; EC 4.1.3.26; EC 4.1.3.4;; hydroxymethylglutaryl-CoA lyase subunit (EC 4.1.3.26; EC 4.1.3.4) MNLPKKVRLVEVGPRDGLQNEKQPIEVADKIRLVDDLSAAGLDYIEVGSFVSPKWVPQMAGSAEVFAGIRQRPGVTYAALAPNLKGFEAALESGVKEVAVFAAASEAFSQRNINCSIKDSLERFVPVLEAARQHQVRVRGYISCVLGCPYDGDVDPRQVAWVARELQQMGCYEVSLGDTIGVGTAGATRRLIEAVASEVPRERLAGHFHDTYGQALANIYASLLEGIAVFDSSVAGLGGCPYAKGATGNVASEDVLYLLNGLEIHTGVDMHALVDAGQRICAVLGKSNGSRAAKALLAKA liuE curated CharProtDB::CH_018268,metacyc::MONOMER-11828 hydroxymethylglutaryl-CoA lyase; EC 4.1.3.4;; hydroxymethylglutaryl-CoA lyase monomer (EC 4.1.3.4) MQAVKVFEVGPRDGLQNERQPLSVAARVGLIGELAGTGLRHIEAGAFVSPRWVPQMAGSDEVLRQLPSNDGVSYTALVPNRQGFEAAQRAGCREVAVFAAASEAFSRNNINCSIDESFERFTPVLRAANEASIRVRGYVSCVLGCPFSGAVAPEAVAKVARRLYELGCYEISLGDTIGAGRPDETAQLFELCARQLPVAALAGHFHDTWGMAIANVHAALAQGVRTFDSSVAGLGGCPYSPGASGNVATEDLLYLLHGLGYSTGVDLEAVAQVGVRISAQLGTANRSRAGLALAARSAREH liuE curated CharProtDB::CH_122457 3-hydroxy-3-methylglutaryl-coenzyme A lyase/3-methylglutaconyl-coenzyme A hydratase; EC 4.1.3.4; EC 4.2.1.18 MQNSTKTVRIVEVGPRDGLQNIPQSIDSTIKLDLIRRLRDAGLQTIELTSFVSPRAIPQLADAQVVVQNADIQKLLKNPKLRLPVLVPNLKGLERALHNGIKEVAVFISATEGFSRANINCTVDEGLERARQVASRAASAGLSVRGYVSCIFADPYDGPTRPSSVLRCTKALLDAGCYEVSLGDTLGIGTPADVRWLITYLQDNGVPLEMLAGHFHDTYGGAVANVWEAYKCGLRMFDSSVAGLGGCPXALGAKGNVASEDLVYMFERSGIHTGVDLSKLVETGEWISRQLSIAISSRAGAALWAMRKQTAVPKSPKVSVSWKLVKQTEGLQLFRSGVNLRINLNRPKNGNALTAIMAQDLTEAVTNAGRDATISRIILTGSGKFFCTGMDLGKGSTAVGQGGSSSNAQFDRLTNLFEAIDQSPKVTIACLNGPAFGGGVGLAFACDMRFAVRAASVTLSEVKLGLCPATISKYVIREFGIALSREAMLSARPVSAGELKARGLVVELADNAEALPGLLDQFLTQLKAASPEASRMSKELIRLAWAHGGKEEQAKGIRALFDGMMRPDGDGAHGVKEFQAKRSVDWDAYTLRRVDSAKV liuE curated SwissProt::D4A5C3 3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic; 3-hydroxy-3-methylglutaryl-CoA lyase-like protein 1; EC 4.1.3.4 MGNLPSAAKHCLNYQQLLREHLWSGESVAGALDPAQEASQLSGLPEYVKIVEVGPRDGLQNEKVIVPTDIKIEFINQLSQTGLSVIEVTSFVSSRWVPQMADHAEVMGGIHQYPGVRYPVLVPNLQGLQHAVAAGATEIAVFGAASESFSKKNINCSIEESMGRFEQVISSARHMNIPVRGYVSCALGCPYEGSIMPQKVTEVSKRLYSMGCYEISLGDTVGVGTPGSMKTMLESVMKEIPPGALAVHCHDTYGQALANILTALQMGINVVDSAVSGLGGCPYAKGASGNVATEDLIYMLNGMGLNTGVDLHKVMEAGDFICKAVNKTTNSKVAQASFKARLE liuE curated SwissProt::O34873 Hydroxymethylglutaryl-CoA lyase YngG; HL; HMG-CoA lyase; 3-hydroxy-3-methylglutarate-CoA lyase; EC 4.1.3.4 MPYPKKVTIKEVGPRDGLQNEPVWIATEDKITWINQLSRTGLSYIEITSFVHPKWIPALRDAIDVAKGIDREKGVTYAALVPNQRGLENALEGGINEACVFMSASETHNRKNINKSTSESLHILKQVNNDAQKANLTTRAYLSTVFGCPYEKDVPIEQVIRLSEALFEFGISELSLGDTIGAANPAQVETVLEALLARFPANQIALHFHDTRGTALANMVTALQMGITVFDGSAGGLGGCPYAPGSSGNAATEDIVYMLEQMDIKTNVKLEKLLSAAKWIEEKMGKPLPSRNLQVFKSS liuE curated SwissProt::O81027 Hydroxymethylglutaryl-CoA lyase, mitochondrial; HL; HMG-CoA lyase; 3-hydroxy-3-methylglutarate-CoA lyase; EC 4.1.3.4 MQWNGVRRAHSIWCKRLTNNTHLHHPSIPVSHFFTMSSLEEPLSFDKLPSMSTMDRIQRFSSGACRPRDDVGMGHRWIEGRDCTTSNSCIDDDKSFAKESFPWRRHTRKLSEGEHMFRNISFAGRTSTVSGTLRESKSFKEQKYSTFSNENGTSHISNKISKGIPKFVKIVEVGPRDGLQNEKNIVPTSVKVELIQRLVSSGLPVVEATSFVSPKWVPQLADAKDVMDAVNTLDGARLPVLTPNLKGFQAAVSAGAKEVAIFASASESFSLSNINCTIEESLLRYRVVATAAKEHSVPVRGYVSCVVGCPVEGPVLPSKVAYVVKELYDMGCFEISLGDTIGIGTPGSVVPMLEAVMAVVPADKLAVHFHDTYGQALANILVSLQMGISIVDSSIAGLGGCPYAKGASGNVATEDVVYMLNGLGVHTNVDLGKLIAAGDFISKHLGRPNGSKAAVALNRRITADASKI liuE curated SwissProt::P38060 Hydroxymethylglutaryl-CoA lyase, mitochondrial; HL; HMG-CoA lyase; 3-hydroxy-3-methylglutarate-CoA lyase; EC 4.1.3.4 MASVRKAFPRRLVGLTSLRAVSTSSMGTLPKQVKIVEVGPRDGLQNEKSIVPTPVKIRLIDMLSEAGLPVIEATSFVSPKWVPQMADHSDVLKGIQKFPGINYPVLTPNMKGFEEAVAAGAKEVSVFGAVSELFTRKNANCSIEESFQRFAGVMQAAQAASISVRGYVSCALGCPYEGKVSPAKVAEVAKKLYSMGCYEISLGDTIGVGTPGLMKDMLTAVMHEVPVTALAVHCHDTYGQALANTLVALQMGVSVVDSSVAGLGGCPYAKGASGNLATEDLVYMLNGLGIHTGVNLQKLLEAGDFICQALNRKTSSKVAQATCKL liuE curated SwissProt::Q8TB92 3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic; 3-hydroxy-3-methylglutaryl-CoA lyase-like protein 1; Endoplasmic reticulum 3-hydroxy-3-methylglutaryl-CoA lyase; er-cHL; EC 4.1.3.4 MGNVPSAVKHCLSYQQLLREHLWIGDSVAGALDPAQTSLLTNLHCFQPDVSGFSVSLAGTVACIHWETSQLSGLPEFVKIVEVGPRDGLQNEKVIVPTDIKIEFINRLSQTGLSVIEVTSFVSSRWVPQMADHTEVMKGIHQYPGVRYPVLTPNLQGFHHAVAAGATEISVFGAASESFSKKNINCSIEESMGKFEEVVKSARHMNIPARGYVSCALGCPYEGSITPQKVTEVSKRLYGMGCYEISLGDTIGVGTPGSMKRMLESVMKEIPPGALAVHCHDTYGQALANILTALQMGINVVDSAVSGLGGCPYAKGASGNVATEDLIYMLNGLGLNTGVNLYKVMEAGDFICKAVNKTTNSKVAQASFNA liuE curated reanno::Pedo557:CA265_RS13115 Hydroxymethylglutaryl-CoA lyase (EC 4.1.3.4) MSQNNFKLVECPRDAMQGLHDFVPTKLKAEYLNLLLQVGFDTLDFGSFVSPKAIPQMADTAEVLAQLDLSNTSTKLLAIVANLRGVEDAVKHQAVNYLGFPFSISETFQQRNTNSSIAQSLNTVEEMLSLCAKNNKKAVVYLSMGFGNPYGDKWNYEIVEKWADVLVSRGVEILSLADTVGISTPEKIENILPKLISRFSNTEIGIHLHSTPAERFEKIEAAYHSGVKRIDSALKGFGGCPMAADDLTGNIATEDVITFLNMKGEKLNLNMDKWNEAMVLSGKIFG liuE curated reanno::Smeli:SM_b21125 Hydroxymethylglutaryl-CoA lyase (EC 4.1.3.4) MTSPAKERVTIVEVAPRDGLQNESRLVATEDKIRLVDLLADCGYERIEVTSFVSPRWVPQLADAPAVMAGIVRRPGTRYAALTPNMRGFEAALAAGADEVAIFASASESFSERNINCSIAESIERFRPVAEASRHRGVPLRGYVSCVVECPYEGAIVPAETARVARLLADLGCYEISLGDTIGRGTPEAVDAMLAAALREIDAPKLAGHFHDTSGRALENIAVALERGIRVFDASAGGLGGCPYAPGAAGNVDTLAVNAFLEAQSFATGLDSEKLDRAAAFARSLRSTA liuE curated2 O34873 Hydroxymethylglutaryl-CoA lyase YngG; HL; HMG-CoA lyase; EC 4.1.3.4; 3-hydroxy-3-methylglutarate-CoA lyase MPYPKKVTIKEVGPRDGLQNEPVWIATEDKITWINQLSRTGLSYIEITSFVHPKWIPALRDAIDVAKGIDREKGVTYAALVPNQRGLENALEGGINEACVFMSASETHNRKNINKSTSESLHILKQVNNDAQKANLTTRAYLSTVFGCPYEKDVPIEQVIRLSEALFEFGISELSLGDTIGAANPAQVETVLEALLARFPANQIALHFHDTRGTALANMVTALQMGITVFDGSAGGLGGCPYAPGSSGNAATEDIVYMLEQMDIKTNVKLEKLLSAAKWIEEKMGKPLPSRNLQVFKSS liuE curated2 P13703 Hydroxymethylglutaryl-CoA lyase; HL; HMG-CoA lyase; EC 4.1.3.4; 3-hydroxy-3-methylglutarate-CoA lyase MQAVKVFEVGPRDGLQNERQPLSVAARVGLIGELAGTGLRHIEAGAFVSPRWVPQMAGSDEVLRQLPSNDGVSYTALVPNRQGFEAAQRAGCREVAVFAAASEAFSRNNINCSIDESFERFTPVLRAANEASIRVRGYVSCVLGCPFSGAVAPEAVAKVARRLYELGCYEISLGDTIGAGRPDETAQLFELCARQLPVAALAGHFHDTWGMAIANVHAALAQGVRTFDSSVAGLGGCPYSPGASGNVATEDLLYLLHGLGYSTGVDLEAVAQVGVRISAQLGTANRSRAGLALAARSAREH liuE curated2 Q9I2A0 3-hydroxy-3-isohexenylglutaryl-CoA/hydroxy-methylglutaryl-CoA lyase; HIHG-CoA lyase; HMG-CoA lyase; EC 4.1.3.26; EC 4.1.3.4; (S)-3-hydroxy-3-methylglutaryl-CoA acetoacetate-lyase; 3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA acetate-lyase MNLPKKVRLVEVGPRDGLQNEKQPIEVADKIRLVDDLSAAGLDYIEVGSFVSPKWVPQMAGSAEVFAGIRQRPGVTYAALAPNLKGFEAALESGVKEVAVFAAASEAFSQRNINCSIKDSLERFVPVLEAARQHQVRVRGYISCVLGCPYDGDVDPRQVAWVARELQQMGCYEVSLGDTIGVGTAGATRRLIEAVASEVPRERLAGHFHDTYGQALANIYASLLEGIAVFDSSVAGLGGCPYAKGATGNVASEDVLYLLNGLEIHTGVDMHALVDAGQRICAVLGKSNGSRAAKALLAKA livF uniprot A0A165KC78 SubName: Full=ABC transporter ATP-binding protein {ECO:0000313|EMBL:KZT15317.1}; MAEKSNKVLLQVKGLKVAYGGIQAVKGVDFEVREGELVSLIGSNGAGKTTTMKAITGTLSMNDGNIEYLGKSIKGKGAWDLVKEGLVMVPEGRGVFARMTITENLQMGAYIRKDKAGILADIEKMFTIFPRLRERKDQLAGTMSGGEQQMLAMGRALMSQPKVLLLDEPSMGLSPIMVDKIFEVVRDVYALGVTIVLVEQNASRALAIADRGYVMESGLITMTGPGQQLLNDPKVRAAYLGE livF uniprot Q1MCU3 SubName: Full=ATP-binding component of a broad range amino acid ABC transporter {ECO:0000313|EMBL:CAK09237.1}; MGDEVMTGQPLLQVNGVETYYGNIRALAGVDVHVNKGEIVSLIGANGAGKSTLMMTICGSPQARTGSVVFEGRDITRMPTHEIARLRIAQSPEGRRIFPRMTVLENLQMGAGLDNLKHFAEDVEKIFTLFPRLKERHAQRGGTLSGGEQQMLSIGRALMARPKLLLLDEPSLGLAPLIVKGIFEAIRKLNEAEGLTVFLVEQNAFAALRLSHRAYVMVNGKVTMSGSGKELLANPEVRAAYLEGGRH livF curated CharProtDB::CH_003736,TCDB::P22731,ecocyc::LIVF-MONOMER,metacyc::LIVF-MONOMER high-affinity branched-chain amino acid ABC transporter, ATP-binding protein LivF;; LivF aka B3454, component of Leucine; leucine/isoleucine/valine porter;; branched chain amino acid/phenylalanine ABC transporter ATP binding subunit LivF (EC 7.4.2.2);; branched chain amino acid/phenylalanine ABC transporter ATP binding subunit LivF (EC 7.4.2.2) MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDDKDITDWQTAKIMREAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSNPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLSDTGDALLANEAVRSAYLGG livF curated TCDB::P21630 High-affinity branched-chain amino acid transport ATP-binding protein BraG, component of Branched chain amino acid uptake transporter. Transports alanine MLSFDKVSTYYGKIQALHDVSVEVKKGEIVTLIGANGAGKSTLLMTLCGSPQAASGSIRYEGEELVGLPSSTIMRKSIAVVPEGRRVFSRLTVEENLAMGGFFTDKDDYQVQMDKVLELFPRLKERYEQRAGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAPIIIQQIFEIIEQLRREGVTVFLVEQNANQALKLADRAYVLENGRIVMHDTGAALLTNPKVRDAYLGG livF curated TCDB::Q8DQH7 ABC transporter ATP-binding protein-branched chain amino acid transport, component of The branched chain hydrophobic amino acid transporter, LivJFGHM MSVLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGLSQVPEGRHVFPGLTVMENLEMGAFLKKNREENQANLKKVFSRFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSEEVRKAYLGG livG uniprot A0A165KC86 SubName: Full=ABC transporter ATP-binding protein {ECO:0000313|EMBL:KZT15318.1}; MTEKSNEVVLKVAGISKRFGGLQALSDVGITIKRGQVYGLIGPNGAGKTTFFNVITGLYTPDAGTFELAGKPYEPTAVHEVAKAGIARTFQNIRLFAEMTALENVMVGRHIRTGSGLFGAVFRTKGFKAEEAAIAKRAQELLDYVGIGKFADYKARTLSYGDQRRLEIARALATDPQLIALDEPAAGMNATEKVQLRELIDRIRNDNRTILLIEHDVKLVMGLCDRVTVLDYGKQIAEGNPAEVQKNEKVIEAYLGTGGH livG uniprot Q1MCU2 SubName: Full=ATP-binding component of a broad range amino acid ABC transporter {ECO:0000313|EMBL:CAK09238.1}; MMSPVTNTMSDDTLLKVEHLSMKFGGLMAINDFSFEAKRGDITALIGPNGAGKTTVFNCITGFYKPTMGMITFNQKSGKQYLLERLPDFRITKEARVARTFQNIRLFSGLTVLENLLVAQHNKLMKASGYTILGLIGVGPYKREAAEAIELARFWLEKADLIDRADDPAGDLPYGAQRRLEIARAMCTGPELLCLDEPAAGLNPRESATLNALLKSIRAETGTSILLIEHDMSVVMEISDHVVVLEYGQKISDGTPDHVKNDPRVIAAYLGVEDEEVEEVIAAVEQLEGGAN livG curated TCDB::P0A9S7,ecocyc::LIVG-MONOMER,metacyc::LIVG-MONOMER High-affinity branched-chain amino acid transport ATP-binding protein LivG aka B3455, component of Leucine; leucine/isoleucine/valine porter;; branched chain amino acid/phenylalanine ABC transporter ATP binding subunit LivG (EC 7.4.2.2);; branched chain amino acid/phenylalanine ABC transporter ATP binding subunit LivG (EC 7.4.2.2) MSQPLLSVNGLMMRFGGLLAVNNVNLELYPQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRDQHLEGLPGQQIARMGVVRTFQHVRLFREMTVIENLLVAQHQQLKTGLFSGLLKTPSFRRAQSEALDRAATWLERIGLLEHANRQASNLAYGDQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNHHNTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEQIRNNPDVIRAYLGEA livG curated TCDB::P21629 High-affinity branched-chain amino acid transport ATP-binding protein BraF, component of Branched chain amino acid uptake transporter. Transports alanine MSRPILEVSGLTMRFGGLLAVNGVNLKVEEKQVVSMIGPNGAGKTTVFNCLTGFYQPTGGLIRLDGEEIQGLPGHKIARKGVVRTFQNVRLFKEMTAVENLLVAQHRHLNTNFLAGLFKTPAFRRSEREAMEYAAHWLEEVNLTEFANRSAGTLAYGQQRRLEIARCMMTRPRILMLDEPAAGLNPKETDDLKALIAKLRSEHNVTVLLIEHDMKLVMSISDHIVVINQGAPLADGTPEQIRDNPDVIKAYLGEA livG curated TCDB::Q8DQH8 ABC transporter ATP-binding protein-branched chain amino acid transport, component of The branched chain hydrophobic amino acid transporter, LivJFGHM MALLEVKQLTKHFGGLTAVGDVTLELNEGELVGLIGPNGAGKTTLFNLLTGVYEPSEGTVTLDGHLLNGKSPYKIASLGLGRTFQNIRLFKDLTVLDNVLIAFGNHHKQHVFTSFLRLPAFYKSEKELKAKALELLKIFDLDGDAETLAKNLSYGQQRRLEIVRALATEPKILFLDEPAAGMNPQETAELTELIRRIKDEFKITIMLIEHDMNLVMEVTERIYVLEYGRLIAQGTPDEIKTNKRVIEAYLGGEA livH uniprot A0A165KC95 SubName: Full=ABC transporter permease {ECO:0000313|EMBL:KZT15319.1}; MDILLQQIINGLVLGSMYALIALGYTMVYGIIQLINFAHGEVLMIGALTSWSCIGMMQGAMPGAPGWVILLLATIIACVVAATLNFVIEKVAYRPLRSSPRLAPLITAIGMSILLQTLAMIIWKPNYKPYPTMLPSSPFEIGGAFITPTQILILGVTAVALASLVYLVNHTNLGRAMRATAENPRVASLMGVKPDMVISATFIIGAVLAAIAGIMYASNYGTAQHTMGFLPGLKAFTAAVFGGIGNLAGAVVGGILLGLIEAIGSGYIGTLTGGLLGSHYTDIFAFIVLIIILTLRPSGLLGERVADRA livH uniprot Q1MCU0 SubName: Full=Transmembrane component of a broad range amino acid ABC transporter {ECO:0000313|EMBL:CAK09240.1}; MEYFVQQLLNGLTLGSIYGLVAIGYTMVYGIIGMINFAHGDIFMLGGFAALIVFLVLTSIFAGLPVAVLLLVMLVVAMLMTSLWNWTIERVAYRPLRGSFRLAPLITAIGMSITLSNFIQVTQGPRNKPIPPMVSSVYQFGNISVSLKQIIIIVITAVLLTIFWYIVNRTALGRAQRATEQDRKMAALLGVNVDQTISITFVMGAALAAVAGTMYLMYYGVASFNDGFTPGVKAFTAAVLGGIGSLPGAVFGGLLIGLIESLWSAYFTIAYKDVATFAILAFVLIFKPTGILGRPEVEKV livH curated TCDB::P21627 High-affinity branched-chain amino acid transport system permease protein BraD, component of Branched chain amino acid uptake transporter. Transports alanine MPEIYHYLQQLVNGLTVGSTYALIAIGYTMVYGIIGMINFAHGEVYMIGSYIAFIAITLLAMMGLDSVPLMMLAAFAASIIVTSAFGYSIERVAYRPLRGGNRLIPLISAIGMSIFLQNAVMLSQDSKEKAIPTLLPGNFVFGESSMNGVVISYMQILIFVVTFLVMFGLTLFISRSRLGRACRACAEDLKMTNLLGINSNNIIALTFVIGAALAAVAAVLLGMQYGVINPGIGFLAGIKAFTAAVLGGIGSIPGAMLGGLLLGVAEAFGADVFGDQYKDVVAFGLLILVLLFRPTGILGRPEVEKV livH curated TCDB::Q8DQI0 ABC transporter membrane-spanning permease-branched chain amino acid transport, component of The branched chain hydrophobic amino acid transporter, LivJFGHM MNLMLQQLVNGLILGSVYALLALGYTMVYGIIKLINFAHGDIYMMGAFIGYFLINSFQMNFFVALIVAMLATAILGVVIEFLAYRPLRHSTRIAVLITAIGVSFLLEYGMVYLVGANTRAFPQAIQTVRYDLGPISLTNVQLMILGISLILMILLQVIVQKTKMGKAMRAVSVDSDAAQLMGINVNRTISFTFALGSALAGAAGVLIALYYNSLEPLMGVTPGLKSFVAAVLGGIGIIPGAALGGFVIGLLETFATAFGMSDFRDAIVYGILLLILIVRPAGILGKNVKEKV livH curated ecocyc::LIVH-MONOMER,CharProtDB::CH_088640,TCDB::P0AEX7,metacyc::LIVH-MONOMER branched chain amino acid/phenylalanine ABC transporter membrane subunit LivH (EC 7.4.2.2);; high-affinity branched-chain amino acid ABC transporter, permease protein LivH;; High-affinity branched-chain amino acid transport system permease protein LivH aka B3457, component of Leucine; leucine/isoleucine/valine porter;; branched chain amino acid/phenylalanine ABC transporter membrane subunit LivH (EC 7.4.2.2) MSEQFLYFLQQMFNGVTLGSTYALIAIGYTMVYGIIGMINFAHGEVYMIGSYVSFMIIAALMMMGIDTGWLLVAAGFVGAIVIASAYGWSIERVAYRPVRNSKRLIALISAIGMSIFLQNYVSLTEGSRDVALPSLFNGQWVVGHSENFSASITTMQAVIWIVTFLAMLALTIFIRYSRMGRACRACAEDLKMASLLGINTDRVIALTFVIGAAMAAVAGVLLGQFYGVINPYIGFMAGMKAFTAAVLGGIGSIPGAMIGGLILGIAEALSSAYLSTEYKDVVSFALLILVLLVMPTGILGRPEVEKV livJ uniprot A0A165KTD4 SubName: Full=Branched chain amino acid ABC transporter substrate-binding protein {ECO:0000313|EMBL:KZT16064.1}; MQLKLKLTVVAAIAAAAGVASAQEQVVKIGHVAPVSGAQAHYGKDNENGARMAIEELNAQGVTIGGKKIKFELVAEDDAADPKQGTAAAQKLCDAKVAGVVGHLNSGTTIPASKVYNDCGIPHVTGAATNPNLTKPGYKTTFRIIANDNALGAGLAFYAVDTLKLKTVAIIDDRTAYGQGVADVFKKTATAKGMKVVDEQFTTDKATDFMAILTAIKAKNPDAIFYGGMDPQGGPMLRQMEQLGMGNVKYFGGDGICTSEIAKLAAGAKTLGNVICAEGGSSLAKMPGGTAWKAKYDAKYPNQFQVYSPYTYDATFLIVDAMKRANSVDPKVYTPELAKSSFKGVTSTIAFEPNGEMKNPAITLYVYKDGKKTPL livJ uniprot Q1MDE9 SubName: Full=Solute-binding (Aliphatic amino acid) component of ABC transporter {ECO:0000313|EMBL:CAK09028.1}; MTLKTLTATLVASLAFAPLAHADITIGLIAPLTGPVAAYGDQVKNGAQTAVDEINKKGGILGEKVVLELADDAGEPKQGVSAANKVVGDGIRFVVGPVTSGVAIPVSDVLAENGVLMVTPTATAPDLTKRGLTNVLRTCGRDDQQAEVAAKYVLKNFKDKRVAIVNDKGAYGKGLADAFKATLNAGGITEVVNDAITPGDKDFSALTTRIKSEKVDVVYFGGYHPEGGLLARQLHDLAANATIIGGDGLSNTEFWAIGTDAAGGTIFTNASDATKSPDSKAAADALAAKNIPAEAFTLNAYAAVEVLKAGIEKAGSAEDAEAVATALKDGKEIPTAIGKVTYGETGDLTSQSFSLYKWEAGKIVAAE livJ curated CharProtDB::CH_107418,TCDB::P04816,ecocyc::LIVK-MONOMER,metacyc::LIVK-MONOMER leucine-specific-binding protein LivK;; Livk aka B3458, component of Leucine; leucine/isoleucine/valine porter;; L-leucine/L-phenylalanine ABC transporter periplasmic binding protein (EC 7.4.2.2);; L-leucine/L-phenylalanine ABC transporter periplasmic binding protein (EC 7.4.2.2) MKRNAKTIIAGMIALAISHTAMADDIKVAVVGAMSGPIAQWGDMEFNGARQAIKDINAKGGIKGDKLVGVEYDDACDPKQAVAVANKIVNDGIKYVIGHLCSSSTQPASDIYEDEGILMISPGATNPELTQRGYQHIMRTAGLDSSQGPTAAKYILETVKPQRIAIIHDKQQYGEGLARSVQDGLKAANANVVFFDGITAGEKDFSALIARLKKENIDFVYYGGYYPEMGQMLRQARSVGLKTQFMGPEGVGNASLSNIAGDAAEGMLVTMPKRYDQDPANQGIVDALKADKKDPSGPYVWITYAAVQSLATALERTGSDEPLALVKDLKANGANTVIGPLNWDEKGDLKGFDFGVFQWHADGSSTAAK livJ curated SwissProt::P21175,TCDB::P21175 Leucine-, isoleucine-, valine-, threonine-, and alanine-binding protein; LIVAT-BP; Leu/Ile/Val/Thr/Ala-binding protein;; Leucine-, isoleucine-, valine-, threonine-, and alanine-binding protein, component of Branched chain amino acid uptake transporter. Transports alanine MKKGTQRLSRLFAAMAIAGFASYSMAADTIKIALAGPVTGPVAQYGDMQRAGALMAIEQINKAGGVNGAQLEGVIYDDACDPKQAVAVANKVVNDGVKFVVGHVCSSSTQPATDIYEDEGVLMITPSATAPEITSRGYKLIFRTIGLDNMQGPVAGKFIAERYKDKTIAVLHDKQQYGEGIATEVKKTVEDAGIKVAVFEGLNAGDKDFNALISKLKKAGVQFVYFGGYHPEMGLLLRQAKQAGLDARFMGPEGVGNSEITAIAGDASEGMLATLPRAFEQDPKNKALIDAFKAKNQDPSGIFVLPAYSAVTVIAKGIEKAGEADPEKVAEALRANTFETPTGNLGFDEKGDLKNFDFTVYEWHKDATRTEVK livJ curated TCDB::P0AD96,ecocyc::LIVJ-MONOMER,metacyc::LIVJ-MONOMER Leu/Ile/Val-binding protein LivJ aka B3460 aka LIV-BP, component of Leucine; leucine/isoleucine/valine porter;; branched chain amino acid/phenylalanine ABC transporter periplasmic binding protein (EC 7.4.2.2);; branched chain amino acid/phenylalanine ABC transporter periplasmic binding protein (EC 7.4.2.2) MNIKGKALLAGCIALAFSNMALAEDIKVAVVGAMSGPVAQYGDQEFTGAEQAVADINAKGGIKGNKLQIVKYDDACDPKQAVAVANKVVNDGIKYVIGHLCSSSTQPASDIYEDEGILMITPAATAPELTARGYQLILRTTGLDSDQGPTAAKYILEKVKPQRIAIVHDKQQYGEGLARAVQDGLKKGNANVVFFDGITAGEKDFSTLVARLKKENIDFVYYGGYHPEMGQILRQARAAGLKTQFMGPEGVANVSLSNIAGESAEGLLVTKPKNYDQVPANKPIVDAIKAKKQDPSGAFVWTTYAALQSLQAGLNQSDDPAEIAKYLKANSVDTVMGPLTWDEKGDLKGFEFGVFDWHANGTATDAK livJ curated TCDB::Q8DQI1 ABC transporter substrate-binding protein-branched chain amino acid transport, component of The branched chain hydrophobic amino acid transporter, LivJFGHM MKKKFALSFVALASVALLAACGEVKSGAVNTAGNSVEEKTIKIGFNFEESGSLAAYGTAEQKGAQLAVDEINAAGGIDGKQIEVVDKDNKSETAEAASVTTNLVTQSKVSAVVGPATSGATAAAVANATKAGVPLISPSATQDGLTKGQDYLFIGTFQDSFQGKIISNYVSEKLNAKKVVLYTDNASDYAKGIAKSFRESYKGEIVADETFVAGDTDFQAALTKMKGKDFDAIVVPGYYNEAGKIVNQARGMGIDKPIVGGDGFNGEEFVQQATAEKASNIYFISGFSTTVEVSAKAKAFLDAYRAKYNEEPSTFAALAYDSVHLVANAAKGAKNSGEIKNNLAKTKDFEGVTGQTSFDADHNTVKTAYMMTMNNGKVEAAEVVKP livJ curated TCDB::Q9L3M3 BraC, component of General L- (and D-)amino acid uptake porter (transports acidic, basic, polar, semipolar and hydrophobic amino acids). The amino and carboxyl groups do not need to be α since γ-aminobutyric acid (GABA) is a substrate. The system may function with additional binding proteins since L-alanine uptake is not dependent on BraC MKKSLLSAVALTAMLAFSGNAWADVLIAVAGPLTGPNAAFGAQLQKGAEQAAADINAAGGINGEQIKIELGDDVSDPKQGISVANKFAADGVKFVIGHFNSGVSIPASEVYAENGILRNHPGRDEPDLHGTGLWNTFRTCGRDDQQGAIAGKYLADHFKDAKIAVVHDKTPYGQGLADETKKAMNAAGVTEVIYEGINVGDKDFSALIAKMKEAGVSIIYWGGLHTEAGLIIRQAADQGLKATLVSGDGIVSNELASIAGDAVAGTLNTFGPDPTANPANKELVEKFKAAGFNPEAYTLYSYAAMQTIAGAAKAAGSLDPEAVAKAMKEKGPFPTVLGDISFDEKGDPKIPGYIMYEWKKVRTASTATSRRHVSFAPLYGT livM uniprot A0A165KER0 SubName: Full=ABC transporter ATP-binding protein {ECO:0000313|EMBL:KZT15410.1}; MKNTKTNWIIGAVALLVLPLILQSFGNAWVRIADLALLYVLLALGLNIVVGYAGLLDLGYVAFYAVGAYLFALMASPHLADNFAAFAAMFPNGLHTSLWIVIPVAALLAAFFGAMLGAPTLKLRGDYLAIVTLGFGEIIRIFLNNLDHPVNLTNGPKGLGQIDSVKVFGLDLGKRLEVFGFDINSVTLYYYLFLVLVVVSVIICYRLQDSRIGRAWMAIREDEIAAKAMGINTRNMKLLAFGMGASFGGVSGAMFGAFQGFVSPESFSLMESVMIVAMVVLGGIGHIPGVILGAVLLSALPEVLRYVAGPLQAMTDGRLDSAILRQLLIALAMIIIMLLRPRGLWPSPEHGKSLTQKT livM uniprot Q1MCU1 SubName: Full=Transmembrane component of a broad range amino acid ABC transporter {ECO:0000313|EMBL:CAK09239.1}; MANIENSAGKPDAGLVRKGLTEALFAAVLSFGMFVLYVGLKTDQNISNELIIVQRWGLLAIFVAVAAIGRFAMVVFIRPNIDRRKLSKAREGELDISTEKSFFHRHFLKIALIALLLYPMVVVAIKGPQGSLTYVDNFGIQILIYVMLAWGLNIVVGLAGLLDLGYVAFYAVGAYSYALLSSYFGLSFWVLLPLSGIFAALWGVILGFPVLRLRGDYLAIVTLAFGEIIRLVLINWTDVTKGTFGISSIPKATLFGIPFDATAGGFAKLFHLPISSAYYKIFLFYLILALCMLTAYVTIRLRRMPIGRAWEALREDEIACRSLGINTVTTKLTAFATGAMFAGFAGSFFAARQGFVSPESFVFLESAVILAIVVLGGMGSLTGIAIAAIVMVGGTELLREMSFLKLIFGPDFTPELYRMLIFGLAMVVVMLFKPRGFVGSREPTAFLRERKAISGSFIKEGHG livM curated SwissProt::P22729,TCDB::P22729,ecocyc::LIVM-MONOMER,metacyc::LIVM-MONOMER High-affinity branched-chain amino acid transport system permease protein LivM; LIV-I protein M;; LivM aka B3456, component of Leucine; leucine/isoleucine/valine porter;; branched chain amino acid/phenylalanine ABC transporter membrane subunit LivM (EC 7.4.2.2);; branched chain amino acid/phenylalanine ABC transporter membrane subunit LivM (EC 7.4.2.2) MKPMHIAMALLSAAMFFVLAGVFMGVQLELDGTKLVVDTASDVRWQWVFIGTAVVFFFQLLRPAFQKGLKSVSGPKFILPAIDGSTVKQKLFLVALLVLAVAWPFMVSRGTVDIATLTMIYIILGLGLNVVVGLSGLLVLGYGGFYAIGAYTFALLNHYYGLGFWTCLPIAGLMAAAAGFLLGFPVLRLRGDYLAIVTLGFGEIVRILLLNNTEITGGPNGISQIPKPTLFGLEFSRTAREGGWDTFSNFFGLKYDPSDRVIFLYLVALLLVVLSLFVINRLLRMPLGRAWEALREDEIACRSLGLSPRRIKLTAFTISAAFAGFAGTLFAARQGFVSPESFTFAESAFVLAIVVLGGMGSQFAVILAAILLVVSRELMRDFNEYSMLMLGGLMVLMMIWRPQGLLPMTRPQLKLKNGAAKGEQA livM curated TCDB::P21628 High-affinity branched-chain amino acid transport system permease protein BraE, component of Branched chain amino acid uptake transporter. Transports alanine MSQSLKRALFSALLVILVSYPILGLKLRTVGIKLEVLGADAQTLWTIAAAALAMFVWQLFRDRIPLKLGRGVGYKVNGSGLKNFLSLPSTQRWAVLALVVVAFVWPFFASRGAVDIATLILIYVMLGIGLNIVVGLAGLLDLGYVGFYAVGAYTYALLAEYAGFGFWTALPIAGMMAALFGFLLGFPVLRLRGDYLAIVTLGFGEIIRILLRNMTEITGGPNGIGSIPKPTLFGLTFERRAPEGMQTFHEFFGIAYNTNYKVILLYVVALLLVLLALFVINRLMRMPIGRAWEALREDEVACRALGLNPTIVKLSAFTIGASFAGFAGSFFAARQGLVTPESFTFIESAMILAIVVLGGMGSQLGVILAAVVMVLLQEMRGFNEYRMLIFGLTMIVMMIWRPQGLLPMQRPHLELKP livM curated TCDB::Q8DQH9 ABC transporter membrane-spanning permease-branched chain amino acid transport, component of The branched chain hydrophobic amino acid transporter, LivJFGHM MKENLKVNILWLLLLLAGYSLISVLVSVGVLNLFYVQILQQIGINIILAVGLNLIVGFSGQFSLGHAGFMAIGAYAAAIIGSKSPTYGAFFGAMLVGALLSGAVALLVGIPTLRLKGDYLAVATLGVSEIIRIFIINGGSLTNGAAGILGIPNFTTWQMVYFFVVITTIATLNFLRSPIGRSTLSVREDEIAAESVGVNTTKIKIIAFVFGAITASIAGSLQAGFIGSVVPKDYTFINSINVLIIVVFGGLGSITGAIVSAIVLGILNMLLQDVASVRMIIYALALVLVMIFRPGGLLGTWELSLSRFFKKSKKEEQN lpd hmm TIGR01350 lpdA: dihydrolipoyl dehydrogenase (EC 1.8.1.4) TIGR01350.hmm lpd curated BRENDA::A0A0H2Z9F5,BRENDA::Q9I3D1 dihydrolipoyl dehydrogenase (EC 1.8.1.4);; dihydrolipoyl dehydrogenase (EC 1.8.1.4) MSQKFDVVVIGAGPGGYVAAIRAAQLGLKTACIEKYIGKEGKVALGGTCLNVGCIPSKALLDSSYKYHEAKEAFKVHGIEAKGVTIDVPAMVARKANIVKNLTGGIATLFKANGVTSFEGHGKLLANKQVEVTGLDGKTQVLEAENVIIASGSRPVEIPPAPLTDDIIVDSTGALEFQAVPKKLGVIGAGVIGLELGSVWARLGAEVTVLEALDKFLPAADEQIAKEALKVLTKQGLNIRLGARVTASEVKKKQVTVTFTDANGEQKETFDKLIVAVGRRPVTTDLLAADSGVTLDERGFIYVDDHCKTSVPGVFAIGDVVRGAMLAHKASEEGVMVAERIAGHKAQMNYDLIPSVIYTHPEIAWVGKTEQTLKAEGVEVNVGTFPFAASGRAMAANDTTGLVKVIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGMMVFSHPTLSEALHEAALAVNGHAIHIANRKKR lpd curated BRENDA::A0A0H2ZB32 dihydrolipoyl dehydrogenase (EC 1.8.1.4) MSQILKTSLLIVGGGPGGYVAAIRAGQLGIPTVLVEGAALGGTCLNVGCIPSKALIHAAEEYLKARHYAGRSALGIQVQAPSIDIARTVEWKDAIVDRLTSGVAALLKKHGVDVVQGWARILDGKSVAVELAGGGSQRIECEHLLLAAGSQSVELPILPLGGKVISSTEALAPGSLPKRLVVVGGGYIGLELGTAYRKLGVEVAVVEAQPRILPGYDEELTKPVAQALRKLGVELYLGHSLLGPSENGVRVRDGAGEEREIAADQVLVAVGRKPRSEGWNLESLGLDMNGRAVKVDDQCRTSMRNVWAIGDLAGEPMLAHRAMAQGEMVAELIAGKRRQFAPVAIPAVCFTDPEVVVAGLSPEQAKDAGLDCLVASFPFAANGRAMTLEANEGFVRVVARRDNHLVVGWQAVGKAVSELSTAFAQSLEMGARLEDIAGTIHAHPTLGEAVQEAALRALGHALHI lpd curated BRENDA::A0A0H2ZHZ0 dihydrolipoyl dehydrogenase (EC 1.8.1.4) MMESYDVIVIGAGPGGYNAAIRAGQLGLKVACVEGRETLGGTCLNVGCMPSKALLHASELYAAASGGEFARLGIRVSPELDLAQMMKQKDESVAALTRGVEFLFRKHKVQWIKGWARLQGEGRVGVALADGGHAQLEARDIVIATGSEPAPLPGVPVDNQRILDSTGALELAEVPRHLVVIGAGVIGLELGSVWRRLGAQVTVLEYLERICPGLDGETARTLQRALTRQGMRFRLGTRVVAARSGEQGVELDLQPAAGGATESLQADYVLVAIGRRPYTEGLGLETVGLASDRRGMLENQGQRSAAPGVWVIGDVTSGPMLAHKAEEEAIVCIERIAGHAAEMNAEVIPSVIYTQPEVASVGLGEEQLQAARREYKVGRFPFSANSRAKINHESEGFIKILSDARSDQVLGVHMIGPGVSEMIGEACVAMEFSASAEDLALTCHPHPTRSEALRQAAMDVHGRAMQN lpd curated BRENDA::A0A0K9R8G5 dihydrolipoyl dehydrogenase (EC 1.8.1.4) MQSSLSLQSSSPISTRSSHTFDFPSVSAKPLNLNVNLRFCGLRKEALSFSVNSRRVQLPCRRVPSSISAALSTNGSSPKTFDYDLLIIGAGVGGHGAALHAVEKGLKTAIIEGDVMGGTCVNRGCVPSKALLAVSGRMRELQNEQHLKSFGIQVGAANYDRQGVADHASNLASKIRGNLTNSLKALGVDILTGFGTILGPQKVQFGKDNIVTAKDIIIATGSVPFVPRGIEVDGKTVITSDHALKLESVPDWIAIVGSGYIGLEFSDVYTALGSEVTFIEALDQLMPGFDPEVSKLAQRILINPRKIDYHTGVFATKITPAKDGKPVTIELTDAKTKEHKDTLEVDAALIATGRAPYTQGLGLESINVVTQRGFVPVDDRMRVIDANGKLVPNLYCIGDANGKMMLAHAASAQGISVVEQVTGRDHVLNHLSIPAACFTHPEISMVGLTEPQAREKAEKEGFPVSVAKTSFKANSKALAENEAEGIAKLIYRPDNGEILGVHIFGLHAADLIHEASNAIAMGTPIQDLKLAVHAHPTLSEVLDELYKAAKVNVQVSSPVKEPVAV lpd curated BRENDA::A4V929 dihydrolipoyl dehydrogenase (EC 1.8.1.4) MNITIIGSGPAGVYSAIVSAKLGNKVKLVEKNDKLGGTCVLYGCIPSKAMLHPLFLKYLAEETGKKLNFSFSEIQKKLQKNVVNRLSKGVEYMLESYGIEVIHGKAQLKGGNIQVGGQTIPSVKIIVATGTEKPQIEGTIASDDLPYLDKEFSKVLVIGGGAGGVEYAWLLKMSGKDVSIVEKSDSLLPYLDEDLKKAVSAYFKKIGIKLYLSSEITLGDKPRIGNEELPQPDIILYTFGRKPALDGFEELPHEKWIKVDKRMYTGVNNIYAAGDITGTFTAHEAIHEGFIAGLNASGVEKYYNPEAVPKVIYTEPQIAYVGNTKGKCVKINMAEIPRAIAEGLTEGFLKVCTEGKKITGAVAFSHDAENIITLISMFINYGIEIDKAIDFIEPHPSYLEAVFEALLRLNS lpd curated BRENDA::A5N930 dihydrolipoyl dehydrogenase (EC 1.8.1.4) MAYKYDLIVIGTGPGGSAAALEAAKSGMKTAVIEKDKLGGTCLNRGCIPMKALLHSAGIYQEIKESKKFGIQVEKAELNVPALLQYKEGVINKLSYGMEMLLQKNKVDVFYASGKIVNAHQVAVSENGEKKIIEAERIIIASGSSAVIPPIPGIQLKNVVTSYELLNKEDLFHHLVIIGGGVIGMEFASLYSAFGCRVTVIEAMNRVLPDMDREIGTNLKQILKKQGVDIHTSASVEKLEQTQEEKILCTYREKEKLQHIEVDGVLVAIGRKPSTEGLFDENFAVETEKGKILVNKYYKTSCPSIYAIGDVIGGIQLAHAASSEALCAVRHIIGKEESLDVRVIPGCVYTNPEIAVVGITASQAKETGIDVITKKYPMMANGKSVLTMQERGFMKVVAEKETEKILGAQLMCARATDIISQFTSAIVNGMTLSQMAHVIHPHPTFSEGIGELMRE lpd curated BRENDA::B6F1A8 dihydrolipoyl dehydrogenase (EC 1.8.1.4) MPHYDVVILGAGPGGYVAAVRSAQLGLSTAIIEEKYWGGVCLNVGCIPSKALLKNAELAHTLNHKADFFGISGEFTIDYGKAFDRSRVVADGRVKGIHFLMKKNKVTEYDGRGTFTGPKAISVAKADGSTEEVTFDNAIIATGSRVRLLPGVELSDNVVTYEEQIMSRELPKSIVIVGAGAIGMEFAYVMTNYGVKVTIIEFLDRALPNEDADVSKEITKQYKNYGVDILTSTKVETVVDNGSSVTVTYTAKDGQQSSIEADKVLMSVGFAPNTEGFGLDATGVKLTERGAIDIDDHMRTNVEGIYAIGDVTAKLQLAHVAEAQGVVAAETIGKAETMTLGDYRMMPRATFCSPQVASFGLTEQQAKDEGRDIKVVSFPFMANGKAHGLGEPVGFVKLIADAEHLELIGAHMIGPDVAELLPELTLAQKWDLTALELARNVHTHPTLSEALQEGFHGLAGHMINF lpd curated BRENDA::P09622,SwissProt::P09622,metacyc::HS01727-MONOMER dihydrolipoyl dehydrogenase (EC 1.8.1.4);; Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; EC 1.8.1.4;; dihydrolipoyl dehydrogenase monomer (EC 1.8.1.4) MQSWSRVYCSLAKRGHFNRISHGLQGLSAVPLRTYADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIEMSEVRLNLDKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKADGGTQVIDTKNILIATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKIDVSIEAASGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAASFGKSINF lpd curated BRENDA::P09623,SwissProt::P09623 dihydrolipoyl dehydrogenase (EC 1.8.1.4);; Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; EC 1.8.1.4 MQSWSRVYCTLAKRGHFNRIAHGLQGVSAVPLRTYADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIEMSEVRLNLEKMMEQKSNAVKALTGGIAHLFKQNKVVRVNGYGKITGKNQVTATKADGSTEVINTKNILIATGSEVTPFPGITIDEDTVVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVELLGHVGGIGIDMEVSKNFQRILQKQGFKFKLNTKVIGATKKSDGNIDVSIEAASGGKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHIIGPGAGEMINEAALALEYGASCEDIARVCHAHPTLSEAFREANLAASFGKAINF lpd curated BRENDA::P0A9P0,CharProtDB::CH_014222,SwissProt::P0A9P0,ecocyc::E3-MONOMER,metacyc::E3-MONOMER dihydrolipoyl dehydrogenase (EC 1.8.1.4);; dihydrolipoyl dehydrogenase; EC 1.8.1.4;; Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes; Glycine cleavage system L protein; EC 1.8.1.4;; lipoamide dehydrogenase (EC 1.8.1.4);; lipoamide dehydrogenase (EC 1.8.1.4) MSTEIKTQVVVLGAGPAGYSAAFRCADLGLETVIVERYNTLGGVCLNVGCIPSKALLHVAKVIEEAKALAEHGIVFGEPKTDIDKIRTWKEKVINQLTGGLAGMAKGRKVKVVNGLGKFTGANTLEVEGENGKTVINFDNAIIAAGSRPIQLPFIPHEDPRIWDSTDALELKEVPERLLVMGGGIIGLEMGTVYHALGSQIDVVEMFDQVIPAADKDIVKVFTKRISKKFNLMLETKVTAVEAKEDGIYVTMEGKKAPAEPQRYDAVLVAIGRVPNGKNLDAGKAGVEVDDRGFIRVDKQLRTNVPHIFAIGDIVGQPMLAHKGVHEGHVAAEVIAGKKHYFDPKVIPSIAYTEPEVAWVGLTEKEAKEKGISYETATFPWAASGRAIASDCADGMTKLIFDKESHRVIGGAIVGTNGGELLGEIGLAIEMGCDAEDIALTIHAHPTLHESVGLAAEVFEGSITDLPNPKAKKK lpd curated BRENDA::P50970 dihydrolipoyl dehydrogenase (EC 1.8.1.4) MADHFDLIVLGGGPGGYVAAIRAAQLNLKVALVERVHLGGICLNWGCIPTKSLLRSAEVYHEMQNAEAYGLTSFKPDFDLDKIIARSREVATRLASGVKTLLRKNKVEVISGVGQLTGNQQMLVETTEGEEKILEAKDIIIATGARARQLPNVHSDGKHIWTYHHALKPPAMPKKLLVIGSGAIGIEFASFYADFGAEVSIVEHAPQILPMEDAEVSAYVAKAFKKRGIRILTQSALQNLTPDDEGVTAEIAGADGKVTKERFSHAIVAIGVVANVENIGLDKLGIKLDRGFIAVDGFGRTNVDHVWAIGDVAGAPCLAHKASHQGVIAAEAIAGCDHVHPLNTQNIPGCTYARPQVASVGLTEEKARQQGYNVKIGNFPFIANGKAIAQGATDGFVKTVFDADSGALLGAHMVGAEVTEMIQGYTVARTLETTEAEIMETIFPHPTLSEAMHESVLAAYGRALHF lpd curated BRENDA::P9WHH8,BRENDA::P9WHH9,SwissProt::P9WHH9 dihydrolipoyl dehydrogenase (EC 1.8.1.4);; dihydrolipoyl dehydrogenase (EC 1.8.1.4);; Dihydrolipoyl dehydrogenase; LPD; Component of peroxynitrite reductase/peroxidase complex; Component of PNR/P; Dihydrolipoamide dehydrogenase; E3 component of alpha-ketoacid dehydrogenase complexes; EC 1.8.1.4 MTHYDVVVLGAGPGGYVAAIRAAQLGLSTAIVEPKYWGGVCLNVGCIPSKALLRNAELVHIFTKDAKAFGISGEVTFDYGIAYDRSRKVAEGRVAGVHFLMKKNKITEIHGYGTFADANTLLVDLNDGGTESVTFDNAIIATGSSTRLVPGTSLSANVVTYEEQILSRELPKSIIIAGAGAIGMEFGYVLKNYGVDVTIVEFLPRALPNEDADVSKEIEKQFKKLGVTILTATKVESIADGGSQVTVTVTKDGVAQELKAEKVLQAIGFAPNVEGYGLDKAGVALTDRKAIGVDDYMRTNVGHIYAIGDVNGLLQLAHVAEAQGVVAAETIAGAETLTLGDHRMLPRATFCQPNVASFGLTEQQARNEGYDVVVAKFPFTANAKAHGVGDPSGFVKLVADAKHGELLGGHLVGHDVAELLPELTLAQRWDLTASELARNVHTHPTMSEALQECFHGLVGHMINF lpd curated BRENDA::Q04829 dihydrolipoyl dehydrogenase (EC 1.8.1.4) MVVGDIATGTELLVIGAGPGGYVAAIRAAQNGIDTTLVEKDAYGGTCLNYGCIPSKALITGANLAHEAGNAEEMGIHADPVVDMSQLRDWKSGVVDQLTGGVEKLCKANGVNLVEGTARFKDENAVRIAHGGEGQGSETIEFEHCIIATGSRVIQIPGFDFGDEPVWSSRDALEADTVPERLVVVGGGYIGMELSTTFAKLGADVTVVEMLDDILPGYESDVARVVRKRAEELGIDMHLGEGASGWREEDDGIMVTTETEDGEENEYRADKVLVAVGRSPVTDTMDIENAGLEADDRGFLSVDDRRRTDVEHIYAVGDVVEDTPMLAHVASKEGIVAAEHVAGEPVAFDSQAVPAAVFTDPEIGTVGMTEADAEEAGFTPVVGQMPFRASGRALTTNHADGFVRVVADEESGFVLGAQIVGPEASELIAELAFAIEMGATLEDVASTIHTHPTLAEAVMEAAENALGQAIHTLNR lpd curated BRENDA::Q0KBV8,CharProtDB::CH_010326 dihydrolipoyl dehydrogenase (EC 1.8.1.4);; dihydrolipoyl dehydrogenase; EC 1.8.1.4 MSVIEVKVPDIGDFDAVEVIEVLVKAGDTVEVEQSLIVLESDKASMDVPSSAAGKVVEVKVKVGDKVGQGAVICTIEAQQAAAAPAPAQAPAPAQAPAPAAAAPAPAPAAASHSGGADIQCEMLVLGAGPGGYSAAFRAADLGMNTVLVERYSTLGGVCLNVGCIPSKALLHNAAVIDEAKALAAHGILFGEAKIDLDGLRHYKNQVVGKLTGGLAGMAKARKVQVVRGIGNFLDPHHMEVELTEGEGKRSTGKKTVIRFEKAIIAAGSQAVKLPFIPEDPRIVDSTGALELPEVPNKMLVIGGGIIGLEMATVYSTLGADIDVVEMLDGLMNGADRDLVKVWEKKNKDRFGKVMLKTKTVGVEAKPDGIYVKFEGEAAPAEPQRYDLVLVSVGRSPNGKRISAEKAGVAVSERGFINVDKQMRTNVPHIFAIGDIVGQPMLAHKAVHEAHVAAEAAHGEKAYFDAKQIPSVAFTDPEVAWAGLTEDECKEKGIKYSKGVFPWAASGRAIANGRDEGFTKLIFDEETHRVIGGGIVGTHAGDLISEVCLAIEMGADAVDIGKTIHPHPTLGESIGMAAEIYEGTCTDVPPPRKR lpd curated BRENDA::Q8MUB0 dihydrolipoyl dehydrogenase (EC 1.8.1.4) MGYKFLKLASPTFRSGSLVRIATRQYATTHDADLVVIGSGPGGYVAAIKAAQLGMKVVSVEKDPTLGGTCLNVGCIPSKALLHNSHLYHMAKHDFKQRGIETGEVTFDFKKMMEYKANAVKGLTGGIAMLFQKNKVNLVKGVGTIVAPNKVEVHGEKGVETVNTKNILIASGSEVTPFPGVTFDEKQIITSTGALSLESVPKKMLVIGAGVIGLELGSVYQRLGADVTAIEFLTSIGGVGIDGEVAKTLQKILSKQGMKFKLGTKVLGVKKEGSTIKVDVEAAKGGNKEVLDCDVVLISIGRRPYTKGLGLDKVGIALDDRGRIPVNNKFQTTVPGIYAIGDVIHGPMLAHKAEDEGIVCVEGIKGMPVHFNYDAIPSVIYTSPEVGWVGKTEEDLKKEGRAYKVGKFPFLANSRAKTNGETEGFVKVLSDKTTDVILGTHIIGPGGGELINEAVLAQEYGAAAEDVARVCHAHPTCAEALREANLAAYSGKPINF lpd curated BRENDA::Q8VPK7 dihydrolipoyl dehydrogenase (EC 1.8.1.4) MALEVIMPKAGVDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYLGEERENIPTAGAASPEASPVPVASTSNDDGKSDDAFDIVVIGGGPAGYVAAIKAAQFGGKVALVEKSELGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGIVIENPNFTVDMEKLLETKSKVVNTLVGGVAGLLRSYGVTVHKGIGTITKDKNVLVNGSELLETKKIILAGGSKVNKINVPGMESPLVMTSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDVEVSKNLRLILERKGMTILTGTKLQEIIEENGQLRIKVEGKDDIIASKALLSIGRMPDLEGIGEVEFELDRGCIKVTEYMETSVPGIYAPGDINGTKMLAHAAFRMGEVSAENALKGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAREKYDVAIGKFNFAANGRAIASDAAQGFVKVIADKKYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSEVMYEAFADVLGMAIHSPKKK lpd curated BRENDA::Q9M5K2,SwissProt::Q9M5K2 dihydrolipoyl dehydrogenase (EC 1.8.1.4);; Dihydrolipoyl dehydrogenase 2, mitochondrial; AtmLPD2; mtLPD2; Dihydrolipoamide dehydrogenase 2; Glycine cleavage system L protein 2; Pyruvate dehydrogenase complex E3 subunit 2; E3-2; PDC-E3 2; EC 1.8.1.4 MAMASLARRKAYFLTRNISNSPTDAFRFSFSLTRGFASSGSDDNDVVIIGGGPGGYVAAIKAAQLGLKTTCIEKRGALGGTCLNVGCIPSKALLHSSHMYHEAKHVFANHGVKVSSVEVDLPAMLAQKDTAVKNLTRGVEGLFKKNKVNYVKGYGKFLSPSEVSVDTIDGENVVVKGKHIIVATGSDVKSLPGITIDEKKIVSSTGALSLTEIPKKLIVIGAGYIGLEMGSVWGRLGSEVTVVEFAADIVPAMDGEIRKQFQRSLEKQKMKFMLKTKVVGVDSSGDGVKLIVEPAEGGEQTTLEADVVLVSAGRTPFTSGLDLEKIGVETDKGGRILVNERFSTNVSGVYAIGDVIPGPMLAHKAEEDGVACVEFIAGKHGHVDYDKVPGVVYTYPEVASVGKTEEQLKKEGVSYNVGKFPFMANSRAKAIDTAEGMVKILADKETDKILGVHIMSPNAGELIHEAVLAINYDASSEDIARVCHAHPTMSEAIKEAAMATYDKPIHM lpd curated CharProtDB::CH_004665,metacyc::MONOMER-11687 dihydrolipoyl dehydrogenase; EC 1.8.1.4;; dihydrolipoyl dehydrogenase component subunit (EC 1.8.1.4) MVVGDFPIETDTLVIGAGPGGYVAAIRAAQLGQKVTVVEKATLGGVCLNVGCIPSKALINAGHRYENAKHSDDMGITAENVTVDFTKVQEWKASVVNKLTGGVAGLLKGNKVDVVKGEAYFVDSNSVRVMDENSAQTYTFKNAIIATGSRPIELPNFKYSERVLNSTGALALKEIPKKLVVIGGGYIGTELGTAYANFGTELVILEGGDEILPGFEKQMSSLVTRRLKKKGNVEIHTNAMAKGVEERPDGVTVTFEVKGEEKTVDADYVLITVGRRPNTDELGLEQVGIEMTDRGIVKTDKQCRTNVPNIYAIGDIIEGPPLAHKASYEGKIAAEAIAGEPAEIDYLGIPAVVFSEPELASVGYTEAQAKEEGLDIVAAKFPFAANGRALSLNETDGFMKLITRKEDGLVIGAQIAGASASDMISELSLAIEGGMTAEDIAMTIHAHPTLGEITMEAAEVAIGSPIHIVK lpd curated CharProtDB::CH_006552 TPP-dependent acetoin dehydrogenase complex, E3 component, dihydrolipoyl dehydrogenase; EC 1.8.1.4 MAKIVVMPKLGLTMTEGTLVTWKKAEGDQVKVGEILFEVSTDKLTNEVESSDEGIVRKLLVNEGDVVECLNPVAIIGSADEDISSLLNGSSEGSGSAEQSDTKAPKKEVEAVKGGDNLVVIGGGPGGYVAAIRAAQLGAKVTLIEKESLGGTCLNVGCIPTKVLLHSSQLLTEMKEGDKLGIDIEGSIVVNWKHIQKRKKIVIKKLVSGVSGLLTCNKVKVIKGTAKFESKDTILVTKEDGVAEKVNFDNAIIATGSMPFIPEIEGNKLSGVIDSTGALSLESNPESIAIIGGGVIGVEFASIFNSLGCKVSIIEMLPHILPPMDREISEIAKAKLIRDGININNNCKVTRIEQGEDGLKVSFIGDKGEESIDVEKVLIAVGRRSNIEGLDVEKIGVKTEGGSIIVNDKMETNVEGIYAIGDCTGKIMLAHVASDQGVVAAENIMGQNKKMDYKTVPACVYTKPELASVGLTEEQAKEKGIDYKVGKFQLAANGKSLIMNETGGVIKIITDKKYEEILGVHILGPRATDLITEAALALRLEATLEEIITTVHAHPTVGEAMKEAALAVNNQAIHMMNK lpd curated CharProtDB::CH_015561 dihydrolipoyl dehydrogenase; EC 1.8.1.4 MTQKFDVVVIGAGPGGYVAAIKAAQLGLKTACIEKYTDAEGKLALGGTCLNVGCIPSKALLDSSWKYKEAKESFNVHGISTGEVKMDVAAMVGRKAGIVKNLTGGVATLFKANGVTSIQGHGKLLAGKKVEVTKADGTTEVIEAENVILASGSRPIDIPPAPVDQNVIVDSTGALEFQAVPKRLGVIGAGVIGLELGSVWARLGAEVTVLEALDTFLMAADTAVSKEAQKTLTKQGLDIKLGARVTGSKVNGNEVEVTYTNAEGEQKITFDKLIVAVGRRPVTTDLLAADSGVTIDERGYIFVDDYCATSVPGVYAIGDVVRGMMLAHKASEEGIMVVERIKGHKAQMNYDLIPSVIYTHPEIAWVGKTEQALKAEGVEVNVGTFPFAASGRAMAANDTGGFVKVIADAKTDRVLGVHVIGPSAAELVQQGAIAMEFGTSAEDLGMMVFSHPTLSEALHEAALAVNGGAIHVANRKKR lpd curated CharProtDB::CH_123536 dihydrolipoyl dehydrogenase; EC 1.8.1.4 MLRSFKSIPANGKLAQFVRYASTKKYDVVVIGGGPGGYVAAIKAAQLGLNTACIEKRGALGGTCLNVGCIPSKSLLNNSHLLHQIQHEAKERGISIQGEVGVDFPKLMAAKEKAVKQLTGGIEMLFKKNKVDYLKGAGSFVNEKTVKVTPIDGSEAQEVEADHIIVATGSEPTPFPGIEIDEERIVTSTGILSLKEVPERLAIIGGGIIGLEMASVYARLGSKVTVIEFQNAIGAGMDAEVAKQSQKLLAKQGLDFKLGTKVVKGERDGEVVKIEVEDVKSGKKSDLEADVLLVAIGRRPFTEGLNFEAIGLEKDNKGRLIIDDQFKTKHDHIRVIGDVTFGPMLAHKAEEEGIAAAEYIKKGHGHVNYANIPSVMYTHPEVAWVGLNEEQLKEQGIKYKVGKFPFIANSRAKTNMDTDGFVKFIADAETQRVLGVHIIGPNAGEMIAEAGLALEYGASTEDISRTCHAHPTLSEAFKEAALATFDKPINF lpd curated CharProtDB::CH_124461 dihydrolipoamide dehydrogenase Dld1; EC 1.8.1.4 MLNSVIKRSALCRFKFTCLQVSECRPAQIEISKRLYSAKASGNGEYDLCVIGGGPGGYVAAIRGAQLGLKTICVEKRGTLGGTCLNVGCIPSKALLNNSHIYHTVKHDTKRRGIDVSGVSVNLSQMMKAKDDSVKSLTSGIEYLFKKNKVEYAKGTGSFIDPQTLSVKGIDGAADQTIKAKNFIIATGSEVKPFPGVTIDEKKIVSSTGALSLSEVPKKMTVLGGGIIGLEMGSVWSRLGAEVTVVEFLPAVGGPMDADISKALSRIISKQGIKFKTSTKLLSAKVNGDSVEVEIENMKNNKRETYQTDVLLVAIGRVPYTEGLGLDKLGISMDKSNRVIMDSEYRTNIPHIRVIGDATLGPMLAHKAEDEGIAAVEYIAKGQGHVNYNCIPAVMYTHPEVAWVGITEQKAKESGIKYRIGTFPFSANSRAKTNMDADGLVKVIVDAETDRLLGVHMIGPMAGELIGEATLALEYGASAEDVARVCHAHPTLSEATKEAMMAAWCGKSIHF lpd curated SwissProt::A8MS68 Dihydrolipoyl dehydrogenase 1, chloroplastic; ptLPD1; Dihydrolipoamide dehydrogenase 1; Protein LIPOAMIDE DEHYDROGENASE 1; Pyruvate dehydrogenase complex E3 subunit 1; E3-1; PDC-E3 1; EC 1.8.1.4 MQSAMALSFSQTSFTRPNHVLGSSGSVFSTPRSLRFCGLRREAFGFSTSNQLAIRSNRIQFLSRKSFQVSASASSNGNGAPPKSFDYDLIIIGAGVGGHGAALHAVEKGLKTAIIEGDVVGGTCVNRGCVPSKALLAVSGRMRELQNEHHMKSFGLQVSAAGYDRQGVADHANNLATKIRNNLTNSMKAIGVDILTGFGSVLGPQKVKYGKDNIITAKDIIIATGSVPFVPKGIEVDGKTVITSDHALKLESVPEWIAIVGSGYIGLEFSDVYTALGSEVTFIEALDQLMPGFDPEISKLAQRVLINPRKIDYHTGVFASKITPARDGKPVLIELIDAKTKEPKDTLEVDAALIATGRAPFTNGLGLENVNVVTQRGFIPVDERMRVIDGKGTLVPNLYCIGDANGKLMLAHAASAQGISVVEQVSGRDHVLNHLSIPAACFTHPEISMVGLTEPQAKEKGEKEGFKVSVVKTSFKANTKALAENEGEGIAKMIYRPDNGEILGVHIFGLHAADLIHEASNAIALGTRIQDIKLAVHAHPTLSEVLDELFKAAKVESHATTRTGDAKIKLNTNQEDRKGRRRGGDDEKQPSVSKDLKDISTRPSSFFENISVGVLSLLSLIFV lpd curated SwissProt::F4JLP5 Dihydrolipoyl dehydrogenase 2, chloroplastic; ptLPD2; Dihydrolipoamide dehydrogenase 2; Protein LIPOAMIDE DEHYDROGENASE 2; Pyruvate dehydrogenase complex E3 subunit 2; E3-2; PDC-E3 2; EC 1.8.1.4 MQSVLSLSFSQASLPLANRTLCSSNAAPSTPRNLRFCGLRREAFCFSPSKQLTSCRFHIQSRRIEVSAAASSSAGNGAPSKSFDYDLIIIGAGVGGHGAALHAVEKGLKTAIIEGDVVGGTCVNRGCVPSKALLAVSGRMRELQNEHHMKAFGLQVSAAGYDRQGVADHASNLATKIRNNLTNSMKALGVDILTGFGAVLGPQKVKYGDNIITGKDIIIATGSVPFVPKGIEVDGKTVITSDHALKLESVPDWIAIVGSGYIGLEFSDVYTALGSEVTFIEALDQLMPGFDPEISKLAQRVLINTRKIDYHTGVFASKITPAKDGKPVLIELIDAKTKEPKDTLEVDAALIATGRAPFTNGLGLENINVTTQRGFIPVDERMRVIDGNGKLVPHLYCIGDANGKLMLAHAASAQGISVVEQVTGRDHVLNHLSIPAACFTHPEISMVGLTEPQAREKAEKEGFKVSIAKTSFKANTKALAENEGEGLAKMIYRPDNGEILGVHIFGLHAADLIHEASNAIALGTRIQDIKLAVHAHPTLSEVVDELFKAAKVDSPASVTAQSVKVTV lpd curated SwissProt::O08749 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; EC 1.8.1.4 MQSWSRVYRSLAKKGHFNRISHGLQGVSSVPLRTYADQPIEADVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIEIPEVRLNLEKMMEQKHSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVTATKADGSTQVIDTKNILVATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGIGIDMEISKNFQRILQRQGFKFKLNTKVTGATKKSDGKIDVSVEAASGGKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNNRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEFKIGKFPFAANSRAKTNADTDGMVKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAAAFGKPINF lpd curated SwissProt::P09063 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of branched-chain alpha-keto acid dehydrogenase complex; LPD-Val; EC 1.8.1.4 MQQTIQTTLLIIGGGPGGYVAAIRAGQLGIPTVLVEGQALGGTCLNIGCIPSKALIHVAEQFHQASRFTEPSPLGISVASPRLDIGQSVAWKDGIVDRLTTGVAALLKKHGVKVVHGWAKVLDGKQVEVDGQRIQCEHLLLATGSSSVELPMLPLGGPVISSTEALAPKALPQHLVVVGGGYIGLELGIAYRKLGAQVSVVEARERILPTYDSELTAPVAESLKKLGIALHLGHSVEGYENGCLLANDGKGGQLRLEADRVLVAVGRRPRTKGFNLECLDLKMNGAAIAIDERCQTSMHNVWAIGDVAGEPMLAHRAMAQGEMVAEIIAGKARRFEPAAIAAVCFTDPEVVVVGKTPEQASQQGLDCIVAQFPFAANGRAMSLESKSGFVRVVARRDNHLILGWQAVGVAVSELSTAFAQSLEMGACLEDVAGTIHAHPTLGEAVQEAALRALGHALHI lpd curated SwissProt::P09624 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine decarboxylase complex subunit L; Lipoamide dehydrogenase component of pyruvate dehydrogenase complex; Pyruvate dehydrogenase complex E3 component; EC 1.8.1.4 MLRIRSLLNNKRAFSSTVRTLTINKSHDVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLGGTCLNVGCIPSKALLNNSHLFHQMHTEAQKRGIDVNGDIKINVANFQKAKDDAVKQLTGGIELLFKKNKVTYYKGNGSFEDETKIRVTPVDGLEGTVKEDHILDVKNIIVATGSEVTPFPGIEIDEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASMDGEVAKATQKFLKKQGLDFKLSTKVISAKRNDDKNVVEIVVEDTKTNKQENLEAEVLLVAVGRRPYIAGLGAEKIGLEVDKRGRLVIDDQFNSKFPHIKVVGDVTFGPMLAHKAEEEGIAAVEMLKTGHGHVNYNNIPSVMYSHPEVAWVGKTEEQLKEAGIDYKIGKFPFAANSRAKTNQDTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCHAHPTLSEAFKEANMAAYDKAIHC lpd curated SwissProt::P11959,BRENDA::P11959,CharProtDB::CH_015557 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4;; dihydrolipoyl dehydrogenase (EC 1.8.1.4);; dihydrolipoyl dehydrogenase; EC 1.8.1.4 MVVGDFAIETETLVVGAGPGGYVAAIRAAQLGQKVTIVEKGNLGGVCLNVGCIPSKALISASHRYEQAKHSEEMGIKAENVTIDFAKVQEWKASVVKKLTGGVEGLLKGNKVEIVKGEAYFVDANTVRVVNGDSAQTYTFKNAIIATGSRPIELPNFKFSNRILDSTGALNLGEVPKSLVVIGGGYIGIELGTAYANFGTKVTILEGAGEILSGFEKQMAAIIKKRLKKKGVEVVTNALAKGAEEREDGVTVTYEANGETKTIDADYVLVTVGRRPNTDELGLEQIGIKMTNRGLIEVDQQCRTSVPNIFAIGDIVPGPALAHKASYEGKVAAEAIAGHPSAVDYVAIPAVVFSDPECASVGYFEQQAKDEGIDVIAAKFPFAANGRALALNDTDGFLKLVVRKEDGVIIGAQIIGPNASDMIAELGLAIEAGMTAEDIALTIHAHPTLGEIAMEAAEVALGTPIHIITK lpd curated SwissProt::P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 MSQKFDVVVIGAGPGGYVAAIRAAQLGLKTACIEKYIGKEGKVALGGTCLNVGCIPSKALLDSSYKYHEAKEAFKVHGIEAKGVTIDVPAMVARKANIVKNLTGGIATLFKANGVTSFEGHGKLLANKQVEVTGLDGKTQVLEAENVIIASGSRPVEIPPAPLSDDIIVDSTGALEFQAVPKKLGVIGAGVIGLELGSVWARLGAEVTVLEALDKFLPAADEQIAKEALKVLTKQGLNIRLGARVTASEVKKKQVTVTFTDANGEQKETFDKLIVAVGRRPVTTDLLAADSGVTLDERGFIYVDDHCKTSVPGVFAIGDVVRGAMLAHKASEEGVMVAERIAGHKAQMNYDLIPSVIYTHPEIAWVGKTEQTLKAEGVEVNVGTFPFAASGRAMAANDTTGLVKVIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGMMVFSHPTLSEALHEAALAVNGHAIHIANRKKR lpd curated SwissProt::P18925,CharProtDB::CH_015565 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4;; dihydrolipoyl dehydrogenase; EC 1.8.1.4 MSQKFDVIVIGAGPGGYVAAIKSAQLGLKTALIEKYKGKEGKTALGGTCLNVGCIPSKALLDSSYKFHEAHESFKLHGISTGEVAIDVPTMIARKDQIVRNLTGGVASLIKANGVTLFEGHGKLLAGKKVEVTAADGSSQVLDTENVILASGSKPVEIPPAPVDQDVIVDSTGALDFQNVPGKLGVIGAGVIGLELGSVWARLGAEVTVLEAMDKFLPAVDEQVAKEAQKILTKQGLKILLGARVTGTEVKNKQVTVKFVDAEGEKSQAFDKLIVAVGRRPVTTDLLAADSGVTLDERGFIYVDDYCATSVPGVYAIGDVVRGAMLAHKASEEGVVVAERIAGHKAQMNYDLIPAVIYTHPEIAGVGKTEQALKAEGVAINVGVFPFAASGRAMAANDTAGFVKVIADAKTDRVLGVHVIGPSAAELVQQGAIAMEFGTSAEDLGMMVFAHPALSEALHEAALAVSGHAIHVANRKK lpd curated SwissProt::P31023 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; Pyruvate dehydrogenase complex E3 subunit; E3; PDC-E3; EC 1.8.1.4 MAMANLARRKGYSLLSSETLRYSFSLRSRAFASGSDENDVVIIGGGPGGYVAAIKAAQLGFKTTCIEKRGALGGTCLNVGCIPSKALLHSSHMYHEAKHSFANHGVKVSNVEIDLAAMMGQKDKAVSNLTRGIEGLFKKNKVTYVKGYGKFVSPSEISVDTIEGENTVVKGKHIIIATGSDVKSLPGVTIDEKKIVSSTGALALSEIPKKLVVIGAGYIGLEMGSVWGRIGSEVTVVEFASEIVPTMDAEIRKQFQRSLEKQGMKFKLKTKVVGVDTSGDGVKLTVEPSAGGEQTIIEADVVLVSAGRTPFTSGLNLDKIGVETDKLGRILVNERFSTNVSGVYAIGDVIPGPMLAHKAEEDGVACVEYLAGKVGHVDYDKVPGVVYTNPEVASVGKTEEQVKETGVEYRVGKFPFMANSRAKAIDNAEGLVKIIAEKETDKILGVHIMAPNAGELIHEAAIALQYDASSEDIARVCHAHPTMSEAIKEAAMATYDKPIHI lpd curated SwissProt::P80647 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; EC 1.8.1.4 LSSGEKDLVVIGSGPGGYVAAIKAAQLGMLTVCIEKYPTFGGTCLNVGCIPSK lpd curated SwissProt::P85207 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; EC 1.8.1.4 MKTYDLIVIGTGPGGYPAAIRGAQLGLKVLAVEAAEVGGVCLNVGCIPTKALLHAAETVHHLKGAEGFGLKAKPELDLKKLGAWRDGVVKKLTGGVAGLLKGNKVELLRGFARFKGPREIEVNGETYGAQSFIIATGSEPMPLKGFPFGEDVWDSTRALRVEEGIPKRLLVIGGGAVGLELGQIYHRLGSEVTLIEYMPEILPAGDRETAALLRKALEKEGLKVRTGTKAVGYEKKQDGLHVLLEAAQGGSQEEIVVDKILVAVGRRPRTEGLGLEKAGVKVDERGFIQVNARMETSAPGVYAIGDVARPPLLAHKAMKEGLVAAENAAGKNALFDFQVPSVVYTGPEWAGVGLTEEEARKAGYNVKVGKFPFSASGRALTLGGAEGLIKVVGDAETDLLLGVFVVGPQAGELIAEATLALEMGATVSDLGLTIHPHPTLSEGLMEAAEALHKQAIHILNR lpd curated SwissProt::Q811C4 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; EC 1.8.1.4 FNRXSPGLQGVSSVPLRTYADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHLAHGKDFASRGIELSEVRLNLEKMMEQKSSAVKALTGGIAHLFKQNKVVHVNGFGNITGKNQVTATKADGSSQVIGTKNILIATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGAEVTAVEFLGHVGGIGIDMEISKKFQRILQKQGFKFKLNPKVPGATKRSDGKIDVSVEAAPGGKAEVIPCDVLLVCIGRRPFTQNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFR lpd curated SwissProt::Q8NTE1 Dihydrolipoyl dehydrogenase; LPD; Dihydrolipoamide dehydrogenase; E3 component of alpha-ketoacid dehydrogenase complexes; EC 1.8.1.4 MTEHYDVVVLGAGPGGYVSAIRAAQLGKKVAVIEKQYWGGVCLNVGCIPSKSLIKNAEVAHTFTHEKKTFGINGEVTFNYEDAHKRSRGVSDKIVGGVHYLMKKNKIIEIHGLGNFKDAKTLEVTDGKDAGKTITFDDCIIATGSVVNTLRGVDFSENVVSFEEQILNPVAPKKMVIVGAGAIGMEFAYVLGNYGVDVTVIEFMDRVLPNEDAEVSKVIAKAYKKMGVKLLPGHATTAVRDNGDFVEVDYQKKGSDKTETLTVDRVMVSVGFRPRVEGFGLENTGVKLTERGAIEIDDYMRTNVDGIYAIGDVTAKLQLAHVAEAQGIVAAETIAGAETQTLGDYMMMPRATFCNPQVSSFGYTEEQAKEKWPDREIKVASFPFSANGKAVGLAETDGFAKIVADAEFGELLGAHLVGANASELINELVLAQNWDLTTEEISRSVHIHPTLSEAVKEAAHGISGHMINF lpd curated SwissProt::Q9M5K3 Dihydrolipoyl dehydrogenase 1, mitochondrial; AtmLPD1; mtLPD1; Dihydrolipoamide dehydrogenase 1; Glycine cleavage system L protein 1; Pyruvate dehydrogenase complex E3 subunit 1; E3-1; PDC-E3 1; EC 1.8.1.4 MAMASLARRKAYFLTRNLSNSPTDALRFSFSLSRGFASSGSDENDVVIIGGGPGGYVAAIKASQLGLKTTCIEKRGALGGTCLNVGCIPSKALLHSSHMYHEAKHSFANHGIKVSSVEVDLPAMLAQKDNAVKNLTRGIEGLFKKNKVTYVKGYGKFISPNEVSVETIDGGNTIVKGKHIIVATGSDVKSLPGITIDEKKIVSSTGALSLSEVPKKLIVIGAGYIGLEMGSVWGRLGSEVTVVEFAGDIVPSMDGEIRKQFQRSLEKQKMKFMLKTKVVSVDSSSDGVKLTVEPAEGGEQSILEADVVLVSAGRTPFTSGLDLEKIGVETDKAGRILVNDRFLSNVPGVYAIGDVIPGPMLAHKAEEDGVACVEFIAGKHGHVDYDKVPGVVYTHPEVASVGKTEEQLKKEGVSYRVGKFPFMANSRAKAIDNAEGLVKILADKETDKILGVHIMAPNAGELIHEAVLAINYDASSEDIARVCHAHPTMSEALKEAAMATYDKPIHI lpd curated metacyc::MONOMER-12931 lipoamide dehydrogenase (EC 1.8.1.4) MQRWGRVSCALARRSHFDRVHHGLQGGCAVPQRTYADQVDADVTVIGSGPGGYVAAIKAAQLGFKTVCVEKNETLGGTCLNVGCIPSKALLNNSHLYHLAHGKDFASRGIEITGIRLNLEKMMEQKSSAVKALTGGIAHLFKQNKVVHVSGFGRITGKNQVTATKDDGSTQVINTKNILIATGSEVAPFPGITIDEDNIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFMGHVGGMGIDMEISKNFQRILQKQGLKFKLNTKVTGATKKPDGKIDVAVEAAAGGKAEVITCDMLLVCIGRRPFTANLGLEDIGIELDKRGRIPVNNRFQTKIPNIYAIGDVVAGPMLAHKAEDEGILCVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGVEYKIGKFPFAANSRAKTNADTDGMVKILSQKSTDRMLGAHILGAGAGEMVNEAALAMEYGASCEDVARVCHAHPTVSEAFREANLAASFGKAINF lpd curated metacyc::MONOMER-18303 dihydrolipoyl dehydrogenase subunit (EC 1.8.1.4) MSSLCRQILVRPLCSHQFLAFAHGLFSSGNEVDLVVIGSGPGGYVAAIKAAQLGMKTVCVEKDPTFGGTCLNVGCMPSKSLLNNSHYYHMAKTGDLNNRGVEVKPTLNLEKMMAAKAGAVKALTGGIALLFKANKVQPINGLGTIVGPNEVSVKKTDGTTENLKTRNILMATGSEVTPFPGIDIDEDQIVSSTGALSLKKVPEKMVVIGAGVIGAELGSVWQRLGAQVTVVEFLDHAGGAGIDLELAKLFHSTLGKQGMKFMLNTKVTSAKKEGGKIVVQTEAVKGGKAQTLEADTLLVAIGRRPYTAQLGTENVGIKLDEKGRVPVNERFQTCVPSIYAIGDVMQGPMLAHKAEDEGVLCVEGLAGGPTHIDYNCIPSVIYTHPEVAWVGKSEETLKEENVKYKVGKFPFSANSRAKTNNETDGFVKVLGDKDTDRLLGVHIMGPNAGEMIAEAVIGLEYGASCEDIARVCHAHPTLSEAFREANLHAYCGKSINNV lpd curated metacyc::MONOMER-18551 dihydrolipoamide dehydrogenase (EC 1.8.1.4) MSQVEIKVPDIGDFDAVEVIEVLVAQGDTVKEEQSLITVESDKASMEIPSSAAGKVVSLSVKVGDKVSEGTVILMLEAAAAGAQAAASDKAAAQPAAKSEAAAQKPAASSAAAEQASAAADQRPAQAAADSSEVRYSPPASAPADGCDVLVLGAGPGGYSAAFRAADLGLSVVLVERYATLGGVCLNVGCIPSKALLHSVAVLEEAKHLSENGITFGEPAIDLDKLRASKDKVVSTLTGGLTGMAKARKVKVIQGLGQFADEYHLTVQKDDGSSETVAFKHAIIAAGSQSVKLPFLPEDERIIDSTGALKLKSIPKKMLIIGGGIIGLEMGTVYSALGARLDVVEMLDGLMQGADRDLVKVWQKKNEGRFDQIMVKTKTVSAEAKPDGIWVKFEGEAAPAEPQRYDLVLQAVGRSPNGAKIGADKAGVQVTERGFINVDEQMRTNVPHIFAIGDIVGQPMLAHKAVHEAHVAAEVIAGHKSYFDVRVIPSVAYTDPEVAWAGLTEEEAKKQGIKFEKGVFPWAASGRAIANGRSEGFTKLLFDAETHRIIGGSIVGTHAGDLISEVALAVEMGADSVDIGKTIHPHPTLGESVGMAAEVAHGTCTDLPPVKRK lpd curated metacyc::MONOMER-585 pyruvate dehydrogenase complex E3 component (EC 1.8.1.4) MNYDLIIIGAGPAGYVAAEYAGKHKLKTLVVEKEYFGGVCLNVGCIPTKTLLKRAKIVDYLRHAQDYGISINGQVALNWNQLLEQKGKVVSKLVGGVKAIIASAKAETVMGEAKVLDPNTVEVAGKTYTTKSIVVATGSRPRYLTLPGFAEARQNGFVIDSTQALSLEGVPRKLVVVGGGVIGIEFAFLYASLGSEVTILQGVDRILEIFDTEVSDLVAKLLQTKNVKIITNAQVTRANNNEVFYSQNGQEGSVVGDRILVSIGRIPNTECLDGLNLQRDERNRIVLNQDLQTSIPNIYIVGDANAQLMLAHFAYQQGRYAVNHILNKKQVKPAQKLTCPSCIYTNPEVASVGYTEMELKKQGIPYVKTNLVLAHCGKAIADNETNGFVKMMFDPQTGKILGCCIIAATASDMIAELALAMGAGLTVFDIANSISPHPTINEMIADVCKKALFDHFK lpd curated reanno::Smeli:SMc03204 Dihydrolipoyl dehydrogenase (EC 1.8.1.4) MKEISCKLLVLGAGPGGYVAAIRAGQLGVNTVIVEKAKAGGTCLNVGCIPSKALIHAADEYHRLRAAASGKGPLGLSLSAPAIDLRRTIAWKDGIVGRLNGGVTGLLKKAGVKAVIGEGRFVDGKTVDVETETGLQRIRAEAIVIATGSAPVELPDLPFGGSVISSTQALALTDVPQTLAVIGGGYIGLELGTAFAKLGSKVTVLEALDRILPQYDADLSKPVMKRLGELGVEVFTRTAAKRLSADRRGLLAEENGRAFEVPAEKVLVTVGRRPVTDGWGLEEIDLDHSGRFIRIDDQCRTSMRGVYAIGDVTGEPMLAHRAMAQGEMVAEIVAGHKRSWDKRCIPAVCFTDPEIVGAGLSPEEARAAGIDVKIGQFPFQANGRAMTTLSEDGFVRVIARADNHLVLGIQAVGHGVSELSATFALAIEMGARLEDIAGTIHAHPTQSEAFQEAALKTLGHALHI lpd curated reanno::WCS417:GFF3432 Dihydrolipoyl dehydrogenase (EC 1.8.1.4) MTQTLNTTLLIIGGGPGGYVAAIRAGQLGIPTILVEGQALGGTCLNIGCIPSKALIHVAEQFQQTIHHSQGSHLGIEVDVPTLDIRKSVEWKDGIVDRLTTGVAALLKKHKVQVIHGWAKVVDGKTVEVGDQRIQCEHLLLATGSKSVNLPMLPIGGPIISSTEALAPTRVPKRLIVVGGGYIGLELGIAYRKLGAEVSVVEAQDRILPAYDAELTQPVNESLKHLGVKLYLKHSVTGFTDGSLQVRDPNGDTVSLATDQVLVAVGRKPNTQGWNLEALNLEMNGAAIKIDSRCQTSMRNVYAIGDLSGEPMLAHRAMAQGEMVAELISGKHREFNPAAIPAVCFTDPELVVVGKTPDEAKAAGLDCIVSSFPFAANGRAMTLESKTGFVRVVARRDNHLIVGWQAVGVGVSELSTAFGLSLEMGSRLEDVAGTIHAHPTLGEAVQEAALRALGHALHL lpd curated reanno::pseudo13_GW456_L13:PfGW456L13_3543 Dihydrolipoyl dehydrogenase (EC 1.8.1.4) MQTLNTTLLIIGGGPGGYVTAIRAGQLGIPTILVEGQSLGGTCLNIGCIPSKALIHVAEQFHQTQHHSQHSALGISVSAPTLDIGKSVEWKDGIVDRLTTGVAALLKKNKVQVVQGWAKVVDGKTVEVGDTRIQCEHLVLATGSKSVNLPMLPIGGPIISSTEALAPTSVPKRLIVVGGGYIGLELGIAYRKLGAEVSVVEAQERILPAYDAELTQPVHDELKKLGVKLYLKHSVQGFDSSNNTLQVLAPNGETLNLETDQVLVAVGRKPNTQGWNLEALNLDMNGSSIKIDNRCQTSMRNVYAIGDLSGEPMLAHRAMAQGEMVAELISGKTREFNPTAIAAVCFTDPELVVVGKTPDEAKAAGWDCIVSSFPFAANGRAMTLESKSGFVRVVARRDNHVIVGWQAVGVGVSELSTAFAQSLEMGARLEDIGGTIHAHPTLGEAVQEAALRALGHALHL lpd curated reanno::pseudo5_N2C3_1:AO356_22975 Dihydrolipoyl dehydrogenase (EC 1.8.1.4) MQQTLNTTLLIIGGGPGGYVAAIRAGQLGISTILVEGQALGGTCLNIGCIPSKALIHVAEQFHQTRHHSQGSALGITVAAPTLDIGKSVEWKDGIVDRLTTGVAALLKKHKVQVIHGWAKVIDGKTVEVGDTRIQCEHLLLATGSKSVNLPMLPLGGPIISSTEALAPTSVPKHLVVVGGGYIGLELGIAYRKLGAEVSVVEAQERILPAYDGELTQPVHEALKQLGVKLYLKHSVEGFDAQASTLQVRDPNGDTLNLETDRVLVAVGRKPNTQGWNLAALDLAMNGSAVKIDSRCQTSMRNVWAIGDLSGEPMLAHRAMAQGEMVAELIAGQHREFNPTAIAAVCFTDPELVVVGKTPDEAKAAGLDCLVSSFPFAANGRAMTLESKSGFVRVVARRDNHLIVGWQAVGVGVSELSTAFGQSLEMGARLEDIAGTIHAHPTLGEAVQEAALRALGHALHL lpd curated reanno::pseudo6_N2E2:Pf6N2E2_478 Dihydrolipoyl dehydrogenase (EC 1.8.1.4) MQQTLNTTLLIIGGGPGGYVAAIRAGQLGIPTILVEGQALGGTCLNIGCIPSKALIHVAEQFHQTRHHSQGSALGITVSAPSLDIGKSVEWKDGIVDRLTTGVAALLKKHKVQVIHGWAKVIDGKTVEVGDTRIQCEHLLLATGSKSVDLPMLPVGGPIISSTEALAPTSVPKHLVVVGGGYIGLELGIAYRKLGAEVSVVEAQERILPAYDGELTQPVHEALKQLGVKLYLKHSVEGFDAQASTLQVRDPAGDTLNLDTDRVLVAVGRKPNTQGWNLEALNLAMNGAAVKIDQRCQTSMRNVWAIGDLSGEPMLAHRAMAQGEMVAELIAGQHREFNPTAIAAVCFTDPELVVVGKTPDEAKAAGLDCIVSSFPFAANGRAMTLESKSGFVRVVARRDNHLIVGWQAVGVGVSELSTAFGQSLEMGARLEDIAGTIHAHPTLGEAVQEAALRALGHALHL lpd curated2 O05940 Dihydrolipoyl dehydrogenase; EC 1.8.1.4; Dihydrolipoamide dehydrogenase; E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes; ORF-E3 MAESYDVIIIGSGPGGYVAAIRASQLGLKTAIVEREHMGGICLNWGCIPTKALLRSAEVLDHANHFKDFGLVLEGSVKPDAKAVVGRSRAVSARLNAGVGFLMKKNKIDIIWGEAKLTKPGEIVVGKSSKPVVEPQHPLPKNVKGEGTYTAKHIIIATGARPRALPGIEPDGKLIWTYFEALKPDALPKSLIVMGSGAIGIEFASFYRSMGVDVTVVEVMPTIMPVEDAEITAIARKQLEKRGLKIFTSAKVTKVEKGAGSITAHVETSDGKVQQITADRMISAVGVQGNIENLGLEALGVKTDRGCVVADGYGKTNVAGIYAIGDVAGPPMLAHKAEHEGVVCVEKIAGLPNVHPTDKGKVPGCTYCNPQVASVGLTEAKAKELGRDIRVGRFSFAANGKAIALGEDQGMVKVIFDKKTGELLGAHMVGAEVTELIQGFVVAMNLETTEEELMHTIFPHPTVSETMKEAVLDAYGRVLNA lpd curated2 O34324 Dihydrolipoyl dehydrogenase; EC 1.8.1.4; Dihydrolipoamide dehydrogenase; E3 component of acetoin cleaving system MTLAIIGGGPAGYAAAVSAAQQGRNVLLIDKGKLGGTCLNEGCIPTKSLLESANVLDKIKHADSFGIELPAGAISVDWSKMQSRKQQVVSQLVQGVQYLMKKNQIQVVKGTASFLSERKLLIEGENGKEIREADQVLIASGSEPIELPFAPFDGEWILDSKDALSLSEIPSSLVIVGGGVIGCEYAGLFARLGSQVTIIETADRLIPAEDEDIARLFQEKLEEDGVEVHTSSRLGRVDQTAKTAIWKSGQREFKTKADYVLVAIGRKPRLDGLQLEQAGVDFSPKGIPVNGHMQTNVPHIYACGDAIGGIQLAHAAFHEGIIAASHASGRDVKINEKHVPRCIYTSPEIACIGMTERQARSIYGDVKIGEFSFSANGKALIKQQAEGKVKIMAEPEFGEIVGVSMIGPDVTELIGQAAAIMNGEMTADMAEHFIAAHPTLSETLHEALLSTIGLAVHA lpd curated2 O84561 Dihydrolipoyl dehydrogenase; EC 1.8.1.4; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex MNEAFDCVVIGAGPGGYVAAITAAQAGLKTALIEKREAGGTCLNRGCIPSKALLAGAEVVTQIRHADQFGIHVEGFSINYPAMVQRKDSVVRSIRDGLNGLIRSNKITVFSGRGSLISSTEVKILGENPSVIKAHSIILATGSEPRAFPGIPFSAESPRILCSTGVLNLKEIPQKMAIIGGGVIGCEFASLFHTLGSEVSVIEASSQILALNNPDISKTMFDKFTRQGLRFVLEASVSNIEDIGDRVRLTINGNVEEYDYVLVSIGRRLNTENIGLDKAGVICDERGVIPTDATMRTNVPNIYAIGDITGKWQLAHVASHQGIIAARNIAGHKEEIDYSAVPSVIFTFPEVASVGLSPTAAQQQKIPVKVTKFPFRAIGKAVAMGEADGFAAIISHETTQQILGAYVIGPHASSLISEITLAVRNELTLPCIYETIHAHPTLAEVWAESALLAVDTPLHMPPAKK lpd curated2 P09063 Dihydrolipoyl dehydrogenase; EC 1.8.1.4; Dihydrolipoamide dehydrogenase; E3 component of branched-chain alpha-keto acid dehydrogenase complex; LPD-Val MQQTIQTTLLIIGGGPGGYVAAIRAGQLGIPTVLVEGQALGGTCLNIGCIPSKALIHVAEQFHQASRFTEPSPLGISVASPRLDIGQSVAWKDGIVDRLTTGVAALLKKHGVKVVHGWAKVLDGKQVEVDGQRIQCEHLLLATGSSSVELPMLPLGGPVISSTEALAPKALPQHLVVVGGGYIGLELGIAYRKLGAQVSVVEARERILPTYDSELTAPVAESLKKLGIALHLGHSVEGYENGCLLANDGKGGQLRLEADRVLVAVGRRPRTKGFNLECLDLKMNGAAIAIDERCQTSMHNVWAIGDVAGEPMLAHRAMAQGEMVAEIIAGKARRFEPAAIAAVCFTDPEVVVVGKTPEQASQQGLDCIVAQFPFAANGRAMSLESKSGFVRVVARRDNHLILGWQAVGVAVSELSTAFAQSLEMGACLEDVAGTIHAHPTLGEAVQEAALRALGHALHI lpd curated2 P0A9P2 Dihydrolipoyl dehydrogenase; EC 1.8.1.4; Dihydrolipoamide dehydrogenase; E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes; Glycine cleavage system L protein MSTEIKTQVVVLGAGPAGYSAAFRCADLGLETVIVERYNTLGGVCLNVGCIPSKALLHVAKVIEEAKALAEHGIVFGEPKTDIDKIRTWKEKVINQLTGGLAGMAKGRKVKVVNGLGKFTGANTLEVEGENGKTVINFDNAIIAAGSRPIQLPFIPHEDPRIWDSTDALELKEVPERLLVMGGGIIGLEMGTVYHALGSQIDVVEMFDQVIPAADKDIVKVFTKRISKKFNLMLETKVTAVEAKEDGIYVTMEGKKAPAEPQRYDAVLVAIGRVPNGKNLDAGKAGVEVDDRGFIRVDKQLRTNVPHIFAIGDIVGQPMLAHKGVHEGHVAAEVIAGKKHYFDPKVIPSIAYTEPEVAWVGLTEKEAKEKGISYETATFPWAASGRAIASDCADGMTKLIFDKESHRVIGGAIVGTNGGELLGEIGLAIEMGCDAEDIALTIHAHPTLHESVGLAAEVFEGSITDLPNPKAKKK lpd curated2 P11959 Dihydrolipoyl dehydrogenase; EC 1.8.1.4; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex MVVGDFAIETETLVVGAGPGGYVAAIRAAQLGQKVTIVEKGNLGGVCLNVGCIPSKALISASHRYEQAKHSEEMGIKAENVTIDFAKVQEWKASVVKKLTGGVEGLLKGNKVEIVKGEAYFVDANTVRVVNGDSAQTYTFKNAIIATGSRPIELPNFKFSNRILDSTGALNLGEVPKSLVVIGGGYIGIELGTAYANFGTKVTILEGAGEILSGFEKQMAAIIKKRLKKKGVEVVTNALAKGAEEREDGVTVTYEANGETKTIDADYVLVTVGRRPNTDELGLEQIGIKMTNRGLIEVDQQCRTSVPNIFAIGDIVPGPALAHKASYEGKVAAEAIAGHPSAVDYVAIPAVVFSDPECASVGYFEQQAKDEGIDVIAAKFPFAANGRALALNDTDGFLKLVVRKEDGVIIGAQIIGPNASDMIAELGLAIEAGMTAEDIALTIHAHPTLGEIAMEAAEVALGTPIHIITK lpd curated2 P50970 Dihydrolipoyl dehydrogenase; EC 1.8.1.4; Dihydrolipoamide dehydrogenase; E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes MADHFDLIVLGGGPGGYVAAIRAAQLNLKVALVERVHLGGICLNWGCIPTKSLLRSAEVYHEMQNAEAYGLTSFKPDFDLDKIIARSREVATRLASGVKTLLRKNKVEVISGVGQLTGNQQMLVETTEGEEKILEAKDIIIATGARARQLPNVHSDGKHIWTYHHALKPPAMPKKLLVIGSGAIGIEFASFYADFGAEVSIVEHAPQILPMEDAEVSAYVAKAFKKRGIRILTQSALQNLTPDDEGVTAEIAGADGKVTKERFSHAIVAIGVVANVENIGLDKLGIKLDRGFIAVDGFGRTNVDHVWAIGDVAGAPCLAHKASHQGVIAAEAIAGCDHVHPLNTQNIPGCTYARPQVASVGLTEEKARQQGYNVKIGNFPFIANGKAIAQGATDGFVKTVFDADSGALLGAHMVGAEVTEMIQGYTVARTLETTEAEIMETIFPHPTLSEAMHESVLAAYGRALHF lpd curated2 P52992 Dihydrolipoyl dehydrogenase; EC 1.8.1.4; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex MSKQFDVLVIGAGPGGYIAAIRAGQLGLNVACCEGNPYDDPKGEARLGGTCLNVGCIPSKALLASSEEFENVQHHLGDHGITVGDVKVDVAKMLKRKDDIVGKMTKGIEFLFRKNKVTLLKGYGKFVGKSAEGFQVDVAGEVVTAKQVIIATGSKARHLPGIKVDNDLVSDNEGALKFPAVPKKLGVIGAGVIGLELGSVWRRLGSDVTVLEALPAFLGAADEGVAKEAQKQLTKQGLKFSLGVNVNEVTTGKNGVTVKYTDKDGKAQTLEVDRLIVSVGRVPNTDNLGLDAVGLAADQRGFIEVDDHCATKVPGLWAIGDVVRGPMLAHKAEDEGVAVAERIAGQKPHIDYNCVPWVIYTFPEIAWVGKTEAQLKAEGREYKAGQFPFMANGRALGMGHADGFVKMLADAKTDEILGVHIVAANASDLIAEAVVAMEFKAASEDIGRVCHPHPSMSEVMREAALAVDKRQLNM lpd curated2 P54533 Dihydrolipoyl dehydrogenase; EC 1.8.1.4; Dihydrolipoamide dehydrogenase; E3 component of branched-chain alpha-keto acid dehydrogenase complex; LPD-Val MATEYDVVILGGGTGGYVAAIRAAQLGLKTAVVEKEKLGGTCLHKGCIPSKALLRSAEVYRTAREADQFGVETAGVSLNFEKVQQRKQAVVDKLAAGVNHLMKKGKIDVYTGYGRILGPSIFSPLPGTISVERGNGEENDMLIPKQVIIATGSRPRMLPGLEVDGKSVLTSDEALQMEELPQSIIIVGGGVIGIEWASMLHDFGVKVTVIEYADRILPTEDLEISKEMESLLKKKGIQFITGAKVLPDTMTKTSDDISIQAEKDGETVTYSAEKMLVSIGRQANIEGIGLENTDIVTENGMISVNESCQTKESHIYAIGDVIGGLQLAHVASHEGIIAVEHFAGLNPHPLDPTLVPKCIYSSPEAASVGLTEDEAKANGHNVKIGKFPFMAIGKALVYGESDGFVKIVADRDTDDILGVHMIGPHVTDMISEAGLAKVLDATPWEVGQTIHPHPTLSEAIGEAALAADGKAIHF lpd curated2 P66005 Dihydrolipoyl dehydrogenase; EC 1.8.1.4; Dihydrolipoamide dehydrogenase; E3 component of alpha-ketoacid dehydrogenase complexes MTHYDVVVLGAGPGGYVAAIRAAQLGLSTAIVEPKYWGGVCLNVGCIPSKALLRNAELVHIFTKDAKAFGISGEVTFDYGIAYDRSRKVAEGRVAGVHFLMKKNKITEIHGYGTFADANTLLVDLNDGGTESVTFDNAIIATGSSTRLVPGTSLSANVVTYEEQILSRELPKSIIIAGAGAIGMEFGYVLKNYGVDVTIVEFLPRALPNEDADVSKEIEKQFKKLGVTILTATKVESIADGGSQVTVTVTKDGVAQELKAEKVLQAIGFAPNVEGYGLDKAGVALTDRKAIGVDDYMRTNVGHIYAIGDVNGLLQLAHVAEAQGVVAAETIAGAETLTLGDHRMLPRATFCQPNVASFGLTEQQARNEGYDVVVAKFPFTANAKAHGVGDPSGFVKLVADAKHGELLGGHLVGHDVAELLPELTLAQRWDLTASELARNVHTHPTMSEALQECFHGLVGHMINF lpd curated2 P72740 Dihydrolipoyl dehydrogenase; EC 1.8.1.4; Dihydrolipoamide dehydrogenase; LPD; E3 component of pyruvate complex MSQDFDYDLVIIGAGVGGHGAALHAVKCGLKTAIIEAKDMGGTCVNRGCIPSKALLAASGRVREMSDQDHLQQLGIQINGVTFTREAIAAHANDLVSKIQSDLTNSLTRLKVDTIRGWGKVSGPQEVTVIGDNETRILKAKEIMLCPGSVPFVPPGIEIDHKTVFTSDEAVKLETLPQWIAIIGSGYIGLEFSDVYTALGCEVTMIEALPDLMPGFDPEIAKIAERVLIKSRDIETYTGVFATKIKAGSPVEIELTDAKTKEVIDTLEVDACLVATGRIPATKNLGLETVGVETDRRGFIEVNDQMQVIKDGKPVPHLWAVGDATGKMMLAHAASGQGVVAVENICGRKTEVDYRAIPAAAFTHPEISYVGLTEAQAKELGEKEGFVVSTAKTYFKGNSKALAEKETDGIAKVVYRQDTGELLGAHIIGIHASDLIQEAAQAIADRKSVRELAFHVHAHPTLSEVLDEAYKRAV lpd curated2 P75393 Dihydrolipoyl dehydrogenase; EC 1.8.1.4; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex MNYDLIIIGAGPAGYVAAEYAGKHKLKTLVVEKEYFGGVCLNVGCIPTKTLLKRAKIVDYLRHAQDYGISINGQVALNWNQLLEQKGKVVSKLVGGVKAIIASAKAETVMGEAKVLDPNTVEVAGKTYTTKSIVVATGSRPRYLTLPGFAEARQNGFVIDSTQALSLEGVPRKLVVVGGGVIGIEFAFLYASLGSEVTILQGVDRILEIFDTEVSDLVAKLLQTKNVKIITNAQVTRANNNEVFYSQNGQEGSVVGDRILVSIGRIPNTECLDGLNLQRDERNRIVLNQDLQTSIPNIYIVGDANAQLMLAHFAYQQGRYAVNHILNKKQVKPAQKLTCPSCIYTNPEVASVGYTEMELKKQGIPYVKTNLVLAHCGKAIADNETNGFVKMMFDPQTGKILGCCIIAATASDMIAELALAMGAGLTVFDIANSISPHPTINEMIADVCKKALFDHFK lpd curated2 P85207 Dihydrolipoyl dehydrogenase; EC 1.8.1.4; Dihydrolipoamide dehydrogenase MKTYDLIVIGTGPGGYPAAIRGAQLGLKVLAVEAAEVGGVCLNVGCIPTKALLHAAETVHHLKGAEGFGLKAKPELDLKKLGAWRDGVVKKLTGGVAGLLKGNKVELLRGFARFKGPREIEVNGETYGAQSFIIATGSEPMPLKGFPFGEDVWDSTRALRVEEGIPKRLLVIGGGAVGLELGQIYHRLGSEVTLIEYMPEILPAGDRETAALLRKALEKEGLKVRTGTKAVGYEKKQDGLHVLLEAAQGGSQEEIVVDKILVAVGRRPRTEGLGLEKAGVKVDERGFIQVNARMETSAPGVYAIGDVARPPLLAHKAMKEGLVAAENAAGKNALFDFQVPSVVYTGPEWAGVGLTEEEARKAGYNVKVGKFPFSASGRALTLGGAEGLIKVVGDAETDLLLGVFVVGPQAGELIAEATLALEMGATVSDLGLTIHPHPTLSEGLMEAAEALHKQAIHILNR lpd curated2 P95596 Dihydrolipoyl dehydrogenase; EC 1.8.1.4; Dihydrolipoamide dehydrogenase; E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes MAEFDVIIIGGGPGGYVCAIRCAQLGLKTACVEGRGALGGTCLNVGCIPSKALLHATHELHEVHENFEKMGLMGAKVKVDWAKIDGNTKGIEFLFKKNKVTYLRGWGSIPAPGQVKVGDEVHTAKNIVIATGSESSGLPGIEIDEQTVVTSTGALSLAKVPKSMVVIGAGVIGLELGSVYARLGAEVTVVEYLDAITPGMDAEVAKGLQRILTRQGLKFVLGAAVQGVDKAKGKNTVRYTLRKDESAHAIEAEVVLVATGRKPFTKGLGLEALGVEMLPRGQVKADSHWATNVPGLYAIGDAIVGPMLAHKAEDEGMAVAEVIAGKHGHVNYDVIPGVIYTTPEVAAVGKTEDALKQEGRAYKVGKFSFMGNGRAKAVFQAEGFVKILADAATDRILGAHIIGPSAGDMIHEICVAMEFGASAQDLALTCHAHPTYSEAVREAALACGDGAIHA lpd curated2 Q5UWH2 Dihydrolipoyl dehydrogenase 3; EC 1.8.1.4; Dihydrolipoamide dehydrogenase 3 MVVGDVTTSTDVLVIGAGPGGYVAAIRAAQLALDVTLVEKGEYGGACLNRGCIPSKALIHGSKLASEAGQAEELGIYADPTVALDEMINWKDGVVDQLTSGIEQLCTAAGVNLLKGTAEFADENKVRIIHQGEGQGSESLKFENCIIATGSRPIEIPGFGFEDERIVSSDGALNFDTVPDELVIVGAGYIGMELATVYSRLGSDVSVIEMLEQALPSYEEDIASIVRKRAERLGVDFHFGYTADSWAASDGKAVLTAVPADEAAHDSDIELTADRILVAVGRRPVTDTLSIDDAGVETNAQGFIPTDSTCRTNKEHIFAVGDVAGEPMLAHKGSKEGEVAAEVIAGEPAAVDYQALPAAVFTDPEIGTVGLTENEAANKGMTPVTGEFQFQASGRALTANRAEGFVRIIATKETERVIGAQIVGPEASELIAEIAAMIEMGAKLEDIGSTVHTHPTLSEAIMEAAQNAREKAIHRRN lpd curated2 Q5UYG6 Dihydrolipoyl dehydrogenase 2; EC 1.8.1.4; Dihydrolipoamide dehydrogenase 2 MVVGDVTTGTELLVIGGGPGGYVAAIRGAQLGLDTTLVERDAYGGTCLNHGCIPSKALISASDVAHDARQAESMGVFADPAVDMAGMTEWKDGVVTRLTRGVESLCKNAGVNLVEGTAEFVDDGTVRVAHGGEGQGSESLSFEHAIVATGSRPMAVPGFEFDGEHILSSKDALALESVPEKLLVVGAGYIGMELSTVFAKLGAEVTVVEMLDDVLPGYEDDIATVVRDRAEELGIDFNFGEAADNWEETDEGIRVQTVDEDEVVTEYNAEKCLVAVGREPVTDTLALDNIDLQTDENGVIPTDDQCRTAFESVFAVGDVAGEPMLAHKAMAEGEVAARAAAGEPAAFDHQAIPAAVFTDPEIATVGMTESEAEAAGFEPVIGQMPVRANGRALTVNEKEGFVRVVADADEEFLLGAQIVGPEASELIAELGLGIEMGARLEDIAGTIHTHPTLSEAVHEAAAAARGEAVHTR lpd curated2 Q89AQ8 Dihydrolipoyl dehydrogenase; EC 1.8.1.4; Dihydrolipoamide dehydrogenase; E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes MISKKVDTQVVIIGSGPSGYSAAFRCSDLGLNVVLIEQYYSLGGVCLNVGCIPSKYLLHIAKVIKDVKKLSRIGISFEKLDINLKEIQCNQKKIIESFSSGISNLARKRNVRIIFGYAKFLDANSIFVQGEHDSYVVSFNKIVIATGSLSKKLSYIPYDDIRIWNSSFAVSIPSIPKKLLIIGGGIIGLEMATIYSALGSNVDIIDNSHDILPHLDRDVIDIFKRSVNHDYNIFFNSNVIKIVQEKNGLLVHIAENDNKNKRFELYDIILVAIGRVPNTDMLDISKVGLKTDNNGFIKVNEQFCTNIPNIYAIGDVIGQPMLAHKGTHEGHIVAEVISGKKHYFNPFVIPCVSYTEPEIAWVGITENEARKNNINYEVSSVLWNTLGRAVSSQCSEGVTKLIFDKKTNKIIGGCIVGSNAGELLGEISLAIEMGCDAEDLALTIHAHPTLYESINLSAQIFQGTITDLINKKIKK lpd curated2 Q8K9T7 Dihydrolipoyl dehydrogenase; EC 1.8.1.4; Dihydrolipoamide dehydrogenase; E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes MHQEIQSEVVIIGSGPAGYSAAFRCADLGLETVLIEHQERLGGVCLNVGCIPSKSLLHIAKIIKDASELSESGVFFNKPIIDIKKINNWKEKIIKKLTTGLSNMGEKRKVRIVQGKALFNTDHSVLVKNKKNDFTIFFKHAIIATGSKPIKIPSLPNEDNRIWNSTDALSLKSIPNRFLIIGGGIIGLEMATIYSALGSKVDIVDRFNAFLPSVDKDITDIYIKSIKKRFKLLLNTHVKSVEKSKDNDLIVKIAEENSDENVCCYDNILVAIGRSPNVDFLGLEKIGLKLNESGFIEINQQLKTNISHIYAIGDVTGFPMLAHKAVQQAHIAAEVISGKKHYFEPKVIPSVAYTDPEIAWVGLSEKEAENNDIDYEVSLFPWSASGRAHASNCTLGMTKLIFNKNTNKIIGGSIIGTNASELISEIGLAIEMGSDAEDISLTIHPHPTLSESISLASEVFQGTITDLLNLKKSLLN lpd curated2 Q8KCW2 Dihydrolipoyl dehydrogenase; EC 1.8.1.4; Dihydrolipoamide dehydrogenase; E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes MQQADTLAAQFDVAVIGSGPGGYEAAIHAARYGLKTCIVEKAVLGGVCVNWGCIPTKALLRSAEVFDLAKNPETFGVNVGNVSFDLAQAVKRSRNVALKSSKGVAYLLKKAAVEVLAGEAVLTGGAGVMVTMPDGSVRMLGAKNIIVATGSTPRVIPGLEPDGKKIITSREALILKEVPKSMIVVGGGAIGVEMAWFYAKAGSKVTIVELMPRMLPAEEAEVSEALKRSFEKAGITVHCGAKLDNVAVSESGVSAELVVEGSAPQTLNASCLLVAVGVTGAIDGLGLDAVGVETERGFIRTDGQCRTSAPGIYAIGDVRGGMLLAHKASAEAAIAVEAIAGKSPEPLSEPLIPRCVYAQPSVASVGLTEEAAVNAGYQVAVGRSQFAASGKANAYGQLEGFVKLVFDAATGKMLGGHLIGHDAVELIGELGLACRYGVTAGGLVNTVHAHPTLSETVREAAFDALQSMG lpd curated2 Q8NTE1 Dihydrolipoyl dehydrogenase; LPD; EC 1.8.1.4; Dihydrolipoamide dehydrogenase; E3 component of alpha-ketoacid dehydrogenase complexes MTEHYDVVVLGAGPGGYVSAIRAAQLGKKVAVIEKQYWGGVCLNVGCIPSKSLIKNAEVAHTFTHEKKTFGINGEVTFNYEDAHKRSRGVSDKIVGGVHYLMKKNKIIEIHGLGNFKDAKTLEVTDGKDAGKTITFDDCIIATGSVVNTLRGVDFSENVVSFEEQILNPVAPKKMVIVGAGAIGMEFAYVLGNYGVDVTVIEFMDRVLPNEDAEVSKVIAKAYKKMGVKLLPGHATTAVRDNGDFVEVDYQKKGSDKTETLTVDRVMVSVGFRPRVEGFGLENTGVKLTERGAIEIDDYMRTNVDGIYAIGDVTAKLQLAHVAEAQGIVAAETIAGAETQTLGDYMMMPRATFCNPQVSSFGYTEEQAKEKWPDREIKVASFPFSANGKAVGLAETDGFAKIVADAEFGELLGAHLVGANASELINELVLAQNWDLTTEEISRSVHIHPTLSEAVKEAAHGISGHMINF lpd curated2 Q9HUY1 Dihydrolipoyl dehydrogenase 3; EC 1.8.1.4; Dihydrolipoamide dehydrogenase 3; LPD-3 MMESYDVIVIGAGPGGYNAAIRAGQLGLKVACVEGRETLGGTCLNVGCMPSKALLHASELYAAASGGEFARLGIRVSPELDLAQMMKQKDESVAALTRGVEFLFRKHKVQWIKGWARLQGEGRVGVALADGGHAQLEARDIVIATGSEPAPLPGVPVDNQRILDSTGALELVEVPRHLVVIGAGVIGLELGSVWRRLGAQVTVLEYLERICPGLDGETARTLQRALTRQGMRFRLGTRVVAARSGEQGVELDLQPAAGGATESLQADYVLVAIGRRPYTEGLGLETVGLASDRRGMLENQGQRSAAPGVWVIGDVTSGPMLAHKAEEEAIVCIERIAGHAAEMNAEVIPSVIYTQPEVASVGLGEEQLQAARREYKVGRFPFSANSRAKINHESEGFIKILSDARSDQVLGVHMIGPGVSEMIGEACVAMEFSASAEDLALTCHPHPTRSEALRQAAMDVHGRAMQN lpd curated2 Q9I3D1 Dihydrolipoyl dehydrogenase; EC 1.8.1.4; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; Glycine oxidation system L-factor; LPD-GLC MSQKFDVVVIGAGPGGYVAAIRAAQLGLKTACIEKYIGKEGKVALGGTCLNVGCIPSKALLDSSYKYHEAKEAFKVHGIEAKGVTIDVPAMVARKANIVKNLTGGIATLFKANGVTSFEGHGKLLANKQVEVTGLDGKTQVLEAENVIIASGSRPVEIPPAPLTDDIIVDSTGALEFQAVPKKLGVIGAGVIGLELGSVWARLGAEVTVLEALDKFLPAADEQIAKEALKVLTKQGLNIRLGARVTASEVKKKQVTVTFTDANGEQKETFDKLIVAVGRRPVTTDLLAADSGVTLDERGFIYVDDHCKTSVPGVFAIGDVVRGAMLAHKASEEGVMVAERIAGHKAQMNYDLIPSVIYTHPEIAWVGKTEQTLKAEGVEVNVGTFPFAASGRAMAANDTTGLVKVIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGMMVFSHPTLSEALHEAALAVNGHAIHIANRKKR natA curated TCDB::Q55164 NatA aka BRAF aka SLR0467, component of Leucine/proline/alanine/serine/glycine (and possibly histidine) porter, NatABCDE MSDRITPAENLGSPESSLLLAQGLSKSFGGLRAVDHADIVVKEGSITGLIGPNGAGKTTLFNLLSNFIRPDQGEVLFNGDSIGQLAPHQIALRGSVRTFQVAKVLSRLTVLENMLLADQHQTGEKFLPRLINFRRVQKEERANREKAMAMLESVGLGAKAQDYAGALSGGQRKLLEMARALMSNPKLILLDEPAAGVNPTLIGQICEHIVNWNRQGITFLVIEHNMDVIMTLCHHVWVLAEGRNLADGTPEQIQSDPRVLEAYLGDS natA curated TCDB::Q7A2H0 NatA, component of The neutral amino acid permease, N-1 (transports pro, phe, leu, gly, ala, ser, gln and his, but gln and his are not transported via NatB) MVNNQSPPLPLLAASGLCKSFGGIKAVQEARIEVAQGSITGLIGPNGAGKTTLFNLLSNFIRPDKGRVIFDGEPIQQLQPHQIAQQGMVRTFQVARTLSRLSVLENMLLAAQKQTGENFWQVQLQPQVVVKEEKQLQEQAMFLLESVGLAKKAYEYAGGLSGGQRKLLEMGRALMTNPKLILLDEPAAGVNPRLIDDICDRILTWNRQDGMTFLIIEHNMDVIMSLCDRVWVLAEGQNLADGTPAEIQTNSQVLEAYLGK natB curated TCDB::Q55387 NatB aka SLR0559, component of Leucine/proline/alanine/serine/glycine (and possibly histidine) porter, NatABCDE MNNLVGDFFRMRLFWPQSRRRLTAIALNLALAGTTAGLMFACAEPEPTPGDGASQPSTGGEGGALKLGALLPATGDLSSIGQNMPLAVQLAVDTINACGGVNGQDVTVVIEDDQTDPTAGVSAMTKLAEADQVAGVVGSFASSVSSAAVPIAVRNNIMMISPGSTSPVFTDQAKKGEFKGFWARTAPPDTYQAQALAALAKKQGFTDAATVVINNDYGVGFEKVFVESFTADGGNVTNKDNPVRYDPKAATLDTEAAQGFANSPDAVAAILYADTGSVLVQSAYRQGLMDGVTLLLTDGVYSPDFVEKVGKDANGVSLLSGALGTVPGADGKSLEAFTAQWKDATGGKDVTAFVPHTYDATVLMMLAAEAAKSNTGAGIQSKIRDVSNGPGEEVTDACEAIAMVREGKDINYQGASGNVDIDENGDVVGTYDVWTVKGDGTLEVIDKVTPGSGS natB curated TCDB::Q8YVY4 NatB, component of The neutral amino acid permease, N-1 (transports pro, phe, leu, gly, ala, ser, gln and his, but gln and his are not transported via NatB) MQRISAALSLGLATFTAGFLLAACETSNTTPNGAANNGATSTPATDTTATSGGSGLKIGSLLPATGDLASIGQQMAAAVPLVVETVNACGGVNGQPVSLVAVDDQTDPKAGAAGMTKLATVDKVAGVVGSFASSVSTAAVSIAAQNKVLLISPGSTSPVFTEKAQKGDFNGFWARTVPPDSYQGPALAELANKKGFKRVSTIVINNDYGVGFEKAFVQAFEKLGGTVVNKNNPVRYDPKATTFETEAAAAFAGKPDAVLGVFYVETGSLLLKSAYQQGVAQGVQIMLTDGMKSDEFPAQVGKTADGKFIASGIIGTVPGSDGKGLEALTKLWQSKKGSAPGEFAPQAWDATALLVLAAQAAKENTGVGIAGKIRDVSSAPGVEVTDVCEGLKLLQEGKDINYQGASGNVDIDANGDVIGVYDVWTVGDDGKIKTIDKVTPK natC curated TCDB::P74455 NatC aka SLL0146, component of Leucine/proline/alanine/serine/glycine (and possibly histidine) porter, NatABCDE MNFGYLIFLITSAATYGIFALGLNLQWGFAGLINFGHVAFMTLGAYATTLLSLRGLPIPLAVLVGMGLAMALGLLIGTSTLRLREDYLAIVTIGVSELIRLIANNEEWLTQGTFGVQSFPWPMDFNPTLLSRIVFVIWLTVLTIYAESILIKSLLKQWKEGKKIQGKSYQPRKPLALLIWGIITTALILTAYVPGVVSLYNYSGKAGLMLLALTLLALTYAGLEFWVHSPWGRILKAIREDEEIPRALGKNVFWYKLQAFMGGGAIAGLAGALFAWQLTSIYPSNFDTLLTFNAWIIVVLGGAGSNAGTVLGTIIFWAYDSLTRFLLPQIAFLDQSQAGALRVMVIGLILMVLMVWRPQGILGKKEELTLGR natC curated TCDB::Q8YY08 NatC, component of The neutral amino acid permease, N-1 (transports pro, phe, leu, gly, ala, ser, gln and his, but gln and his are not transported via NatB) MIEYLIFLAISTATFALFSLGLNLQWGFTGLINFGHIAFMTLGAYTTVLLSLKGVPLFISAIVGAIFAALLGLVIGFATLRLREDYLAIVTIGTGELIRLVVNNQDLPVGDTWVSGAFGVQSYPIPLSTEPNLFFRLLMIGILTLLFAVTVFSLWRWIRNAQKLQLTDATDKTSSKQEIASRFGVGIILGLLATAIYISGVITLYNYIPKAGLMLVSLLVLAFVFWRLEYLVRSPWGRVLKAIREDEEIPKAMGKNVFWYKLQSLMLGGAIAGIAGAFFAWQISAIYPDNFQPQLTFDSWIMVILGGAGNNIGSILGAVIYFAYDAITREVLPKIIPLDEARLGAFRIMCIGLILMVLMIWRPQGILGKKEELTLGK natD curated TCDB::P74318 NatD aka LivH aka SLR0949, component of Leucine/proline/alanine/serine/glycine (and possibly histidine) porter, NatABCDE MDLSQLIFNGIAVGSIIALGAVGLTLTYGILRLSNFAHGDFMTLAAYLTWWANTSGINLWLSMALGCVGTIIAMFIGEWLLWKPMRARRATATTLIIISIGLALFLRNGILLIWGGNNQNYRVPIVPAQDFMGIKFEYYRLLVIAMAIAAMVVLHLILQRTKVGKAMRAVADNVDLAKVSGINVEWVVMWTWVMTAVLTALGGSMYGLMTTLKPNMGWFLILPMFASVILGGIGNPYGAIAGGIIIGVAQEVSVPWFGTSYKMGVALLLMIIILFIRPQGLFKGTQ natD curated TCDB::Q8YXD0 NatD, component of The neutral amino acid permease, N-1 (transports pro, phe, leu, gly, ala, ser, gln and his, but gln and his are not transported via NatB) MDIQTIQLIVNGIAVGSIIALAAVGLTLTYGILRLSNFAHGDFLTLGAYLTFFVNTFGVNIWLSMIVAVVGTVGVMLLSEKLLWSRMRSIRANSTTLIIISIGLALFLRNGIILIWGGRNQNYNLPITPALDIFGVKVPQNQLLVLALAVLSIGALHYLLQNTKIGKAMRAVADDLDLAKVSGIDVEQVIFWTWLIAGTVTSLGGSMYGLITAVRPNMGWFLILPLFASVILGGIGNPYGAIAAAFIIGIVQEVSTPFLGSQYKQGVALLIMILVLLIRPKGLFKGTM natE curated TCDB::P73650 NatE aka LivF aka SLR1881, component of Leucine/proline/alanine/serine/glycine (and possibly histidine) porter, NatABCDE MSDLLVVKDVFAGYVADVPILQGINFSIAPGELVTVIGPNGAGKSTLAKTIFGLLTPSQGEIIFKGENITGLGSDQIVRRGMCYVPQVCNVFGSLTVAENLDMGAFLHQGPTQTLKDRIYTMFPKLAQRRNQRAGTLSGGERQMLAMGRALMLDPDLLLLDEPSAALSPILVKDVFAQIKAINATGKAIILVEQNAKQALMMADRGYVLENGRDKLEGSGQSLLNDPLVGELYLGAAYHN natE curated TCDB::Q8YT15 NatE, component of The neutral amino acid permease, N-1 (transports pro, phe, leu, gly, ala, ser, gln and his, but gln and his are not transported via NatB) MSGSAQNFTPLLEVENVHAGYIKDVDILQGVNFRVESGELVTVIGPNGAGKSTLAKTIFGLLTPHTGKITFKGKNIAGLKSNQIVRLGMCYVPQIANVFPSLSVEENLEMGAFIRNDSLQPLKDKIFAMFPRLSDRRRQRAGTLSGGERQMLAMGKALMLEPSLLVLDEPSAALSPILVTQVFEQVKQINQEGTAIILVEQNARKALEMADRGYVLESGRDAISGPGQELLTDPKVAELYLGAGKGH ofo curated reanno::Cup4G11:RR42_RS19540 3-methyl-2-oxobutanoate:ferredoxin oxidoreductase (EC 1.2.7.7) MNAPLTPPVSDAIRRALANVSLEDKYTLERGRVYISGTQALVRLPMLQRERDRAAGLNTAGFISGYRGSPLGALDQSLWKAKQHLAAHDIVFQAGLNEDLAATSVWGSQQVNMYPDARFEGVFGMWYGKGPGVDRTSDVFKHANSAGSSRHGGVLVLAGDDHAAKSSTLAHQSEHIFKACGLPVLYPSNVQEYLDYGLHAWAMSRYSGLWVSMKCVTDVVESSASVELDPHRVEIVLPQDFILPPGGLNIRWPDPPLEQEARLLDYKWYAGLAYVRANKIDRIEIDSPHARFGIMTGGKAYLDTRQALANLGLDDETCARIGIRLYKVGCVWPLEAHGARAFAEGLQEILVVEEKRQIMEYALKEELYNWRDDVRPKVYGKFDEKDNAGGEWSIPQSNWLLPAHYELSPAIIARAIATRLDKFELPADVRARIAARIAVIEAKEKAMAVPRVAAERKPWFCSGCPHNTSTNVPEGSRALAGIGCHYMTVWMDRSTSTFSQMGGEGVAWIGQAPFAGDKHVFANLGDGTYFHSGLLAIRASIAAGVNITYKILYNDAVAMTGGQPIDGKLSVQDVANQVAAEGARKIVVVTDEPEKYSAAIKLPQGVEVHHRDELDRIQRELREVPGATILIYDQTCATEKRRRRKRGTYPDPAKRAFINDAVCEGCGDCSVKSNCLSVEPLETELGTKRQINQSSCNKDFSCVNGFCPSFVTAEGAQVKKPERHGVSMDNLPALPQPALPGLEHPYGVLVTGVGGTGVVTIGGLLGMAAHLENKGVTVLDMAGLAQKGGAVLSHVQIAAHPDQLHATRIAMGEADLVIGCDAIVSAIDDVISKTQVGRTRAIVNTAQTPTAEFIKNPKWQFPGLSAEQDVRNAVGEACDFINASGLAVALIGDAIFTNPLVLGYAWQKGWLPLSLDALVRAIELNGTAVEKNKAAFDWGRHMAHDPEHVLSLTGKLRNTAEGAEVVKLPTSSGALLEKLIAHRAEHLTAYQDAAYAQTFRDTVSRVRAAESALVGNGKPLPLTEAAARNLSKLMAYKDEYEVARLYTDPIFLDKLRNQFEGEPGRDYQLNFWLAPPLMAKRDEKGHLVKRRFGPSTMKLFGVLAKLKGLRGGVFDVFGKTAERRTERALIGEYRALLEELTRGLSAANHATAITLASLPDDIRGFGHVKDDNLAKVRTRWTALLEQFRHPETAQRVA ofo curated reanno::psRCH2:GFF3452 branched-chain ketoacid ferredoxin reductase (EC 1.2.7.7) active on 4-methyl-2-oxopentanoate, (S)-3-methyl-2-oxopentanoate, or 3-methyl-2-oxobutanoate MSLAEIRLDDKYRLATGHLYLTGTQALTRLPMLQHQRDQARGLNTGGFISGYRGSPLGGLDKSLWEARDYLKQHAIHFQPGVNEELAATAVWGSQQTNLFPGAKYDGVFAMWYGKGPGVDRAGDVFKHANAAGVSPQGGVLLLAGDDHGCKSSTLPHQSEHAFIAASIPVLNPANVQEILDYGIIGWELSRYSGCWVALKTIAENVDSSAVVEVDPLRVQTRIPEDFELPEDGVHIRWPDPPLAQEKRLNLYKIYAARAFARANNLNRVMLDSPNPRLGIITTGKSYLDVRQALDDLGLDEALCASVGLRVLKVGMSWPLEPVSVHEFAQGLDEILVVEEKRSIIEDQLTGQLYNWPVSKRPRVVGEFDEQGNSLLPNLSELTPAMIARVIAKRLAPIYTSDSIQARLAFLAAKEKALAARSYSTVRTPHYCSGCPHNSSTKVPEGSRASAGIGCHYMVQWMDRRTETFTQMGGEGVNWIGQAPFTDTPHMFQNLGDGTYFHSGSLAVRAAVAAGVNVTYKILYNDAVAMTGGQPIDGELRVDQLSRQIFHEGVKRIALVSDEPDKYPSRDTFAPITSFHHRRELDAVQRELREFKGVSVIIYDQTCATEKRRRRKRGKMEDPAKRAFINPAVCEGCGDCGEKSNCLAVLPLETELGRKREIDQNACNKDFSCVEGFCPSFVTVHGGGLRKPEAVAGGIEAATLPEPQHPTLDRPWNVLIPGVGGSGVTTLGALLGMAAHLEGKGCTVLDQAGLAQKFGPVTTHVRIAAKQSDIYAVRIAAGEADLLLGCDLIVAAGDESLTRLNEQISNAVVNSHESATAEFTRNPDAQVPGAAMRQAISDAVGADKTHFVDATRLATRLLGDSIATNLFLLGFAYQQGLLPISAEAIEKAIELNGVSAKLNLQAFRWGRRAVLEREAVEQLARPVDMVEPICKTLEEIVDWRVDFLTRYQSAGLARRYRQLVERVRDADSADDLALSKAVARYYFKLLAYKDEYEVARLYSEPEFRQQLEAQFEGDYKLQFHLAPAWLAKRDPVTGEPRKRELGPWVLNLFGVLAKFRFLRGTPLDPFGYGHDRRVERQLISEYEKTVDELLAQLKPTNYRTAVAIAALPEQIRGYGPVKERSIAKARQQEKLLREQLAKGDEVQSVRLFQPAA ofo ignore SwissProt::A0A0E3JT70 2-oxoacid:ferredoxin oxidoreductase subunit alpha; OFOR; EC 1.2.7.11 MRISWMIGGAQGSGVDTSANIFGNAVAASGYYIYGNREYYSNIKGRHSYFNLTISDKPPRSIAQQIEILTSFDAETIFQHFNEVKDVLIYSTEVENTKAEQVQSMEPEITEHVVKFLKEKGYGTTVKDVINYLKKEKGVKVIPIDYMEILKKVADQAKVQLSVADRARNTIAIAASYKLLGLKEQYLINSITRTFRQEVFAKINTIAAQLAMQQIQPMYNLPELPNNEEKINLDGNTAAAIGKIYGGLRFQSYYPITPASDESVFIEAHQTVFTVDPKTGEKRKSTIVVVQAEDELAAINMASGAALTGVRAATATSGPGFSLMVEGMGWAGMNEVPVVITYYIRGGPSTGQPTRTSQADLMFALNAGHGEFPRIVIASGDHVEAFHDGTWALNLAQKYQTPVIHLVDKALANSYSIIPKKTLGMENIRIEKGKIVINTNTPELKRFEITEDGISPFAPLGTARVHYTGDEHDEYGFIAEASENREKMYEKRIKKLMTADKEIPEESRVNVYGNTDSKVAIITWGSPKGAILDAMEELENEGIKPMLIQIRMFSPFPKNLMRKLLNGKEFIIDVESNYFGQAGEVLKLNTGIEPTHYILKWNGRPMMRDEVKEGIKAVVQKGERRVVLHGGA ofo ignore SwissProt::A0A0E3KBH3 2-oxoacid:ferredoxin oxidoreductase subunit beta; OFOR; EC 1.2.7.11 MAGLKVEWNDWCPGCGNFGILSAEQQAIQELGLDPKKVVLVSGIGCSGKIPHFIRLPASGVHTLHGRALTFAIGIKLANPSLEVIVNGGDGDQLGIGVGHFVSAGRRNVDLTVIVHNNGVYGLTKGQASPTLKLGVKTKSLPKPNINSDINPIALAISSGYTFVARGYAYDVKHLKEIIKKAIKHKGLAMIDVLQPCPTYNDIHTKEYYDKRVYKLDEDPSWDPIVKKPEEMDDKMSKAILKSMEWGDRTPIGIFYQNELVSTYEQRIAERSPSYLDNPPAHDVIEFEGKPTTDVEDILKERRVT ofo ignore SwissProt::B6D9A7 Ketoisovalerate reductase; KIVR; EC 1.2.7.7 MPSPEHPSWLSTLLADTRPPPKLFAWSPANLDSPTAVKPDRADRGDFDPGKYPVDAPITTASEPVKRIYIVGPGNVGRLYASYMSRQRDALPITLVVHRKELLSQWVTSEGVVLADRGGKVTKNKQFDVEWWTESRPRYGPVREVADGEKLHNVFISTKADAGLGEADRLRRYLGRCSSVVFAQNGVSKLWAPYGPLYVASRYHADDAPSFSACVVNHGISAAGLFYSIHTSPSDAFIGPIFKGSAAPAHGQNKRRRLDDDFFTTYISSTPFLDTKHVSSGQLWIIQLEKLVLNAAINPLTTLLRCKTGQLFASYDSHDALTRVLDQLLWQASAVIQALINHDANIDMLTSYAETVHRLVPGSDDYGRNFANIRRKLTVRFSQPILKAKLYAFGLNIREHRSSMLQDAEAGRKTEIRDVNGWIVDMAEYLGLDLDVGIHRGLIELIEECVVLDKEELARRLL ofo ignore SwissProt::G3GBU6 Ketoisovalerate reductase BEA2; KIVR; EC 1.2.7.7 MTSQEHPNWLTALLVDTRPPPKLFAWSPANIQPKLDEGIDMGSSNSDEEYDNDACVCQSTDSDQRIYIIGPGNIGRLYATHMARHPNALPITLVVHRKELLSQWVACEGVGLADITSGKLFLNKGFTVEWWTETRPPYGPVKEVADGKKLHNVFISTKAEAGLAEADRIRRYLGRCSSVVFAQNGVCKLWPPHGPLYISHRYPSGDTPTFSACVVSHGVASAGPFLSVHAAPADAYIGPVFWASDPESPWRHPSDDFFIRHIATTPHVNTKQVSSGEIWLLQLEKLVMNAAINPLTALLRCKTGELFTSYGSDDPLALVIDKLLWQTSAVIQGLVDHKTSHSVITSYAEHMSQPGTSCSVPKVRKKLMERFSQPILKAKLGWEEDRDTGL ofo ignore SwissProt::P72578,BRENDA::P72578,metacyc::MONOMER-11911 2-oxoacid:ferredoxin oxidoreductase subunit alpha; OFOR; EC 1.2.7.11;; 2-oxoacid oxidoreductase (ferredoxin) (subunit 2/2) (EC 1.2.7.11);; 2-oxoacid:ferredoxin oxidoreductase α subunit (EC 1.2.7.11; EC 1.2.7.1; EC 1.2.7.3; EC 1.2.7.7) MRLSWVIGGAQGTGIDTAANIFGNAVASAGYYIYGNREYYSNIKGGHSYFSLTISDKRVRSNTQKIDILVSFDAETVFQHFYDVKDILIYNKAVETTKIDAVQSMEPELAERIKDFLTKQGYETTVKGALEYASKNNVTLIPVNYDEIAKKVADEMKVPLSVTERVKNIVGITISYKLLGLDVNYLIEAINSTFKQDLYRKMNELAVKDSYDIVESRYNLKPSSKERRRFWLDGNTAVAIGKIYGGVRFQSYYPITPASDESVYIEAHQDVLMEDPITGDKKKGTIVVVQAEDELAAINMAIGAALTGVRAATATSGPGFSLMVEGLGWAGMNEVPVVITYYIRGGPSTGLPTRTAQSDLIFPIFAGHGEFPKIVLASGDHAEAFKDAIWALNLAEKYQTPVIHLVEKTLANSYSTIPYEELELDKLKAERGKIVESGDISYKRFKFTEDGISPRAFLGKATMYYTGDEHNEEGHISEDVVNRTMMYEKRMKKLEVADKEIPEESRVKIYGDLNSRNLIITWGSPTGVLRDILEESNFDFTLLQIRMFSPFPKNLVSKLMEGRDKIITVEGNYLAQTSLLVKMYTGKDVTNSILKWNGRPFLRDELEEALIKVIKDGEKRVVLNGGIYTSME ofo ignore SwissProt::P72579,BRENDA::P72579,metacyc::MONOMER-11912 2-oxoacid:ferredoxin oxidoreductase subunit beta; OFOR; EC 1.2.7.11;; 2-oxoacid oxidoreductase (ferredoxin) (subunit 1/2) (EC 1.2.7.11);; 2-oxoacid:ferredoxin oxidoreductase β subunit (EC 1.2.7.11; EC 1.2.7.1; EC 1.2.7.3; EC 1.2.7.7) MAAFTPQWNDWCPGCGNFGILNAEQQAIVELGVDTKNVVVVSGIGCSGKIPHFFRTPISGVHTLHGRAIAFATGIKLSNPDLVVIVNGGDGDLLGIGAGHFVAAGRRNVDMVVILHDNGVYGLTKGQASPTLKRGEKPKSLPRPNINDAVNPIALAISSGYTFVARGYAYDVKHLKELIKSAIKHKGLALIDVLQPCPTYNDINTKEWYDKRIYKLDTLPDWDPVVKKPEEVNEKIKRAIDKSLEWGDRIPIGIFYQNELVPSYEERIKANSPAYLDYTPAKQLIEKEGKLTTIIDPLLKEREVD ofo ignore SwissProt::P80908 Ketoisovalerate oxidoreductase subunit VorB; VOR; 2-oxoisovalerate ferredoxin reductase subunit beta; 2-oxoisovalerate oxidoreductase beta chain; EC 1.2.7.7 MATQMVKGNTAVIIGAMYAGCDCYFGYPITPASEILHEASRYFPLVGRKFVQAESEEAAINMVYGAAAAGHRVMTASSGPGMSLKQEGISFLAGAELPAVIVDVMRAGPGLGNIGPEQADYNQLVKGGGHGNYRNIVLAPNSVQEMCDLTMDAFELADKYRNPVIILADAVLGQMAEPLRFPERAVEHRPDTSWAVCGSRETMKNLVTSIFLDFDELEEFNFYLQEKYAAVEENEVRYEEYMVEDAEIVLVAYGISSRVAKSAVDTARADGIKVGLLRPITLFPFPSERIRELAEGGCTFISVEMSSGQMREDIKMASGCRDVELVNRMGGNLIELRDILRKIREIAGESND ofo ignore SwissProt::P80909 Ketoisovalerate oxidoreductase subunit VorC; VOR; 2-oxoisovalerate ferredoxin reductase subunit gamma; 2-oxoisovalerate oxidoreductase gamma chain; EC 1.2.7.7 MKKAYPVINRVECKACERCIIACPRKVLYMSNKINERGYHYVEYRGEGCNGCGNCYYTCPEINAIEVHIERCEDGDTDG ofo ignore SwissProt::Q96XT2,BRENDA::Q96XT2 2-oxoacid:ferredoxin oxidoreductase 2, subunit alpha; OFOR2; EC 1.2.7.11;; 2-oxoacid oxidoreductase (ferredoxin) (subunit 2/2) (EC 1.2.7.11) MTRIVWMIGGAQGLGVDTSANIFGNAVAKAGYYLFGNREYYSNIKGRHSYFEVVISEKPIRSLSSYVNILASFDAETVFQHFTETKEYLIYNVEYENTTVDLVKSMEPEMAEQVKEALSKERLGFTIKDVLEYLKRRGVKVIGFNYTELIKKIADTFKVPMSVVERAKNMIAVGASYGLLGLKFDYLKDAISSTFKNELFIKFNTMAAELGYNSVPNVYKLQEYKIEKQRIQVDGNTISAMGKLAGGLRFQSYYPITPASDESVYIEANQNLDMIVEGNELRKGGVVVVQAEDELAAINMAVGAALTGVRSATATSGPGFSLMSEGISWAGMNEVPVVITYYMRGAPATGLPTRSGQADLKFALNVGHGEFPRIVIASGDHVEIFWDAIWALNLAEKYQTPVIHIIEKTLANAYSVFEEELITNRPYVIERGKIVKPTSDYFNRFEVTEDGISPRVFLGQASIFYTGDEHNEEGHITENSINRMKMYEKRNKKLETADKEIPEEQRVNIVGDADIVLLTWGSPKGAILDAMEELSKDGIKTMMVQVKMFNPYPKNLMKKILSGKSKIIAVENNYNAQGAEVLAEKTGIFATNYILKWTGRPITREEVIEGIKKILERDEKRVVLYGGA ofo ignore SwissProt::Q96XT4,BRENDA::Q96XT4 2-oxoacid:ferredoxin oxidoreductase 2, subunit beta; OFOR2; EC 1.2.7.11;; 2-oxoacid oxidoreductase (ferredoxin) (subunit 1/2) (EC 1.2.7.11) MVERKPVFVDWCPGCGDFGILRAEEMAIRELGINPKSVVIVSGIGCSGKIPHFMNLPISGVHTLHGRSIAFATGIKLSNPSLEVIVNVGDGDGLGIGMGHFVHLGRRNIDIAVLVHNNGVYGLTKGQASPTLHRGEKTKSLPKPNIMDAVNPLAVALAAGYTFVARGYAYDVMHLKELIKKAILHKGSALVDILQPCPTYNDINTKEWYDKRVYKLDNVPGWDPVVRKEEEAQKKFEQAIMKSYEWGEKIPIGIFYQNELVPTFEDRLTSNIPNYREYYPAKQQIEINGISTTKIDELIKAKRI ofo ignore SwissProt::Q96Y66,BRENDA::Q96Y66 2-oxoacid:ferredoxin oxidoreductase 1, subunit alpha; OFOR1; EC 1.2.7.11;; 2-oxoacid oxidoreductase (ferredoxin) (subunit 2/2) (EC 1.2.7.11) MRLSWVIGGAQGTGIDTAANIFGNAVASAGYYIYGNREYYSNIKGRHSYFSLTISDKRVRSNTQKIDILVSFDAETVFQHFYDVKDILIYNKAVETTKIDAVQSMEPELAERIKDFLTKQGYETTVKGALEYASKNNVTLIPVNYDEIAKKVADEMKVPLSVTERVKNIVGITISYKLLGLDVNYLIEAINSTFKQDLYRKMNELAVKDSYDIVESRYNLKPSSKERRRFWLDGNTAVAIGKIYGGVRFQSYYPITPASDESVYIEAHQDVLMEDPITGDKKKGTIVVVQAEDELAAINMAIGAALTGVRAATATSGPGFSLMVEGLGWAGMNEVPVVITYYIRGGPSTGLPTRTAQSDLIFPIFAGHGEFPKIVLASGDHAEAFKDAIWALNLAEKYQTPVIHLVEKTLANSYSTIPYEELELDKLKAERGKIVESGDISYKRFKFTEDGISPRAFLGKATMYYTGDEHNEEGHISEDVVNRTMMYEKRMKKLEVADKEIPEESRVKIYGDLNSRNLIITWGSPTGVLRDILEESNFDFTLLQIRMFSPFPKNLVSKLMEGRDKIITVEGNYLAQTSLLVKMYTGKDVTNSILKWNGRPFLRDELEEALIKVIKDGEKRVVLNGGI ofo ignore SwissProt::Q96Y68,BRENDA::Q96Y68 2-oxoacid:ferredoxin oxidoreductase 1, subunit beta; OFOR1; EC 1.2.7.11;; 2-oxoacid oxidoreductase (ferredoxin) (subunit 1/2) (EC 1.2.7.11) MAAFKPQWNDWCPGCGNFGILNAEQQAIVELGVDTKNVVVVSGIGCSGKIPHFFRTPISGVHTLHGRAIAFATGIKLSNPDLVVIVNGGDGDLLGIGAGHFVAAGRRNVDMVVILHDNGVYGLTKGQASPTLKRGEKPKSLPRPNINDAVNPIALAISSGYTFVARGYAYDVKHLKELIKSAIKHKGLALIDVLQPCPTYNDINTKEWYDKRIYKLDTLPDWDPVVKKPEEVNEKIKRAIDKSLEWGDRIPIGIFYQNELVPSYEERIKANSPAYLDYTPAKQLIEKEGKLTTIIDPLLKEREVD ofo ignore SwissProt::Q9YA11 2-oxoacid:ferredoxin oxidoreductase 1, subunit beta; OFOR1; EC 1.2.7.11 MASRGVASYRTEVWSDWCPGCGDFGILAAMQKAFAELNLDPAQTVVVSGIGCSSKTPHFINVNGVHTIHGRGIAFATGIKLANPQLKVIVNGGDGDLLGIGVAHFVALGRRNLDVTVLIHNNKVYGLTKGQASPTLRRGEKVKSLPVPNLQDAVNPIALAIASGYTFVARAYSLWVDHLKEILKAAINHKGSAVIDVLQPCVTYNDIYTAEFYKDRLYKLEDDPSWDPIVRDPSEDEEKKAAAIKKAEEWGTRIPVGVFYVNPLKDTYEERLAQRNPSYSIDNPPALQPISREDGSPIVGPDEFRKIFKRFIVNVKKL ofo ignore SwissProt::Q9YA13 2-oxoacid:ferredoxin oxidoreductase 1, subunit alpha; OFOR1; EC 1.2.7.11 MRKDVVLLVGGAQGSGLETTMQVLAPAYASLGYGVLANREYFSNIVGRHSYIHIRVSSSGEARPLYYPADFLGAMDAETVFTHWDDIGEGAFLLYDLGTARMRLQQIASMEPDLRSRLMQQYREAGIEPFTVEKVVEYLEREKRVRVIGLSFTALFDVLIKKHGLSRAQAQRFRSSILIGAIAGLTSLDREALDLGLQRRFGSRPKVLEINRDFIASVADEVEKEYGAQLKLEPAEPKSGEYVVASGNDVVAMGKVVGGVRYQAYYPITPASDESVLLEEFEGLKIDGESLGSIAILQTEDEIAAVSSVIGAALTGARASTATSGPGFSLMVEALGWAGKNDVPMVITYYQRGGPSTGLPTRGSQSDLLFSLFASHGEFPRIILSSGDHLEAFYDAIEAYNLAERFQMPVIHLLDKFLANMVASVPFPDWKAIKIDRGKTLFKAPTGPFKRFPRDQPLADRPVLGSGAITWYTGDENDEYGHIDEDPVNRLVMYERRWKKMEIADREIPEDFRVKYYGDEDAEVLLVGWGSVKIPALEAIERLREMGVNAAYLHLRMLSPLPKRRVSEVLSRFDADRVIAVEANYLGQASKIVTMETGFMFRKYILKWTGRPVYLHELVEGVLDIVRNGRDKVVLSYGK ofo ignore SwissProt::Q9YBX7 2-oxoacid:ferredoxin oxidoreductase 2, subunit alpha; OFOR2; EC 1.2.7.11 MVDISLIIGGPQGGGIESAGQIAIKSMVLLGYEVLGSREYHSNIMGAHSYYHLRVQQHRPRSLKLPVDGVLALDAESVFTHFRDVRPGGILVYDPGTKSTRVDAIQPMAGPLKKRLKSLFDSRGMQPVVESAVKLAEEAGARIVGLPLKEMLKTLSERTGAPVARVSRALNTLGLASMLYMLGVPVEYIEKAISLQFAGKEKVINMNVEAVRIAVDYVREAFGEPESRLPPGPRRGQTMMVATGNDLVAMGKIVGGLGVITYYPITPSSDEALYVEKHSYISIDGPLAEKLGYDKIAVAIVQMEDELASINAVLGAAAAGARASTTTSGPGFSLMNEAVSLAVEAEIPVVVTLWMRAGPSTGMPTRTGQQDLLHSIFSGHGDAPKIVLASGDHVEAFYDAIKAFNWAEEFQTPVIHLLDKYLASSMVSLAREDLDPSKVPITRGKLLDNPPADYRRYEVVEDGISPRARLGSATMVITGLEHDEYGYATEDPVMREIMMFKRERKFKVIEERIPDEEKAVLHGDSEASVALVSFGSTKQPILEALEMLRDEGVRARFAQVRLLYPFPGRLVEEMLEGVEKVIMVEQNLLGQLAMLLRAHTSIKPDSSIVKINGRPLYSFEVAGAVKRILETGEERVVVSHGS ofo ignore SwissProt::Q9YBX8 2-oxoacid:ferredoxin oxidoreductase 2, subunit beta; OFOR2; EC 1.2.7.11 MARSWLDYKTQAWVQWCPGCGDFGILNSIYRAVSELGIDPENLAVVGGIGCSGRTTYYVKGSNFHALHGRAIPVATGVKLANPHLNVIVAGGDGDLMGIGGGHFVALGRRNLNITVLLFDNAVYGLTKGQAAPTLPAWVKTKALSMPNIHDNINPVLLAFAAGYTFIARGYAYHTQQLKELIKTAVRHRGAALVDILQPCPTYNNIMTNKWYEERIYYVDQEEGYDPIIRTPEEFQKKAPAIAAKLMEFGDRIPLGILYWNQTRESFEERLEKIMPGYMSAPPATRRIELEGKPFLHPFDIFKDRLVTP ofo ignore SwissProt::S0EGG0 Ketoisovalerate reductase BEA2; KIVR; Beauvericin biosynthesis cluster protein 2; EC 1.2.7.7 MASQEHPNWLTALLADTRPPPKLFAWSPANIQPKLDEGIDMGSSNSDEEYDNDACVCPSTDSDQRIYIIGPGNIGRLYATHMARHPNALPITLVVHRKELLSQWAACEGVGLADLTSGKIFLNKRFTVEWWTETRPPYGPVKEVADGKKLHNVFISTKAEAGLSEADRIRRYLGRCSSVVFAQNGVCKLWPPHGPLYISHRYPSGDTPTFSACVVSHGVASAGPFLSVHAAPADAYIGPVFWASDPESPWRQPSDDFFIRHIATTPLVNTKQVSSGEIWLLQLEKLVMNAAINPLTALLRYKTGELFTSYGSDDPLARVIDKLLWQTSAVIQGLIDHETSHSVITSYAEQMSQPGTSCSVPKVRKKLTERFSQPILKAKLYAFGLKIFEHRSSMLQDIEAGRKTEIRDFNGWIVDTACFLGTGLDVSVHSGLTGLIERCERFDKMELGRALL ofoA curated SwissProt::P72578,BRENDA::P72578,metacyc::MONOMER-11911 2-oxoacid:ferredoxin oxidoreductase subunit alpha; OFOR; EC 1.2.7.11;; 2-oxoacid oxidoreductase (ferredoxin) (subunit 2/2) (EC 1.2.7.11);; 2-oxoacid:ferredoxin oxidoreductase α subunit (EC 1.2.7.11; EC 1.2.7.1; EC 1.2.7.3; EC 1.2.7.7) MRLSWVIGGAQGTGIDTAANIFGNAVASAGYYIYGNREYYSNIKGGHSYFSLTISDKRVRSNTQKIDILVSFDAETVFQHFYDVKDILIYNKAVETTKIDAVQSMEPELAERIKDFLTKQGYETTVKGALEYASKNNVTLIPVNYDEIAKKVADEMKVPLSVTERVKNIVGITISYKLLGLDVNYLIEAINSTFKQDLYRKMNELAVKDSYDIVESRYNLKPSSKERRRFWLDGNTAVAIGKIYGGVRFQSYYPITPASDESVYIEAHQDVLMEDPITGDKKKGTIVVVQAEDELAAINMAIGAALTGVRAATATSGPGFSLMVEGLGWAGMNEVPVVITYYIRGGPSTGLPTRTAQSDLIFPIFAGHGEFPKIVLASGDHAEAFKDAIWALNLAEKYQTPVIHLVEKTLANSYSTIPYEELELDKLKAERGKIVESGDISYKRFKFTEDGISPRAFLGKATMYYTGDEHNEEGHISEDVVNRTMMYEKRMKKLEVADKEIPEESRVKIYGDLNSRNLIITWGSPTGVLRDILEESNFDFTLLQIRMFSPFPKNLVSKLMEGRDKIITVEGNYLAQTSLLVKMYTGKDVTNSILKWNGRPFLRDELEEALIKVIKDGEKRVVLNGGIYTSME ofoA ignore SwissProt::A0A0E3JT70 2-oxoacid:ferredoxin oxidoreductase subunit alpha; OFOR; EC 1.2.7.11 MRISWMIGGAQGSGVDTSANIFGNAVAASGYYIYGNREYYSNIKGRHSYFNLTISDKPPRSIAQQIEILTSFDAETIFQHFNEVKDVLIYSTEVENTKAEQVQSMEPEITEHVVKFLKEKGYGTTVKDVINYLKKEKGVKVIPIDYMEILKKVADQAKVQLSVADRARNTIAIAASYKLLGLKEQYLINSITRTFRQEVFAKINTIAAQLAMQQIQPMYNLPELPNNEEKINLDGNTAAAIGKIYGGLRFQSYYPITPASDESVFIEAHQTVFTVDPKTGEKRKSTIVVVQAEDELAAINMASGAALTGVRAATATSGPGFSLMVEGMGWAGMNEVPVVITYYIRGGPSTGQPTRTSQADLMFALNAGHGEFPRIVIASGDHVEAFHDGTWALNLAQKYQTPVIHLVDKALANSYSIIPKKTLGMENIRIEKGKIVINTNTPELKRFEITEDGISPFAPLGTARVHYTGDEHDEYGFIAEASENREKMYEKRIKKLMTADKEIPEESRVNVYGNTDSKVAIITWGSPKGAILDAMEELENEGIKPMLIQIRMFSPFPKNLMRKLLNGKEFIIDVESNYFGQAGEVLKLNTGIEPTHYILKWNGRPMMRDEVKEGIKAVVQKGERRVVLHGGA ofoA ignore SwissProt::A0A0E3KBH3 2-oxoacid:ferredoxin oxidoreductase subunit beta; OFOR; EC 1.2.7.11 MAGLKVEWNDWCPGCGNFGILSAEQQAIQELGLDPKKVVLVSGIGCSGKIPHFIRLPASGVHTLHGRALTFAIGIKLANPSLEVIVNGGDGDQLGIGVGHFVSAGRRNVDLTVIVHNNGVYGLTKGQASPTLKLGVKTKSLPKPNINSDINPIALAISSGYTFVARGYAYDVKHLKEIIKKAIKHKGLAMIDVLQPCPTYNDIHTKEYYDKRVYKLDEDPSWDPIVKKPEEMDDKMSKAILKSMEWGDRTPIGIFYQNELVSTYEQRIAERSPSYLDNPPAHDVIEFEGKPTTDVEDILKERRVT ofoA ignore SwissProt::B6D9A7 Ketoisovalerate reductase; KIVR; EC 1.2.7.7 MPSPEHPSWLSTLLADTRPPPKLFAWSPANLDSPTAVKPDRADRGDFDPGKYPVDAPITTASEPVKRIYIVGPGNVGRLYASYMSRQRDALPITLVVHRKELLSQWVTSEGVVLADRGGKVTKNKQFDVEWWTESRPRYGPVREVADGEKLHNVFISTKADAGLGEADRLRRYLGRCSSVVFAQNGVSKLWAPYGPLYVASRYHADDAPSFSACVVNHGISAAGLFYSIHTSPSDAFIGPIFKGSAAPAHGQNKRRRLDDDFFTTYISSTPFLDTKHVSSGQLWIIQLEKLVLNAAINPLTTLLRCKTGQLFASYDSHDALTRVLDQLLWQASAVIQALINHDANIDMLTSYAETVHRLVPGSDDYGRNFANIRRKLTVRFSQPILKAKLYAFGLNIREHRSSMLQDAEAGRKTEIRDVNGWIVDMAEYLGLDLDVGIHRGLIELIEECVVLDKEELARRLL ofoA ignore SwissProt::G3GBU6 Ketoisovalerate reductase BEA2; KIVR; EC 1.2.7.7 MTSQEHPNWLTALLVDTRPPPKLFAWSPANIQPKLDEGIDMGSSNSDEEYDNDACVCQSTDSDQRIYIIGPGNIGRLYATHMARHPNALPITLVVHRKELLSQWVACEGVGLADITSGKLFLNKGFTVEWWTETRPPYGPVKEVADGKKLHNVFISTKAEAGLAEADRIRRYLGRCSSVVFAQNGVCKLWPPHGPLYISHRYPSGDTPTFSACVVSHGVASAGPFLSVHAAPADAYIGPVFWASDPESPWRHPSDDFFIRHIATTPHVNTKQVSSGEIWLLQLEKLVMNAAINPLTALLRCKTGELFTSYGSDDPLALVIDKLLWQTSAVIQGLVDHKTSHSVITSYAEHMSQPGTSCSVPKVRKKLMERFSQPILKAKLGWEEDRDTGL ofoA ignore SwissProt::P72579,BRENDA::P72579,metacyc::MONOMER-11912 2-oxoacid:ferredoxin oxidoreductase subunit beta; OFOR; EC 1.2.7.11;; 2-oxoacid oxidoreductase (ferredoxin) (subunit 1/2) (EC 1.2.7.11);; 2-oxoacid:ferredoxin oxidoreductase β subunit (EC 1.2.7.11; EC 1.2.7.1; EC 1.2.7.3; EC 1.2.7.7) MAAFTPQWNDWCPGCGNFGILNAEQQAIVELGVDTKNVVVVSGIGCSGKIPHFFRTPISGVHTLHGRAIAFATGIKLSNPDLVVIVNGGDGDLLGIGAGHFVAAGRRNVDMVVILHDNGVYGLTKGQASPTLKRGEKPKSLPRPNINDAVNPIALAISSGYTFVARGYAYDVKHLKELIKSAIKHKGLALIDVLQPCPTYNDINTKEWYDKRIYKLDTLPDWDPVVKKPEEVNEKIKRAIDKSLEWGDRIPIGIFYQNELVPSYEERIKANSPAYLDYTPAKQLIEKEGKLTTIIDPLLKEREVD ofoA ignore SwissProt::P80908 Ketoisovalerate oxidoreductase subunit VorB; VOR; 2-oxoisovalerate ferredoxin reductase subunit beta; 2-oxoisovalerate oxidoreductase beta chain; EC 1.2.7.7 MATQMVKGNTAVIIGAMYAGCDCYFGYPITPASEILHEASRYFPLVGRKFVQAESEEAAINMVYGAAAAGHRVMTASSGPGMSLKQEGISFLAGAELPAVIVDVMRAGPGLGNIGPEQADYNQLVKGGGHGNYRNIVLAPNSVQEMCDLTMDAFELADKYRNPVIILADAVLGQMAEPLRFPERAVEHRPDTSWAVCGSRETMKNLVTSIFLDFDELEEFNFYLQEKYAAVEENEVRYEEYMVEDAEIVLVAYGISSRVAKSAVDTARADGIKVGLLRPITLFPFPSERIRELAEGGCTFISVEMSSGQMREDIKMASGCRDVELVNRMGGNLIELRDILRKIREIAGESND ofoA ignore SwissProt::P80909 Ketoisovalerate oxidoreductase subunit VorC; VOR; 2-oxoisovalerate ferredoxin reductase subunit gamma; 2-oxoisovalerate oxidoreductase gamma chain; EC 1.2.7.7 MKKAYPVINRVECKACERCIIACPRKVLYMSNKINERGYHYVEYRGEGCNGCGNCYYTCPEINAIEVHIERCEDGDTDG ofoA ignore SwissProt::Q96XT2,BRENDA::Q96XT2 2-oxoacid:ferredoxin oxidoreductase 2, subunit alpha; OFOR2; EC 1.2.7.11;; 2-oxoacid oxidoreductase (ferredoxin) (subunit 2/2) (EC 1.2.7.11) MTRIVWMIGGAQGLGVDTSANIFGNAVAKAGYYLFGNREYYSNIKGRHSYFEVVISEKPIRSLSSYVNILASFDAETVFQHFTETKEYLIYNVEYENTTVDLVKSMEPEMAEQVKEALSKERLGFTIKDVLEYLKRRGVKVIGFNYTELIKKIADTFKVPMSVVERAKNMIAVGASYGLLGLKFDYLKDAISSTFKNELFIKFNTMAAELGYNSVPNVYKLQEYKIEKQRIQVDGNTISAMGKLAGGLRFQSYYPITPASDESVYIEANQNLDMIVEGNELRKGGVVVVQAEDELAAINMAVGAALTGVRSATATSGPGFSLMSEGISWAGMNEVPVVITYYMRGAPATGLPTRSGQADLKFALNVGHGEFPRIVIASGDHVEIFWDAIWALNLAEKYQTPVIHIIEKTLANAYSVFEEELITNRPYVIERGKIVKPTSDYFNRFEVTEDGISPRVFLGQASIFYTGDEHNEEGHITENSINRMKMYEKRNKKLETADKEIPEEQRVNIVGDADIVLLTWGSPKGAILDAMEELSKDGIKTMMVQVKMFNPYPKNLMKKILSGKSKIIAVENNYNAQGAEVLAEKTGIFATNYILKWTGRPITREEVIEGIKKILERDEKRVVLYGGA ofoA ignore SwissProt::Q96XT4,BRENDA::Q96XT4 2-oxoacid:ferredoxin oxidoreductase 2, subunit beta; OFOR2; EC 1.2.7.11;; 2-oxoacid oxidoreductase (ferredoxin) (subunit 1/2) (EC 1.2.7.11) MVERKPVFVDWCPGCGDFGILRAEEMAIRELGINPKSVVIVSGIGCSGKIPHFMNLPISGVHTLHGRSIAFATGIKLSNPSLEVIVNVGDGDGLGIGMGHFVHLGRRNIDIAVLVHNNGVYGLTKGQASPTLHRGEKTKSLPKPNIMDAVNPLAVALAAGYTFVARGYAYDVMHLKELIKKAILHKGSALVDILQPCPTYNDINTKEWYDKRVYKLDNVPGWDPVVRKEEEAQKKFEQAIMKSYEWGEKIPIGIFYQNELVPTFEDRLTSNIPNYREYYPAKQQIEINGISTTKIDELIKAKRI ofoA ignore SwissProt::Q96Y66,BRENDA::Q96Y66 2-oxoacid:ferredoxin oxidoreductase 1, subunit alpha; OFOR1; EC 1.2.7.11;; 2-oxoacid oxidoreductase (ferredoxin) (subunit 2/2) (EC 1.2.7.11) MRLSWVIGGAQGTGIDTAANIFGNAVASAGYYIYGNREYYSNIKGRHSYFSLTISDKRVRSNTQKIDILVSFDAETVFQHFYDVKDILIYNKAVETTKIDAVQSMEPELAERIKDFLTKQGYETTVKGALEYASKNNVTLIPVNYDEIAKKVADEMKVPLSVTERVKNIVGITISYKLLGLDVNYLIEAINSTFKQDLYRKMNELAVKDSYDIVESRYNLKPSSKERRRFWLDGNTAVAIGKIYGGVRFQSYYPITPASDESVYIEAHQDVLMEDPITGDKKKGTIVVVQAEDELAAINMAIGAALTGVRAATATSGPGFSLMVEGLGWAGMNEVPVVITYYIRGGPSTGLPTRTAQSDLIFPIFAGHGEFPKIVLASGDHAEAFKDAIWALNLAEKYQTPVIHLVEKTLANSYSTIPYEELELDKLKAERGKIVESGDISYKRFKFTEDGISPRAFLGKATMYYTGDEHNEEGHISEDVVNRTMMYEKRMKKLEVADKEIPEESRVKIYGDLNSRNLIITWGSPTGVLRDILEESNFDFTLLQIRMFSPFPKNLVSKLMEGRDKIITVEGNYLAQTSLLVKMYTGKDVTNSILKWNGRPFLRDELEEALIKVIKDGEKRVVLNGGI ofoA ignore SwissProt::Q96Y68,BRENDA::Q96Y68 2-oxoacid:ferredoxin oxidoreductase 1, subunit beta; OFOR1; EC 1.2.7.11;; 2-oxoacid oxidoreductase (ferredoxin) (subunit 1/2) (EC 1.2.7.11) MAAFKPQWNDWCPGCGNFGILNAEQQAIVELGVDTKNVVVVSGIGCSGKIPHFFRTPISGVHTLHGRAIAFATGIKLSNPDLVVIVNGGDGDLLGIGAGHFVAAGRRNVDMVVILHDNGVYGLTKGQASPTLKRGEKPKSLPRPNINDAVNPIALAISSGYTFVARGYAYDVKHLKELIKSAIKHKGLALIDVLQPCPTYNDINTKEWYDKRIYKLDTLPDWDPVVKKPEEVNEKIKRAIDKSLEWGDRIPIGIFYQNELVPSYEERIKANSPAYLDYTPAKQLIEKEGKLTTIIDPLLKEREVD ofoA ignore SwissProt::Q9YA11 2-oxoacid:ferredoxin oxidoreductase 1, subunit beta; OFOR1; EC 1.2.7.11 MASRGVASYRTEVWSDWCPGCGDFGILAAMQKAFAELNLDPAQTVVVSGIGCSSKTPHFINVNGVHTIHGRGIAFATGIKLANPQLKVIVNGGDGDLLGIGVAHFVALGRRNLDVTVLIHNNKVYGLTKGQASPTLRRGEKVKSLPVPNLQDAVNPIALAIASGYTFVARAYSLWVDHLKEILKAAINHKGSAVIDVLQPCVTYNDIYTAEFYKDRLYKLEDDPSWDPIVRDPSEDEEKKAAAIKKAEEWGTRIPVGVFYVNPLKDTYEERLAQRNPSYSIDNPPALQPISREDGSPIVGPDEFRKIFKRFIVNVKKL ofoA ignore SwissProt::Q9YA13 2-oxoacid:ferredoxin oxidoreductase 1, subunit alpha; OFOR1; EC 1.2.7.11 MRKDVVLLVGGAQGSGLETTMQVLAPAYASLGYGVLANREYFSNIVGRHSYIHIRVSSSGEARPLYYPADFLGAMDAETVFTHWDDIGEGAFLLYDLGTARMRLQQIASMEPDLRSRLMQQYREAGIEPFTVEKVVEYLEREKRVRVIGLSFTALFDVLIKKHGLSRAQAQRFRSSILIGAIAGLTSLDREALDLGLQRRFGSRPKVLEINRDFIASVADEVEKEYGAQLKLEPAEPKSGEYVVASGNDVVAMGKVVGGVRYQAYYPITPASDESVLLEEFEGLKIDGESLGSIAILQTEDEIAAVSSVIGAALTGARASTATSGPGFSLMVEALGWAGKNDVPMVITYYQRGGPSTGLPTRGSQSDLLFSLFASHGEFPRIILSSGDHLEAFYDAIEAYNLAERFQMPVIHLLDKFLANMVASVPFPDWKAIKIDRGKTLFKAPTGPFKRFPRDQPLADRPVLGSGAITWYTGDENDEYGHIDEDPVNRLVMYERRWKKMEIADREIPEDFRVKYYGDEDAEVLLVGWGSVKIPALEAIERLREMGVNAAYLHLRMLSPLPKRRVSEVLSRFDADRVIAVEANYLGQASKIVTMETGFMFRKYILKWTGRPVYLHELVEGVLDIVRNGRDKVVLSYGK ofoA ignore SwissProt::Q9YBX7 2-oxoacid:ferredoxin oxidoreductase 2, subunit alpha; OFOR2; EC 1.2.7.11 MVDISLIIGGPQGGGIESAGQIAIKSMVLLGYEVLGSREYHSNIMGAHSYYHLRVQQHRPRSLKLPVDGVLALDAESVFTHFRDVRPGGILVYDPGTKSTRVDAIQPMAGPLKKRLKSLFDSRGMQPVVESAVKLAEEAGARIVGLPLKEMLKTLSERTGAPVARVSRALNTLGLASMLYMLGVPVEYIEKAISLQFAGKEKVINMNVEAVRIAVDYVREAFGEPESRLPPGPRRGQTMMVATGNDLVAMGKIVGGLGVITYYPITPSSDEALYVEKHSYISIDGPLAEKLGYDKIAVAIVQMEDELASINAVLGAAAAGARASTTTSGPGFSLMNEAVSLAVEAEIPVVVTLWMRAGPSTGMPTRTGQQDLLHSIFSGHGDAPKIVLASGDHVEAFYDAIKAFNWAEEFQTPVIHLLDKYLASSMVSLAREDLDPSKVPITRGKLLDNPPADYRRYEVVEDGISPRARLGSATMVITGLEHDEYGYATEDPVMREIMMFKRERKFKVIEERIPDEEKAVLHGDSEASVALVSFGSTKQPILEALEMLRDEGVRARFAQVRLLYPFPGRLVEEMLEGVEKVIMVEQNLLGQLAMLLRAHTSIKPDSSIVKINGRPLYSFEVAGAVKRILETGEERVVVSHGS ofoA ignore SwissProt::Q9YBX8 2-oxoacid:ferredoxin oxidoreductase 2, subunit beta; OFOR2; EC 1.2.7.11 MARSWLDYKTQAWVQWCPGCGDFGILNSIYRAVSELGIDPENLAVVGGIGCSGRTTYYVKGSNFHALHGRAIPVATGVKLANPHLNVIVAGGDGDLMGIGGGHFVALGRRNLNITVLLFDNAVYGLTKGQAAPTLPAWVKTKALSMPNIHDNINPVLLAFAAGYTFIARGYAYHTQQLKELIKTAVRHRGAALVDILQPCPTYNNIMTNKWYEERIYYVDQEEGYDPIIRTPEEFQKKAPAIAAKLMEFGDRIPLGILYWNQTRESFEERLEKIMPGYMSAPPATRRIELEGKPFLHPFDIFKDRLVTP ofoA ignore SwissProt::S0EGG0 Ketoisovalerate reductase BEA2; KIVR; Beauvericin biosynthesis cluster protein 2; EC 1.2.7.7 MASQEHPNWLTALLADTRPPPKLFAWSPANIQPKLDEGIDMGSSNSDEEYDNDACVCPSTDSDQRIYIIGPGNIGRLYATHMARHPNALPITLVVHRKELLSQWAACEGVGLADLTSGKIFLNKRFTVEWWTETRPPYGPVKEVADGKKLHNVFISTKAEAGLSEADRIRRYLGRCSSVVFAQNGVCKLWPPHGPLYISHRYPSGDTPTFSACVVSHGVASAGPFLSVHAAPADAYIGPVFWASDPESPWRQPSDDFFIRHIATTPLVNTKQVSSGEIWLLQLEKLVMNAAINPLTALLRYKTGELFTSYGSDDPLARVIDKLLWQTSAVIQGLIDHETSHSVITSYAEQMSQPGTSCSVPKVRKKLTERFSQPILKAKLYAFGLKIFEHRSSMLQDIEAGRKTEIRDFNGWIVDTACFLGTGLDVSVHSGLTGLIERCERFDKMELGRALL ofoA ignore reanno::Cup4G11:RR42_RS19540 3-methyl-2-oxobutanoate:ferredoxin oxidoreductase (EC 1.2.7.7) MNAPLTPPVSDAIRRALANVSLEDKYTLERGRVYISGTQALVRLPMLQRERDRAAGLNTAGFISGYRGSPLGALDQSLWKAKQHLAAHDIVFQAGLNEDLAATSVWGSQQVNMYPDARFEGVFGMWYGKGPGVDRTSDVFKHANSAGSSRHGGVLVLAGDDHAAKSSTLAHQSEHIFKACGLPVLYPSNVQEYLDYGLHAWAMSRYSGLWVSMKCVTDVVESSASVELDPHRVEIVLPQDFILPPGGLNIRWPDPPLEQEARLLDYKWYAGLAYVRANKIDRIEIDSPHARFGIMTGGKAYLDTRQALANLGLDDETCARIGIRLYKVGCVWPLEAHGARAFAEGLQEILVVEEKRQIMEYALKEELYNWRDDVRPKVYGKFDEKDNAGGEWSIPQSNWLLPAHYELSPAIIARAIATRLDKFELPADVRARIAARIAVIEAKEKAMAVPRVAAERKPWFCSGCPHNTSTNVPEGSRALAGIGCHYMTVWMDRSTSTFSQMGGEGVAWIGQAPFAGDKHVFANLGDGTYFHSGLLAIRASIAAGVNITYKILYNDAVAMTGGQPIDGKLSVQDVANQVAAEGARKIVVVTDEPEKYSAAIKLPQGVEVHHRDELDRIQRELREVPGATILIYDQTCATEKRRRRKRGTYPDPAKRAFINDAVCEGCGDCSVKSNCLSVEPLETELGTKRQINQSSCNKDFSCVNGFCPSFVTAEGAQVKKPERHGVSMDNLPALPQPALPGLEHPYGVLVTGVGGTGVVTIGGLLGMAAHLENKGVTVLDMAGLAQKGGAVLSHVQIAAHPDQLHATRIAMGEADLVIGCDAIVSAIDDVISKTQVGRTRAIVNTAQTPTAEFIKNPKWQFPGLSAEQDVRNAVGEACDFINASGLAVALIGDAIFTNPLVLGYAWQKGWLPLSLDALVRAIELNGTAVEKNKAAFDWGRHMAHDPEHVLSLTGKLRNTAEGAEVVKLPTSSGALLEKLIAHRAEHLTAYQDAAYAQTFRDTVSRVRAAESALVGNGKPLPLTEAAARNLSKLMAYKDEYEVARLYTDPIFLDKLRNQFEGEPGRDYQLNFWLAPPLMAKRDEKGHLVKRRFGPSTMKLFGVLAKLKGLRGGVFDVFGKTAERRTERALIGEYRALLEELTRGLSAANHATAITLASLPDDIRGFGHVKDDNLAKVRTRWTALLEQFRHPETAQRVA ofoA ignore reanno::psRCH2:GFF3452 branched-chain ketoacid ferredoxin reductase (EC 1.2.7.7) active on 4-methyl-2-oxopentanoate, (S)-3-methyl-2-oxopentanoate, or 3-methyl-2-oxobutanoate MSLAEIRLDDKYRLATGHLYLTGTQALTRLPMLQHQRDQARGLNTGGFISGYRGSPLGGLDKSLWEARDYLKQHAIHFQPGVNEELAATAVWGSQQTNLFPGAKYDGVFAMWYGKGPGVDRAGDVFKHANAAGVSPQGGVLLLAGDDHGCKSSTLPHQSEHAFIAASIPVLNPANVQEILDYGIIGWELSRYSGCWVALKTIAENVDSSAVVEVDPLRVQTRIPEDFELPEDGVHIRWPDPPLAQEKRLNLYKIYAARAFARANNLNRVMLDSPNPRLGIITTGKSYLDVRQALDDLGLDEALCASVGLRVLKVGMSWPLEPVSVHEFAQGLDEILVVEEKRSIIEDQLTGQLYNWPVSKRPRVVGEFDEQGNSLLPNLSELTPAMIARVIAKRLAPIYTSDSIQARLAFLAAKEKALAARSYSTVRTPHYCSGCPHNSSTKVPEGSRASAGIGCHYMVQWMDRRTETFTQMGGEGVNWIGQAPFTDTPHMFQNLGDGTYFHSGSLAVRAAVAAGVNVTYKILYNDAVAMTGGQPIDGELRVDQLSRQIFHEGVKRIALVSDEPDKYPSRDTFAPITSFHHRRELDAVQRELREFKGVSVIIYDQTCATEKRRRRKRGKMEDPAKRAFINPAVCEGCGDCGEKSNCLAVLPLETELGRKREIDQNACNKDFSCVEGFCPSFVTVHGGGLRKPEAVAGGIEAATLPEPQHPTLDRPWNVLIPGVGGSGVTTLGALLGMAAHLEGKGCTVLDQAGLAQKFGPVTTHVRIAAKQSDIYAVRIAAGEADLLLGCDLIVAAGDESLTRLNEQISNAVVNSHESATAEFTRNPDAQVPGAAMRQAISDAVGADKTHFVDATRLATRLLGDSIATNLFLLGFAYQQGLLPISAEAIEKAIELNGVSAKLNLQAFRWGRRAVLEREAVEQLARPVDMVEPICKTLEEIVDWRVDFLTRYQSAGLARRYRQLVERVRDADSADDLALSKAVARYYFKLLAYKDEYEVARLYSEPEFRQQLEAQFEGDYKLQFHLAPAWLAKRDPVTGEPRKRELGPWVLNLFGVLAKFRFLRGTPLDPFGYGHDRRVERQLISEYEKTVDELLAQLKPTNYRTAVAIAALPEQIRGYGPVKERSIAKARQQEKLLREQLAKGDEVQSVRLFQPAA ofoB curated SwissProt::P72579,BRENDA::P72579,metacyc::MONOMER-11912 2-oxoacid:ferredoxin oxidoreductase subunit beta; OFOR; EC 1.2.7.11;; 2-oxoacid oxidoreductase (ferredoxin) (subunit 1/2) (EC 1.2.7.11);; 2-oxoacid:ferredoxin oxidoreductase β subunit (EC 1.2.7.11; EC 1.2.7.1; EC 1.2.7.3; EC 1.2.7.7) MAAFTPQWNDWCPGCGNFGILNAEQQAIVELGVDTKNVVVVSGIGCSGKIPHFFRTPISGVHTLHGRAIAFATGIKLSNPDLVVIVNGGDGDLLGIGAGHFVAAGRRNVDMVVILHDNGVYGLTKGQASPTLKRGEKPKSLPRPNINDAVNPIALAISSGYTFVARGYAYDVKHLKELIKSAIKHKGLALIDVLQPCPTYNDINTKEWYDKRIYKLDTLPDWDPVVKKPEEVNEKIKRAIDKSLEWGDRIPIGIFYQNELVPSYEERIKANSPAYLDYTPAKQLIEKEGKLTTIIDPLLKEREVD ofoB ignore SwissProt::A0A0E3JT70 2-oxoacid:ferredoxin oxidoreductase subunit alpha; OFOR; EC 1.2.7.11 MRISWMIGGAQGSGVDTSANIFGNAVAASGYYIYGNREYYSNIKGRHSYFNLTISDKPPRSIAQQIEILTSFDAETIFQHFNEVKDVLIYSTEVENTKAEQVQSMEPEITEHVVKFLKEKGYGTTVKDVINYLKKEKGVKVIPIDYMEILKKVADQAKVQLSVADRARNTIAIAASYKLLGLKEQYLINSITRTFRQEVFAKINTIAAQLAMQQIQPMYNLPELPNNEEKINLDGNTAAAIGKIYGGLRFQSYYPITPASDESVFIEAHQTVFTVDPKTGEKRKSTIVVVQAEDELAAINMASGAALTGVRAATATSGPGFSLMVEGMGWAGMNEVPVVITYYIRGGPSTGQPTRTSQADLMFALNAGHGEFPRIVIASGDHVEAFHDGTWALNLAQKYQTPVIHLVDKALANSYSIIPKKTLGMENIRIEKGKIVINTNTPELKRFEITEDGISPFAPLGTARVHYTGDEHDEYGFIAEASENREKMYEKRIKKLMTADKEIPEESRVNVYGNTDSKVAIITWGSPKGAILDAMEELENEGIKPMLIQIRMFSPFPKNLMRKLLNGKEFIIDVESNYFGQAGEVLKLNTGIEPTHYILKWNGRPMMRDEVKEGIKAVVQKGERRVVLHGGA ofoB ignore SwissProt::A0A0E3KBH3 2-oxoacid:ferredoxin oxidoreductase subunit beta; OFOR; EC 1.2.7.11 MAGLKVEWNDWCPGCGNFGILSAEQQAIQELGLDPKKVVLVSGIGCSGKIPHFIRLPASGVHTLHGRALTFAIGIKLANPSLEVIVNGGDGDQLGIGVGHFVSAGRRNVDLTVIVHNNGVYGLTKGQASPTLKLGVKTKSLPKPNINSDINPIALAISSGYTFVARGYAYDVKHLKEIIKKAIKHKGLAMIDVLQPCPTYNDIHTKEYYDKRVYKLDEDPSWDPIVKKPEEMDDKMSKAILKSMEWGDRTPIGIFYQNELVSTYEQRIAERSPSYLDNPPAHDVIEFEGKPTTDVEDILKERRVT ofoB ignore SwissProt::B6D9A7 Ketoisovalerate reductase; KIVR; EC 1.2.7.7 MPSPEHPSWLSTLLADTRPPPKLFAWSPANLDSPTAVKPDRADRGDFDPGKYPVDAPITTASEPVKRIYIVGPGNVGRLYASYMSRQRDALPITLVVHRKELLSQWVTSEGVVLADRGGKVTKNKQFDVEWWTESRPRYGPVREVADGEKLHNVFISTKADAGLGEADRLRRYLGRCSSVVFAQNGVSKLWAPYGPLYVASRYHADDAPSFSACVVNHGISAAGLFYSIHTSPSDAFIGPIFKGSAAPAHGQNKRRRLDDDFFTTYISSTPFLDTKHVSSGQLWIIQLEKLVLNAAINPLTTLLRCKTGQLFASYDSHDALTRVLDQLLWQASAVIQALINHDANIDMLTSYAETVHRLVPGSDDYGRNFANIRRKLTVRFSQPILKAKLYAFGLNIREHRSSMLQDAEAGRKTEIRDVNGWIVDMAEYLGLDLDVGIHRGLIELIEECVVLDKEELARRLL ofoB ignore SwissProt::G3GBU6 Ketoisovalerate reductase BEA2; KIVR; EC 1.2.7.7 MTSQEHPNWLTALLVDTRPPPKLFAWSPANIQPKLDEGIDMGSSNSDEEYDNDACVCQSTDSDQRIYIIGPGNIGRLYATHMARHPNALPITLVVHRKELLSQWVACEGVGLADITSGKLFLNKGFTVEWWTETRPPYGPVKEVADGKKLHNVFISTKAEAGLAEADRIRRYLGRCSSVVFAQNGVCKLWPPHGPLYISHRYPSGDTPTFSACVVSHGVASAGPFLSVHAAPADAYIGPVFWASDPESPWRHPSDDFFIRHIATTPHVNTKQVSSGEIWLLQLEKLVMNAAINPLTALLRCKTGELFTSYGSDDPLALVIDKLLWQTSAVIQGLVDHKTSHSVITSYAEHMSQPGTSCSVPKVRKKLMERFSQPILKAKLGWEEDRDTGL ofoB ignore SwissProt::P72578,BRENDA::P72578,metacyc::MONOMER-11911 2-oxoacid:ferredoxin oxidoreductase subunit alpha; OFOR; EC 1.2.7.11;; 2-oxoacid oxidoreductase (ferredoxin) (subunit 2/2) (EC 1.2.7.11);; 2-oxoacid:ferredoxin oxidoreductase α subunit (EC 1.2.7.11; EC 1.2.7.1; EC 1.2.7.3; EC 1.2.7.7) MRLSWVIGGAQGTGIDTAANIFGNAVASAGYYIYGNREYYSNIKGGHSYFSLTISDKRVRSNTQKIDILVSFDAETVFQHFYDVKDILIYNKAVETTKIDAVQSMEPELAERIKDFLTKQGYETTVKGALEYASKNNVTLIPVNYDEIAKKVADEMKVPLSVTERVKNIVGITISYKLLGLDVNYLIEAINSTFKQDLYRKMNELAVKDSYDIVESRYNLKPSSKERRRFWLDGNTAVAIGKIYGGVRFQSYYPITPASDESVYIEAHQDVLMEDPITGDKKKGTIVVVQAEDELAAINMAIGAALTGVRAATATSGPGFSLMVEGLGWAGMNEVPVVITYYIRGGPSTGLPTRTAQSDLIFPIFAGHGEFPKIVLASGDHAEAFKDAIWALNLAEKYQTPVIHLVEKTLANSYSTIPYEELELDKLKAERGKIVESGDISYKRFKFTEDGISPRAFLGKATMYYTGDEHNEEGHISEDVVNRTMMYEKRMKKLEVADKEIPEESRVKIYGDLNSRNLIITWGSPTGVLRDILEESNFDFTLLQIRMFSPFPKNLVSKLMEGRDKIITVEGNYLAQTSLLVKMYTGKDVTNSILKWNGRPFLRDELEEALIKVIKDGEKRVVLNGGIYTSME ofoB ignore SwissProt::P80908 Ketoisovalerate oxidoreductase subunit VorB; VOR; 2-oxoisovalerate ferredoxin reductase subunit beta; 2-oxoisovalerate oxidoreductase beta chain; EC 1.2.7.7 MATQMVKGNTAVIIGAMYAGCDCYFGYPITPASEILHEASRYFPLVGRKFVQAESEEAAINMVYGAAAAGHRVMTASSGPGMSLKQEGISFLAGAELPAVIVDVMRAGPGLGNIGPEQADYNQLVKGGGHGNYRNIVLAPNSVQEMCDLTMDAFELADKYRNPVIILADAVLGQMAEPLRFPERAVEHRPDTSWAVCGSRETMKNLVTSIFLDFDELEEFNFYLQEKYAAVEENEVRYEEYMVEDAEIVLVAYGISSRVAKSAVDTARADGIKVGLLRPITLFPFPSERIRELAEGGCTFISVEMSSGQMREDIKMASGCRDVELVNRMGGNLIELRDILRKIREIAGESND ofoB ignore SwissProt::P80909 Ketoisovalerate oxidoreductase subunit VorC; VOR; 2-oxoisovalerate ferredoxin reductase subunit gamma; 2-oxoisovalerate oxidoreductase gamma chain; EC 1.2.7.7 MKKAYPVINRVECKACERCIIACPRKVLYMSNKINERGYHYVEYRGEGCNGCGNCYYTCPEINAIEVHIERCEDGDTDG ofoB ignore SwissProt::Q96XT2,BRENDA::Q96XT2 2-oxoacid:ferredoxin oxidoreductase 2, subunit alpha; OFOR2; EC 1.2.7.11;; 2-oxoacid oxidoreductase (ferredoxin) (subunit 2/2) (EC 1.2.7.11) MTRIVWMIGGAQGLGVDTSANIFGNAVAKAGYYLFGNREYYSNIKGRHSYFEVVISEKPIRSLSSYVNILASFDAETVFQHFTETKEYLIYNVEYENTTVDLVKSMEPEMAEQVKEALSKERLGFTIKDVLEYLKRRGVKVIGFNYTELIKKIADTFKVPMSVVERAKNMIAVGASYGLLGLKFDYLKDAISSTFKNELFIKFNTMAAELGYNSVPNVYKLQEYKIEKQRIQVDGNTISAMGKLAGGLRFQSYYPITPASDESVYIEANQNLDMIVEGNELRKGGVVVVQAEDELAAINMAVGAALTGVRSATATSGPGFSLMSEGISWAGMNEVPVVITYYMRGAPATGLPTRSGQADLKFALNVGHGEFPRIVIASGDHVEIFWDAIWALNLAEKYQTPVIHIIEKTLANAYSVFEEELITNRPYVIERGKIVKPTSDYFNRFEVTEDGISPRVFLGQASIFYTGDEHNEEGHITENSINRMKMYEKRNKKLETADKEIPEEQRVNIVGDADIVLLTWGSPKGAILDAMEELSKDGIKTMMVQVKMFNPYPKNLMKKILSGKSKIIAVENNYNAQGAEVLAEKTGIFATNYILKWTGRPITREEVIEGIKKILERDEKRVVLYGGA ofoB ignore SwissProt::Q96XT4,BRENDA::Q96XT4 2-oxoacid:ferredoxin oxidoreductase 2, subunit beta; OFOR2; EC 1.2.7.11;; 2-oxoacid oxidoreductase (ferredoxin) (subunit 1/2) (EC 1.2.7.11) MVERKPVFVDWCPGCGDFGILRAEEMAIRELGINPKSVVIVSGIGCSGKIPHFMNLPISGVHTLHGRSIAFATGIKLSNPSLEVIVNVGDGDGLGIGMGHFVHLGRRNIDIAVLVHNNGVYGLTKGQASPTLHRGEKTKSLPKPNIMDAVNPLAVALAAGYTFVARGYAYDVMHLKELIKKAILHKGSALVDILQPCPTYNDINTKEWYDKRVYKLDNVPGWDPVVRKEEEAQKKFEQAIMKSYEWGEKIPIGIFYQNELVPTFEDRLTSNIPNYREYYPAKQQIEINGISTTKIDELIKAKRI ofoB ignore SwissProt::Q96Y66,BRENDA::Q96Y66 2-oxoacid:ferredoxin oxidoreductase 1, subunit alpha; OFOR1; EC 1.2.7.11;; 2-oxoacid oxidoreductase (ferredoxin) (subunit 2/2) (EC 1.2.7.11) MRLSWVIGGAQGTGIDTAANIFGNAVASAGYYIYGNREYYSNIKGRHSYFSLTISDKRVRSNTQKIDILVSFDAETVFQHFYDVKDILIYNKAVETTKIDAVQSMEPELAERIKDFLTKQGYETTVKGALEYASKNNVTLIPVNYDEIAKKVADEMKVPLSVTERVKNIVGITISYKLLGLDVNYLIEAINSTFKQDLYRKMNELAVKDSYDIVESRYNLKPSSKERRRFWLDGNTAVAIGKIYGGVRFQSYYPITPASDESVYIEAHQDVLMEDPITGDKKKGTIVVVQAEDELAAINMAIGAALTGVRAATATSGPGFSLMVEGLGWAGMNEVPVVITYYIRGGPSTGLPTRTAQSDLIFPIFAGHGEFPKIVLASGDHAEAFKDAIWALNLAEKYQTPVIHLVEKTLANSYSTIPYEELELDKLKAERGKIVESGDISYKRFKFTEDGISPRAFLGKATMYYTGDEHNEEGHISEDVVNRTMMYEKRMKKLEVADKEIPEESRVKIYGDLNSRNLIITWGSPTGVLRDILEESNFDFTLLQIRMFSPFPKNLVSKLMEGRDKIITVEGNYLAQTSLLVKMYTGKDVTNSILKWNGRPFLRDELEEALIKVIKDGEKRVVLNGGI ofoB ignore SwissProt::Q96Y68,BRENDA::Q96Y68 2-oxoacid:ferredoxin oxidoreductase 1, subunit beta; OFOR1; EC 1.2.7.11;; 2-oxoacid oxidoreductase (ferredoxin) (subunit 1/2) (EC 1.2.7.11) MAAFKPQWNDWCPGCGNFGILNAEQQAIVELGVDTKNVVVVSGIGCSGKIPHFFRTPISGVHTLHGRAIAFATGIKLSNPDLVVIVNGGDGDLLGIGAGHFVAAGRRNVDMVVILHDNGVYGLTKGQASPTLKRGEKPKSLPRPNINDAVNPIALAISSGYTFVARGYAYDVKHLKELIKSAIKHKGLALIDVLQPCPTYNDINTKEWYDKRIYKLDTLPDWDPVVKKPEEVNEKIKRAIDKSLEWGDRIPIGIFYQNELVPSYEERIKANSPAYLDYTPAKQLIEKEGKLTTIIDPLLKEREVD ofoB ignore SwissProt::Q9YA11 2-oxoacid:ferredoxin oxidoreductase 1, subunit beta; OFOR1; EC 1.2.7.11 MASRGVASYRTEVWSDWCPGCGDFGILAAMQKAFAELNLDPAQTVVVSGIGCSSKTPHFINVNGVHTIHGRGIAFATGIKLANPQLKVIVNGGDGDLLGIGVAHFVALGRRNLDVTVLIHNNKVYGLTKGQASPTLRRGEKVKSLPVPNLQDAVNPIALAIASGYTFVARAYSLWVDHLKEILKAAINHKGSAVIDVLQPCVTYNDIYTAEFYKDRLYKLEDDPSWDPIVRDPSEDEEKKAAAIKKAEEWGTRIPVGVFYVNPLKDTYEERLAQRNPSYSIDNPPALQPISREDGSPIVGPDEFRKIFKRFIVNVKKL ofoB ignore SwissProt::Q9YA13 2-oxoacid:ferredoxin oxidoreductase 1, subunit alpha; OFOR1; EC 1.2.7.11 MRKDVVLLVGGAQGSGLETTMQVLAPAYASLGYGVLANREYFSNIVGRHSYIHIRVSSSGEARPLYYPADFLGAMDAETVFTHWDDIGEGAFLLYDLGTARMRLQQIASMEPDLRSRLMQQYREAGIEPFTVEKVVEYLEREKRVRVIGLSFTALFDVLIKKHGLSRAQAQRFRSSILIGAIAGLTSLDREALDLGLQRRFGSRPKVLEINRDFIASVADEVEKEYGAQLKLEPAEPKSGEYVVASGNDVVAMGKVVGGVRYQAYYPITPASDESVLLEEFEGLKIDGESLGSIAILQTEDEIAAVSSVIGAALTGARASTATSGPGFSLMVEALGWAGKNDVPMVITYYQRGGPSTGLPTRGSQSDLLFSLFASHGEFPRIILSSGDHLEAFYDAIEAYNLAERFQMPVIHLLDKFLANMVASVPFPDWKAIKIDRGKTLFKAPTGPFKRFPRDQPLADRPVLGSGAITWYTGDENDEYGHIDEDPVNRLVMYERRWKKMEIADREIPEDFRVKYYGDEDAEVLLVGWGSVKIPALEAIERLREMGVNAAYLHLRMLSPLPKRRVSEVLSRFDADRVIAVEANYLGQASKIVTMETGFMFRKYILKWTGRPVYLHELVEGVLDIVRNGRDKVVLSYGK ofoB ignore SwissProt::Q9YBX7 2-oxoacid:ferredoxin oxidoreductase 2, subunit alpha; OFOR2; EC 1.2.7.11 MVDISLIIGGPQGGGIESAGQIAIKSMVLLGYEVLGSREYHSNIMGAHSYYHLRVQQHRPRSLKLPVDGVLALDAESVFTHFRDVRPGGILVYDPGTKSTRVDAIQPMAGPLKKRLKSLFDSRGMQPVVESAVKLAEEAGARIVGLPLKEMLKTLSERTGAPVARVSRALNTLGLASMLYMLGVPVEYIEKAISLQFAGKEKVINMNVEAVRIAVDYVREAFGEPESRLPPGPRRGQTMMVATGNDLVAMGKIVGGLGVITYYPITPSSDEALYVEKHSYISIDGPLAEKLGYDKIAVAIVQMEDELASINAVLGAAAAGARASTTTSGPGFSLMNEAVSLAVEAEIPVVVTLWMRAGPSTGMPTRTGQQDLLHSIFSGHGDAPKIVLASGDHVEAFYDAIKAFNWAEEFQTPVIHLLDKYLASSMVSLAREDLDPSKVPITRGKLLDNPPADYRRYEVVEDGISPRARLGSATMVITGLEHDEYGYATEDPVMREIMMFKRERKFKVIEERIPDEEKAVLHGDSEASVALVSFGSTKQPILEALEMLRDEGVRARFAQVRLLYPFPGRLVEEMLEGVEKVIMVEQNLLGQLAMLLRAHTSIKPDSSIVKINGRPLYSFEVAGAVKRILETGEERVVVSHGS ofoB ignore SwissProt::Q9YBX8 2-oxoacid:ferredoxin oxidoreductase 2, subunit beta; OFOR2; EC 1.2.7.11 MARSWLDYKTQAWVQWCPGCGDFGILNSIYRAVSELGIDPENLAVVGGIGCSGRTTYYVKGSNFHALHGRAIPVATGVKLANPHLNVIVAGGDGDLMGIGGGHFVALGRRNLNITVLLFDNAVYGLTKGQAAPTLPAWVKTKALSMPNIHDNINPVLLAFAAGYTFIARGYAYHTQQLKELIKTAVRHRGAALVDILQPCPTYNNIMTNKWYEERIYYVDQEEGYDPIIRTPEEFQKKAPAIAAKLMEFGDRIPLGILYWNQTRESFEERLEKIMPGYMSAPPATRRIELEGKPFLHPFDIFKDRLVTP ofoB ignore SwissProt::S0EGG0 Ketoisovalerate reductase BEA2; KIVR; Beauvericin biosynthesis cluster protein 2; EC 1.2.7.7 MASQEHPNWLTALLADTRPPPKLFAWSPANIQPKLDEGIDMGSSNSDEEYDNDACVCPSTDSDQRIYIIGPGNIGRLYATHMARHPNALPITLVVHRKELLSQWAACEGVGLADLTSGKIFLNKRFTVEWWTETRPPYGPVKEVADGKKLHNVFISTKAEAGLSEADRIRRYLGRCSSVVFAQNGVCKLWPPHGPLYISHRYPSGDTPTFSACVVSHGVASAGPFLSVHAAPADAYIGPVFWASDPESPWRQPSDDFFIRHIATTPLVNTKQVSSGEIWLLQLEKLVMNAAINPLTALLRYKTGELFTSYGSDDPLARVIDKLLWQTSAVIQGLIDHETSHSVITSYAEQMSQPGTSCSVPKVRKKLTERFSQPILKAKLYAFGLKIFEHRSSMLQDIEAGRKTEIRDFNGWIVDTACFLGTGLDVSVHSGLTGLIERCERFDKMELGRALL ofoB ignore reanno::Cup4G11:RR42_RS19540 3-methyl-2-oxobutanoate:ferredoxin oxidoreductase (EC 1.2.7.7) MNAPLTPPVSDAIRRALANVSLEDKYTLERGRVYISGTQALVRLPMLQRERDRAAGLNTAGFISGYRGSPLGALDQSLWKAKQHLAAHDIVFQAGLNEDLAATSVWGSQQVNMYPDARFEGVFGMWYGKGPGVDRTSDVFKHANSAGSSRHGGVLVLAGDDHAAKSSTLAHQSEHIFKACGLPVLYPSNVQEYLDYGLHAWAMSRYSGLWVSMKCVTDVVESSASVELDPHRVEIVLPQDFILPPGGLNIRWPDPPLEQEARLLDYKWYAGLAYVRANKIDRIEIDSPHARFGIMTGGKAYLDTRQALANLGLDDETCARIGIRLYKVGCVWPLEAHGARAFAEGLQEILVVEEKRQIMEYALKEELYNWRDDVRPKVYGKFDEKDNAGGEWSIPQSNWLLPAHYELSPAIIARAIATRLDKFELPADVRARIAARIAVIEAKEKAMAVPRVAAERKPWFCSGCPHNTSTNVPEGSRALAGIGCHYMTVWMDRSTSTFSQMGGEGVAWIGQAPFAGDKHVFANLGDGTYFHSGLLAIRASIAAGVNITYKILYNDAVAMTGGQPIDGKLSVQDVANQVAAEGARKIVVVTDEPEKYSAAIKLPQGVEVHHRDELDRIQRELREVPGATILIYDQTCATEKRRRRKRGTYPDPAKRAFINDAVCEGCGDCSVKSNCLSVEPLETELGTKRQINQSSCNKDFSCVNGFCPSFVTAEGAQVKKPERHGVSMDNLPALPQPALPGLEHPYGVLVTGVGGTGVVTIGGLLGMAAHLENKGVTVLDMAGLAQKGGAVLSHVQIAAHPDQLHATRIAMGEADLVIGCDAIVSAIDDVISKTQVGRTRAIVNTAQTPTAEFIKNPKWQFPGLSAEQDVRNAVGEACDFINASGLAVALIGDAIFTNPLVLGYAWQKGWLPLSLDALVRAIELNGTAVEKNKAAFDWGRHMAHDPEHVLSLTGKLRNTAEGAEVVKLPTSSGALLEKLIAHRAEHLTAYQDAAYAQTFRDTVSRVRAAESALVGNGKPLPLTEAAARNLSKLMAYKDEYEVARLYTDPIFLDKLRNQFEGEPGRDYQLNFWLAPPLMAKRDEKGHLVKRRFGPSTMKLFGVLAKLKGLRGGVFDVFGKTAERRTERALIGEYRALLEELTRGLSAANHATAITLASLPDDIRGFGHVKDDNLAKVRTRWTALLEQFRHPETAQRVA ofoB ignore reanno::psRCH2:GFF3452 branched-chain ketoacid ferredoxin reductase (EC 1.2.7.7) active on 4-methyl-2-oxopentanoate, (S)-3-methyl-2-oxopentanoate, or 3-methyl-2-oxobutanoate MSLAEIRLDDKYRLATGHLYLTGTQALTRLPMLQHQRDQARGLNTGGFISGYRGSPLGGLDKSLWEARDYLKQHAIHFQPGVNEELAATAVWGSQQTNLFPGAKYDGVFAMWYGKGPGVDRAGDVFKHANAAGVSPQGGVLLLAGDDHGCKSSTLPHQSEHAFIAASIPVLNPANVQEILDYGIIGWELSRYSGCWVALKTIAENVDSSAVVEVDPLRVQTRIPEDFELPEDGVHIRWPDPPLAQEKRLNLYKIYAARAFARANNLNRVMLDSPNPRLGIITTGKSYLDVRQALDDLGLDEALCASVGLRVLKVGMSWPLEPVSVHEFAQGLDEILVVEEKRSIIEDQLTGQLYNWPVSKRPRVVGEFDEQGNSLLPNLSELTPAMIARVIAKRLAPIYTSDSIQARLAFLAAKEKALAARSYSTVRTPHYCSGCPHNSSTKVPEGSRASAGIGCHYMVQWMDRRTETFTQMGGEGVNWIGQAPFTDTPHMFQNLGDGTYFHSGSLAVRAAVAAGVNVTYKILYNDAVAMTGGQPIDGELRVDQLSRQIFHEGVKRIALVSDEPDKYPSRDTFAPITSFHHRRELDAVQRELREFKGVSVIIYDQTCATEKRRRRKRGKMEDPAKRAFINPAVCEGCGDCGEKSNCLAVLPLETELGRKREIDQNACNKDFSCVEGFCPSFVTVHGGGLRKPEAVAGGIEAATLPEPQHPTLDRPWNVLIPGVGGSGVTTLGALLGMAAHLEGKGCTVLDQAGLAQKFGPVTTHVRIAAKQSDIYAVRIAAGEADLLLGCDLIVAAGDESLTRLNEQISNAVVNSHESATAEFTRNPDAQVPGAAMRQAISDAVGADKTHFVDATRLATRLLGDSIATNLFLLGFAYQQGLLPISAEAIEKAIELNGVSAKLNLQAFRWGRRAVLEREAVEQLARPVDMVEPICKTLEEIVDWRVDFLTRYQSAGLARRYRQLVERVRDADSADDLALSKAVARYYFKLLAYKDEYEVARLYSEPEFRQQLEAQFEGDYKLQFHLAPAWLAKRDPVTGEPRKRELGPWVLNLFGVLAKFRFLRGTPLDPFGYGHDRRVERQLISEYEKTVDELLAQLKPTNYRTAVAIAALPEQIRGYGPVKERSIAKARQQEKLLREQLAKGDEVQSVRLFQPAA vorA curated SwissProt::P80907 Ketoisovalerate oxidoreductase subunit VorA; VOR; 2-oxoisovalerate oxidoreductase alpha chain; 2-oxoisovalerate-ferredoxin oxidoreductase subunit alpha; EC 1.-.-.- MTKKVIRKPDSLHEVFERKGGSAPTATHYCAGCGHGILHKLIGEAIDELGIQERSVMISPVGCAVFAYYYFDCGNVQVAHGRAPAVGTGISRAEDTPVVLLYQGDGDLASIGLNETIQAANRGEKMAVFFVNNTVYGMTGGQMAPTTLIGEVTVTCPGGRDPRYAGYPLHMCELLDNLQAPVFIERVSLADPKSIRKAKRAVKRALEIQRDGKGYAFVEVLSPCPTNLRQDAEGAERFLKEEMEREFPVKNFRDRSSETEPLIRSESDFSRESLDRIFQIKEDSVPDPVDDPEFREVRVKIAGFGGQGVLSMGLTLAQAACSEGRHTSWYPAYGPEQRGGTSSCGVVISGERVGSPAVDTPDVLVAFNQPSLDEFAGDVREGGIVLYDTATADFSKKENLRAIGVPALEIAKEHGTGRAANTAMLGVMMALGITGLDEESFRDAIRFTFSGKDKIIDINLKILEAGADWARKNLEGEF vorA ignore SwissProt::B6D9A7 Ketoisovalerate reductase; KIVR; EC 1.2.7.7 MPSPEHPSWLSTLLADTRPPPKLFAWSPANLDSPTAVKPDRADRGDFDPGKYPVDAPITTASEPVKRIYIVGPGNVGRLYASYMSRQRDALPITLVVHRKELLSQWVTSEGVVLADRGGKVTKNKQFDVEWWTESRPRYGPVREVADGEKLHNVFISTKADAGLGEADRLRRYLGRCSSVVFAQNGVSKLWAPYGPLYVASRYHADDAPSFSACVVNHGISAAGLFYSIHTSPSDAFIGPIFKGSAAPAHGQNKRRRLDDDFFTTYISSTPFLDTKHVSSGQLWIIQLEKLVLNAAINPLTTLLRCKTGQLFASYDSHDALTRVLDQLLWQASAVIQALINHDANIDMLTSYAETVHRLVPGSDDYGRNFANIRRKLTVRFSQPILKAKLYAFGLNIREHRSSMLQDAEAGRKTEIRDVNGWIVDMAEYLGLDLDVGIHRGLIELIEECVVLDKEELARRLL vorA ignore SwissProt::G3GBU6 Ketoisovalerate reductase BEA2; KIVR; EC 1.2.7.7 MTSQEHPNWLTALLVDTRPPPKLFAWSPANIQPKLDEGIDMGSSNSDEEYDNDACVCQSTDSDQRIYIIGPGNIGRLYATHMARHPNALPITLVVHRKELLSQWVACEGVGLADITSGKLFLNKGFTVEWWTETRPPYGPVKEVADGKKLHNVFISTKAEAGLAEADRIRRYLGRCSSVVFAQNGVCKLWPPHGPLYISHRYPSGDTPTFSACVVSHGVASAGPFLSVHAAPADAYIGPVFWASDPESPWRHPSDDFFIRHIATTPHVNTKQVSSGEIWLLQLEKLVMNAAINPLTALLRCKTGELFTSYGSDDPLALVIDKLLWQTSAVIQGLVDHKTSHSVITSYAEHMSQPGTSCSVPKVRKKLMERFSQPILKAKLGWEEDRDTGL vorA ignore SwissProt::P72578,BRENDA::P72578,metacyc::MONOMER-11911 2-oxoacid:ferredoxin oxidoreductase subunit alpha; OFOR; EC 1.2.7.11;; 2-oxoacid oxidoreductase (ferredoxin) (subunit 2/2) (EC 1.2.7.11);; 2-oxoacid:ferredoxin oxidoreductase α subunit (EC 1.2.7.11; EC 1.2.7.1; EC 1.2.7.3; EC 1.2.7.7) MRLSWVIGGAQGTGIDTAANIFGNAVASAGYYIYGNREYYSNIKGGHSYFSLTISDKRVRSNTQKIDILVSFDAETVFQHFYDVKDILIYNKAVETTKIDAVQSMEPELAERIKDFLTKQGYETTVKGALEYASKNNVTLIPVNYDEIAKKVADEMKVPLSVTERVKNIVGITISYKLLGLDVNYLIEAINSTFKQDLYRKMNELAVKDSYDIVESRYNLKPSSKERRRFWLDGNTAVAIGKIYGGVRFQSYYPITPASDESVYIEAHQDVLMEDPITGDKKKGTIVVVQAEDELAAINMAIGAALTGVRAATATSGPGFSLMVEGLGWAGMNEVPVVITYYIRGGPSTGLPTRTAQSDLIFPIFAGHGEFPKIVLASGDHAEAFKDAIWALNLAEKYQTPVIHLVEKTLANSYSTIPYEELELDKLKAERGKIVESGDISYKRFKFTEDGISPRAFLGKATMYYTGDEHNEEGHISEDVVNRTMMYEKRMKKLEVADKEIPEESRVKIYGDLNSRNLIITWGSPTGVLRDILEESNFDFTLLQIRMFSPFPKNLVSKLMEGRDKIITVEGNYLAQTSLLVKMYTGKDVTNSILKWNGRPFLRDELEEALIKVIKDGEKRVVLNGGIYTSME vorA ignore SwissProt::P72579,BRENDA::P72579,metacyc::MONOMER-11912 2-oxoacid:ferredoxin oxidoreductase subunit beta; OFOR; EC 1.2.7.11;; 2-oxoacid oxidoreductase (ferredoxin) (subunit 1/2) (EC 1.2.7.11);; 2-oxoacid:ferredoxin oxidoreductase β subunit (EC 1.2.7.11; EC 1.2.7.1; EC 1.2.7.3; EC 1.2.7.7) MAAFTPQWNDWCPGCGNFGILNAEQQAIVELGVDTKNVVVVSGIGCSGKIPHFFRTPISGVHTLHGRAIAFATGIKLSNPDLVVIVNGGDGDLLGIGAGHFVAAGRRNVDMVVILHDNGVYGLTKGQASPTLKRGEKPKSLPRPNINDAVNPIALAISSGYTFVARGYAYDVKHLKELIKSAIKHKGLALIDVLQPCPTYNDINTKEWYDKRIYKLDTLPDWDPVVKKPEEVNEKIKRAIDKSLEWGDRIPIGIFYQNELVPSYEERIKANSPAYLDYTPAKQLIEKEGKLTTIIDPLLKEREVD vorA ignore SwissProt::P80908 Ketoisovalerate oxidoreductase subunit VorB; VOR; 2-oxoisovalerate ferredoxin reductase subunit beta; 2-oxoisovalerate oxidoreductase beta chain; EC 1.2.7.7 MATQMVKGNTAVIIGAMYAGCDCYFGYPITPASEILHEASRYFPLVGRKFVQAESEEAAINMVYGAAAAGHRVMTASSGPGMSLKQEGISFLAGAELPAVIVDVMRAGPGLGNIGPEQADYNQLVKGGGHGNYRNIVLAPNSVQEMCDLTMDAFELADKYRNPVIILADAVLGQMAEPLRFPERAVEHRPDTSWAVCGSRETMKNLVTSIFLDFDELEEFNFYLQEKYAAVEENEVRYEEYMVEDAEIVLVAYGISSRVAKSAVDTARADGIKVGLLRPITLFPFPSERIRELAEGGCTFISVEMSSGQMREDIKMASGCRDVELVNRMGGNLIELRDILRKIREIAGESND vorA ignore SwissProt::P80909 Ketoisovalerate oxidoreductase subunit VorC; VOR; 2-oxoisovalerate ferredoxin reductase subunit gamma; 2-oxoisovalerate oxidoreductase gamma chain; EC 1.2.7.7 MKKAYPVINRVECKACERCIIACPRKVLYMSNKINERGYHYVEYRGEGCNGCGNCYYTCPEINAIEVHIERCEDGDTDG vorA ignore SwissProt::S0EGG0 Ketoisovalerate reductase BEA2; KIVR; Beauvericin biosynthesis cluster protein 2; EC 1.2.7.7 MASQEHPNWLTALLADTRPPPKLFAWSPANIQPKLDEGIDMGSSNSDEEYDNDACVCPSTDSDQRIYIIGPGNIGRLYATHMARHPNALPITLVVHRKELLSQWAACEGVGLADLTSGKIFLNKRFTVEWWTETRPPYGPVKEVADGKKLHNVFISTKAEAGLSEADRIRRYLGRCSSVVFAQNGVCKLWPPHGPLYISHRYPSGDTPTFSACVVSHGVASAGPFLSVHAAPADAYIGPVFWASDPESPWRQPSDDFFIRHIATTPLVNTKQVSSGEIWLLQLEKLVMNAAINPLTALLRYKTGELFTSYGSDDPLARVIDKLLWQTSAVIQGLIDHETSHSVITSYAEQMSQPGTSCSVPKVRKKLTERFSQPILKAKLYAFGLKIFEHRSSMLQDIEAGRKTEIRDFNGWIVDTACFLGTGLDVSVHSGLTGLIERCERFDKMELGRALL vorA ignore reanno::Cup4G11:RR42_RS19540 3-methyl-2-oxobutanoate:ferredoxin oxidoreductase (EC 1.2.7.7) MNAPLTPPVSDAIRRALANVSLEDKYTLERGRVYISGTQALVRLPMLQRERDRAAGLNTAGFISGYRGSPLGALDQSLWKAKQHLAAHDIVFQAGLNEDLAATSVWGSQQVNMYPDARFEGVFGMWYGKGPGVDRTSDVFKHANSAGSSRHGGVLVLAGDDHAAKSSTLAHQSEHIFKACGLPVLYPSNVQEYLDYGLHAWAMSRYSGLWVSMKCVTDVVESSASVELDPHRVEIVLPQDFILPPGGLNIRWPDPPLEQEARLLDYKWYAGLAYVRANKIDRIEIDSPHARFGIMTGGKAYLDTRQALANLGLDDETCARIGIRLYKVGCVWPLEAHGARAFAEGLQEILVVEEKRQIMEYALKEELYNWRDDVRPKVYGKFDEKDNAGGEWSIPQSNWLLPAHYELSPAIIARAIATRLDKFELPADVRARIAARIAVIEAKEKAMAVPRVAAERKPWFCSGCPHNTSTNVPEGSRALAGIGCHYMTVWMDRSTSTFSQMGGEGVAWIGQAPFAGDKHVFANLGDGTYFHSGLLAIRASIAAGVNITYKILYNDAVAMTGGQPIDGKLSVQDVANQVAAEGARKIVVVTDEPEKYSAAIKLPQGVEVHHRDELDRIQRELREVPGATILIYDQTCATEKRRRRKRGTYPDPAKRAFINDAVCEGCGDCSVKSNCLSVEPLETELGTKRQINQSSCNKDFSCVNGFCPSFVTAEGAQVKKPERHGVSMDNLPALPQPALPGLEHPYGVLVTGVGGTGVVTIGGLLGMAAHLENKGVTVLDMAGLAQKGGAVLSHVQIAAHPDQLHATRIAMGEADLVIGCDAIVSAIDDVISKTQVGRTRAIVNTAQTPTAEFIKNPKWQFPGLSAEQDVRNAVGEACDFINASGLAVALIGDAIFTNPLVLGYAWQKGWLPLSLDALVRAIELNGTAVEKNKAAFDWGRHMAHDPEHVLSLTGKLRNTAEGAEVVKLPTSSGALLEKLIAHRAEHLTAYQDAAYAQTFRDTVSRVRAAESALVGNGKPLPLTEAAARNLSKLMAYKDEYEVARLYTDPIFLDKLRNQFEGEPGRDYQLNFWLAPPLMAKRDEKGHLVKRRFGPSTMKLFGVLAKLKGLRGGVFDVFGKTAERRTERALIGEYRALLEELTRGLSAANHATAITLASLPDDIRGFGHVKDDNLAKVRTRWTALLEQFRHPETAQRVA vorA ignore reanno::psRCH2:GFF3452 branched-chain ketoacid ferredoxin reductase (EC 1.2.7.7) active on 4-methyl-2-oxopentanoate, (S)-3-methyl-2-oxopentanoate, or 3-methyl-2-oxobutanoate MSLAEIRLDDKYRLATGHLYLTGTQALTRLPMLQHQRDQARGLNTGGFISGYRGSPLGGLDKSLWEARDYLKQHAIHFQPGVNEELAATAVWGSQQTNLFPGAKYDGVFAMWYGKGPGVDRAGDVFKHANAAGVSPQGGVLLLAGDDHGCKSSTLPHQSEHAFIAASIPVLNPANVQEILDYGIIGWELSRYSGCWVALKTIAENVDSSAVVEVDPLRVQTRIPEDFELPEDGVHIRWPDPPLAQEKRLNLYKIYAARAFARANNLNRVMLDSPNPRLGIITTGKSYLDVRQALDDLGLDEALCASVGLRVLKVGMSWPLEPVSVHEFAQGLDEILVVEEKRSIIEDQLTGQLYNWPVSKRPRVVGEFDEQGNSLLPNLSELTPAMIARVIAKRLAPIYTSDSIQARLAFLAAKEKALAARSYSTVRTPHYCSGCPHNSSTKVPEGSRASAGIGCHYMVQWMDRRTETFTQMGGEGVNWIGQAPFTDTPHMFQNLGDGTYFHSGSLAVRAAVAAGVNVTYKILYNDAVAMTGGQPIDGELRVDQLSRQIFHEGVKRIALVSDEPDKYPSRDTFAPITSFHHRRELDAVQRELREFKGVSVIIYDQTCATEKRRRRKRGKMEDPAKRAFINPAVCEGCGDCGEKSNCLAVLPLETELGRKREIDQNACNKDFSCVEGFCPSFVTVHGGGLRKPEAVAGGIEAATLPEPQHPTLDRPWNVLIPGVGGSGVTTLGALLGMAAHLEGKGCTVLDQAGLAQKFGPVTTHVRIAAKQSDIYAVRIAAGEADLLLGCDLIVAAGDESLTRLNEQISNAVVNSHESATAEFTRNPDAQVPGAAMRQAISDAVGADKTHFVDATRLATRLLGDSIATNLFLLGFAYQQGLLPISAEAIEKAIELNGVSAKLNLQAFRWGRRAVLEREAVEQLARPVDMVEPICKTLEEIVDWRVDFLTRYQSAGLARRYRQLVERVRDADSADDLALSKAVARYYFKLLAYKDEYEVARLYSEPEFRQQLEAQFEGDYKLQFHLAPAWLAKRDPVTGEPRKRELGPWVLNLFGVLAKFRFLRGTPLDPFGYGHDRRVERQLISEYEKTVDELLAQLKPTNYRTAVAIAALPEQIRGYGPVKERSIAKARQQEKLLREQLAKGDEVQSVRLFQPAA vorB curated SwissProt::P80908 Ketoisovalerate oxidoreductase subunit VorB; VOR; 2-oxoisovalerate ferredoxin reductase subunit beta; 2-oxoisovalerate oxidoreductase beta chain; EC 1.2.7.7 MATQMVKGNTAVIIGAMYAGCDCYFGYPITPASEILHEASRYFPLVGRKFVQAESEEAAINMVYGAAAAGHRVMTASSGPGMSLKQEGISFLAGAELPAVIVDVMRAGPGLGNIGPEQADYNQLVKGGGHGNYRNIVLAPNSVQEMCDLTMDAFELADKYRNPVIILADAVLGQMAEPLRFPERAVEHRPDTSWAVCGSRETMKNLVTSIFLDFDELEEFNFYLQEKYAAVEENEVRYEEYMVEDAEIVLVAYGISSRVAKSAVDTARADGIKVGLLRPITLFPFPSERIRELAEGGCTFISVEMSSGQMREDIKMASGCRDVELVNRMGGNLIELRDILRKIREIAGESND vorB ignore SwissProt::B6D9A7 Ketoisovalerate reductase; KIVR; EC 1.2.7.7 MPSPEHPSWLSTLLADTRPPPKLFAWSPANLDSPTAVKPDRADRGDFDPGKYPVDAPITTASEPVKRIYIVGPGNVGRLYASYMSRQRDALPITLVVHRKELLSQWVTSEGVVLADRGGKVTKNKQFDVEWWTESRPRYGPVREVADGEKLHNVFISTKADAGLGEADRLRRYLGRCSSVVFAQNGVSKLWAPYGPLYVASRYHADDAPSFSACVVNHGISAAGLFYSIHTSPSDAFIGPIFKGSAAPAHGQNKRRRLDDDFFTTYISSTPFLDTKHVSSGQLWIIQLEKLVLNAAINPLTTLLRCKTGQLFASYDSHDALTRVLDQLLWQASAVIQALINHDANIDMLTSYAETVHRLVPGSDDYGRNFANIRRKLTVRFSQPILKAKLYAFGLNIREHRSSMLQDAEAGRKTEIRDVNGWIVDMAEYLGLDLDVGIHRGLIELIEECVVLDKEELARRLL vorB ignore SwissProt::G3GBU6 Ketoisovalerate reductase BEA2; KIVR; EC 1.2.7.7 MTSQEHPNWLTALLVDTRPPPKLFAWSPANIQPKLDEGIDMGSSNSDEEYDNDACVCQSTDSDQRIYIIGPGNIGRLYATHMARHPNALPITLVVHRKELLSQWVACEGVGLADITSGKLFLNKGFTVEWWTETRPPYGPVKEVADGKKLHNVFISTKAEAGLAEADRIRRYLGRCSSVVFAQNGVCKLWPPHGPLYISHRYPSGDTPTFSACVVSHGVASAGPFLSVHAAPADAYIGPVFWASDPESPWRHPSDDFFIRHIATTPHVNTKQVSSGEIWLLQLEKLVMNAAINPLTALLRCKTGELFTSYGSDDPLALVIDKLLWQTSAVIQGLVDHKTSHSVITSYAEHMSQPGTSCSVPKVRKKLMERFSQPILKAKLGWEEDRDTGL vorB ignore SwissProt::P72578,BRENDA::P72578,metacyc::MONOMER-11911 2-oxoacid:ferredoxin oxidoreductase subunit alpha; OFOR; EC 1.2.7.11;; 2-oxoacid oxidoreductase (ferredoxin) (subunit 2/2) (EC 1.2.7.11);; 2-oxoacid:ferredoxin oxidoreductase α subunit (EC 1.2.7.11; EC 1.2.7.1; EC 1.2.7.3; EC 1.2.7.7) MRLSWVIGGAQGTGIDTAANIFGNAVASAGYYIYGNREYYSNIKGGHSYFSLTISDKRVRSNTQKIDILVSFDAETVFQHFYDVKDILIYNKAVETTKIDAVQSMEPELAERIKDFLTKQGYETTVKGALEYASKNNVTLIPVNYDEIAKKVADEMKVPLSVTERVKNIVGITISYKLLGLDVNYLIEAINSTFKQDLYRKMNELAVKDSYDIVESRYNLKPSSKERRRFWLDGNTAVAIGKIYGGVRFQSYYPITPASDESVYIEAHQDVLMEDPITGDKKKGTIVVVQAEDELAAINMAIGAALTGVRAATATSGPGFSLMVEGLGWAGMNEVPVVITYYIRGGPSTGLPTRTAQSDLIFPIFAGHGEFPKIVLASGDHAEAFKDAIWALNLAEKYQTPVIHLVEKTLANSYSTIPYEELELDKLKAERGKIVESGDISYKRFKFTEDGISPRAFLGKATMYYTGDEHNEEGHISEDVVNRTMMYEKRMKKLEVADKEIPEESRVKIYGDLNSRNLIITWGSPTGVLRDILEESNFDFTLLQIRMFSPFPKNLVSKLMEGRDKIITVEGNYLAQTSLLVKMYTGKDVTNSILKWNGRPFLRDELEEALIKVIKDGEKRVVLNGGIYTSME vorB ignore SwissProt::P72579,BRENDA::P72579,metacyc::MONOMER-11912 2-oxoacid:ferredoxin oxidoreductase subunit beta; OFOR; EC 1.2.7.11;; 2-oxoacid oxidoreductase (ferredoxin) (subunit 1/2) (EC 1.2.7.11);; 2-oxoacid:ferredoxin oxidoreductase β subunit (EC 1.2.7.11; EC 1.2.7.1; EC 1.2.7.3; EC 1.2.7.7) MAAFTPQWNDWCPGCGNFGILNAEQQAIVELGVDTKNVVVVSGIGCSGKIPHFFRTPISGVHTLHGRAIAFATGIKLSNPDLVVIVNGGDGDLLGIGAGHFVAAGRRNVDMVVILHDNGVYGLTKGQASPTLKRGEKPKSLPRPNINDAVNPIALAISSGYTFVARGYAYDVKHLKELIKSAIKHKGLALIDVLQPCPTYNDINTKEWYDKRIYKLDTLPDWDPVVKKPEEVNEKIKRAIDKSLEWGDRIPIGIFYQNELVPSYEERIKANSPAYLDYTPAKQLIEKEGKLTTIIDPLLKEREVD vorB ignore SwissProt::P80909 Ketoisovalerate oxidoreductase subunit VorC; VOR; 2-oxoisovalerate ferredoxin reductase subunit gamma; 2-oxoisovalerate oxidoreductase gamma chain; EC 1.2.7.7 MKKAYPVINRVECKACERCIIACPRKVLYMSNKINERGYHYVEYRGEGCNGCGNCYYTCPEINAIEVHIERCEDGDTDG vorB ignore SwissProt::S0EGG0 Ketoisovalerate reductase BEA2; KIVR; Beauvericin biosynthesis cluster protein 2; EC 1.2.7.7 MASQEHPNWLTALLADTRPPPKLFAWSPANIQPKLDEGIDMGSSNSDEEYDNDACVCPSTDSDQRIYIIGPGNIGRLYATHMARHPNALPITLVVHRKELLSQWAACEGVGLADLTSGKIFLNKRFTVEWWTETRPPYGPVKEVADGKKLHNVFISTKAEAGLSEADRIRRYLGRCSSVVFAQNGVCKLWPPHGPLYISHRYPSGDTPTFSACVVSHGVASAGPFLSVHAAPADAYIGPVFWASDPESPWRQPSDDFFIRHIATTPLVNTKQVSSGEIWLLQLEKLVMNAAINPLTALLRYKTGELFTSYGSDDPLARVIDKLLWQTSAVIQGLIDHETSHSVITSYAEQMSQPGTSCSVPKVRKKLTERFSQPILKAKLYAFGLKIFEHRSSMLQDIEAGRKTEIRDFNGWIVDTACFLGTGLDVSVHSGLTGLIERCERFDKMELGRALL vorB ignore reanno::Cup4G11:RR42_RS19540 3-methyl-2-oxobutanoate:ferredoxin oxidoreductase (EC 1.2.7.7) MNAPLTPPVSDAIRRALANVSLEDKYTLERGRVYISGTQALVRLPMLQRERDRAAGLNTAGFISGYRGSPLGALDQSLWKAKQHLAAHDIVFQAGLNEDLAATSVWGSQQVNMYPDARFEGVFGMWYGKGPGVDRTSDVFKHANSAGSSRHGGVLVLAGDDHAAKSSTLAHQSEHIFKACGLPVLYPSNVQEYLDYGLHAWAMSRYSGLWVSMKCVTDVVESSASVELDPHRVEIVLPQDFILPPGGLNIRWPDPPLEQEARLLDYKWYAGLAYVRANKIDRIEIDSPHARFGIMTGGKAYLDTRQALANLGLDDETCARIGIRLYKVGCVWPLEAHGARAFAEGLQEILVVEEKRQIMEYALKEELYNWRDDVRPKVYGKFDEKDNAGGEWSIPQSNWLLPAHYELSPAIIARAIATRLDKFELPADVRARIAARIAVIEAKEKAMAVPRVAAERKPWFCSGCPHNTSTNVPEGSRALAGIGCHYMTVWMDRSTSTFSQMGGEGVAWIGQAPFAGDKHVFANLGDGTYFHSGLLAIRASIAAGVNITYKILYNDAVAMTGGQPIDGKLSVQDVANQVAAEGARKIVVVTDEPEKYSAAIKLPQGVEVHHRDELDRIQRELREVPGATILIYDQTCATEKRRRRKRGTYPDPAKRAFINDAVCEGCGDCSVKSNCLSVEPLETELGTKRQINQSSCNKDFSCVNGFCPSFVTAEGAQVKKPERHGVSMDNLPALPQPALPGLEHPYGVLVTGVGGTGVVTIGGLLGMAAHLENKGVTVLDMAGLAQKGGAVLSHVQIAAHPDQLHATRIAMGEADLVIGCDAIVSAIDDVISKTQVGRTRAIVNTAQTPTAEFIKNPKWQFPGLSAEQDVRNAVGEACDFINASGLAVALIGDAIFTNPLVLGYAWQKGWLPLSLDALVRAIELNGTAVEKNKAAFDWGRHMAHDPEHVLSLTGKLRNTAEGAEVVKLPTSSGALLEKLIAHRAEHLTAYQDAAYAQTFRDTVSRVRAAESALVGNGKPLPLTEAAARNLSKLMAYKDEYEVARLYTDPIFLDKLRNQFEGEPGRDYQLNFWLAPPLMAKRDEKGHLVKRRFGPSTMKLFGVLAKLKGLRGGVFDVFGKTAERRTERALIGEYRALLEELTRGLSAANHATAITLASLPDDIRGFGHVKDDNLAKVRTRWTALLEQFRHPETAQRVA vorB ignore reanno::psRCH2:GFF3452 branched-chain ketoacid ferredoxin reductase (EC 1.2.7.7) active on 4-methyl-2-oxopentanoate, (S)-3-methyl-2-oxopentanoate, or 3-methyl-2-oxobutanoate MSLAEIRLDDKYRLATGHLYLTGTQALTRLPMLQHQRDQARGLNTGGFISGYRGSPLGGLDKSLWEARDYLKQHAIHFQPGVNEELAATAVWGSQQTNLFPGAKYDGVFAMWYGKGPGVDRAGDVFKHANAAGVSPQGGVLLLAGDDHGCKSSTLPHQSEHAFIAASIPVLNPANVQEILDYGIIGWELSRYSGCWVALKTIAENVDSSAVVEVDPLRVQTRIPEDFELPEDGVHIRWPDPPLAQEKRLNLYKIYAARAFARANNLNRVMLDSPNPRLGIITTGKSYLDVRQALDDLGLDEALCASVGLRVLKVGMSWPLEPVSVHEFAQGLDEILVVEEKRSIIEDQLTGQLYNWPVSKRPRVVGEFDEQGNSLLPNLSELTPAMIARVIAKRLAPIYTSDSIQARLAFLAAKEKALAARSYSTVRTPHYCSGCPHNSSTKVPEGSRASAGIGCHYMVQWMDRRTETFTQMGGEGVNWIGQAPFTDTPHMFQNLGDGTYFHSGSLAVRAAVAAGVNVTYKILYNDAVAMTGGQPIDGELRVDQLSRQIFHEGVKRIALVSDEPDKYPSRDTFAPITSFHHRRELDAVQRELREFKGVSVIIYDQTCATEKRRRRKRGKMEDPAKRAFINPAVCEGCGDCGEKSNCLAVLPLETELGRKREIDQNACNKDFSCVEGFCPSFVTVHGGGLRKPEAVAGGIEAATLPEPQHPTLDRPWNVLIPGVGGSGVTTLGALLGMAAHLEGKGCTVLDQAGLAQKFGPVTTHVRIAAKQSDIYAVRIAAGEADLLLGCDLIVAAGDESLTRLNEQISNAVVNSHESATAEFTRNPDAQVPGAAMRQAISDAVGADKTHFVDATRLATRLLGDSIATNLFLLGFAYQQGLLPISAEAIEKAIELNGVSAKLNLQAFRWGRRAVLEREAVEQLARPVDMVEPICKTLEEIVDWRVDFLTRYQSAGLARRYRQLVERVRDADSADDLALSKAVARYYFKLLAYKDEYEVARLYSEPEFRQQLEAQFEGDYKLQFHLAPAWLAKRDPVTGEPRKRELGPWVLNLFGVLAKFRFLRGTPLDPFGYGHDRRVERQLISEYEKTVDELLAQLKPTNYRTAVAIAALPEQIRGYGPVKERSIAKARQQEKLLREQLAKGDEVQSVRLFQPAA vorC curated SwissProt::P80909 Ketoisovalerate oxidoreductase subunit VorC; VOR; 2-oxoisovalerate ferredoxin reductase subunit gamma; 2-oxoisovalerate oxidoreductase gamma chain; EC 1.2.7.7 MKKAYPVINRVECKACERCIIACPRKVLYMSNKINERGYHYVEYRGEGCNGCGNCYYTCPEINAIEVHIERCEDGDTDG vorC ignore SwissProt::B6D9A7 Ketoisovalerate reductase; KIVR; EC 1.2.7.7 MPSPEHPSWLSTLLADTRPPPKLFAWSPANLDSPTAVKPDRADRGDFDPGKYPVDAPITTASEPVKRIYIVGPGNVGRLYASYMSRQRDALPITLVVHRKELLSQWVTSEGVVLADRGGKVTKNKQFDVEWWTESRPRYGPVREVADGEKLHNVFISTKADAGLGEADRLRRYLGRCSSVVFAQNGVSKLWAPYGPLYVASRYHADDAPSFSACVVNHGISAAGLFYSIHTSPSDAFIGPIFKGSAAPAHGQNKRRRLDDDFFTTYISSTPFLDTKHVSSGQLWIIQLEKLVLNAAINPLTTLLRCKTGQLFASYDSHDALTRVLDQLLWQASAVIQALINHDANIDMLTSYAETVHRLVPGSDDYGRNFANIRRKLTVRFSQPILKAKLYAFGLNIREHRSSMLQDAEAGRKTEIRDVNGWIVDMAEYLGLDLDVGIHRGLIELIEECVVLDKEELARRLL vorC ignore SwissProt::G3GBU6 Ketoisovalerate reductase BEA2; KIVR; EC 1.2.7.7 MTSQEHPNWLTALLVDTRPPPKLFAWSPANIQPKLDEGIDMGSSNSDEEYDNDACVCQSTDSDQRIYIIGPGNIGRLYATHMARHPNALPITLVVHRKELLSQWVACEGVGLADITSGKLFLNKGFTVEWWTETRPPYGPVKEVADGKKLHNVFISTKAEAGLAEADRIRRYLGRCSSVVFAQNGVCKLWPPHGPLYISHRYPSGDTPTFSACVVSHGVASAGPFLSVHAAPADAYIGPVFWASDPESPWRHPSDDFFIRHIATTPHVNTKQVSSGEIWLLQLEKLVMNAAINPLTALLRCKTGELFTSYGSDDPLALVIDKLLWQTSAVIQGLVDHKTSHSVITSYAEHMSQPGTSCSVPKVRKKLMERFSQPILKAKLGWEEDRDTGL vorC ignore SwissProt::P72578,BRENDA::P72578,metacyc::MONOMER-11911 2-oxoacid:ferredoxin oxidoreductase subunit alpha; OFOR; EC 1.2.7.11;; 2-oxoacid oxidoreductase (ferredoxin) (subunit 2/2) (EC 1.2.7.11);; 2-oxoacid:ferredoxin oxidoreductase α subunit (EC 1.2.7.11; EC 1.2.7.1; EC 1.2.7.3; EC 1.2.7.7) MRLSWVIGGAQGTGIDTAANIFGNAVASAGYYIYGNREYYSNIKGGHSYFSLTISDKRVRSNTQKIDILVSFDAETVFQHFYDVKDILIYNKAVETTKIDAVQSMEPELAERIKDFLTKQGYETTVKGALEYASKNNVTLIPVNYDEIAKKVADEMKVPLSVTERVKNIVGITISYKLLGLDVNYLIEAINSTFKQDLYRKMNELAVKDSYDIVESRYNLKPSSKERRRFWLDGNTAVAIGKIYGGVRFQSYYPITPASDESVYIEAHQDVLMEDPITGDKKKGTIVVVQAEDELAAINMAIGAALTGVRAATATSGPGFSLMVEGLGWAGMNEVPVVITYYIRGGPSTGLPTRTAQSDLIFPIFAGHGEFPKIVLASGDHAEAFKDAIWALNLAEKYQTPVIHLVEKTLANSYSTIPYEELELDKLKAERGKIVESGDISYKRFKFTEDGISPRAFLGKATMYYTGDEHNEEGHISEDVVNRTMMYEKRMKKLEVADKEIPEESRVKIYGDLNSRNLIITWGSPTGVLRDILEESNFDFTLLQIRMFSPFPKNLVSKLMEGRDKIITVEGNYLAQTSLLVKMYTGKDVTNSILKWNGRPFLRDELEEALIKVIKDGEKRVVLNGGIYTSME vorC ignore SwissProt::P72579,BRENDA::P72579,metacyc::MONOMER-11912 2-oxoacid:ferredoxin oxidoreductase subunit beta; OFOR; EC 1.2.7.11;; 2-oxoacid oxidoreductase (ferredoxin) (subunit 1/2) (EC 1.2.7.11);; 2-oxoacid:ferredoxin oxidoreductase β subunit (EC 1.2.7.11; EC 1.2.7.1; EC 1.2.7.3; EC 1.2.7.7) MAAFTPQWNDWCPGCGNFGILNAEQQAIVELGVDTKNVVVVSGIGCSGKIPHFFRTPISGVHTLHGRAIAFATGIKLSNPDLVVIVNGGDGDLLGIGAGHFVAAGRRNVDMVVILHDNGVYGLTKGQASPTLKRGEKPKSLPRPNINDAVNPIALAISSGYTFVARGYAYDVKHLKELIKSAIKHKGLALIDVLQPCPTYNDINTKEWYDKRIYKLDTLPDWDPVVKKPEEVNEKIKRAIDKSLEWGDRIPIGIFYQNELVPSYEERIKANSPAYLDYTPAKQLIEKEGKLTTIIDPLLKEREVD vorC ignore SwissProt::P80908 Ketoisovalerate oxidoreductase subunit VorB; VOR; 2-oxoisovalerate ferredoxin reductase subunit beta; 2-oxoisovalerate oxidoreductase beta chain; EC 1.2.7.7 MATQMVKGNTAVIIGAMYAGCDCYFGYPITPASEILHEASRYFPLVGRKFVQAESEEAAINMVYGAAAAGHRVMTASSGPGMSLKQEGISFLAGAELPAVIVDVMRAGPGLGNIGPEQADYNQLVKGGGHGNYRNIVLAPNSVQEMCDLTMDAFELADKYRNPVIILADAVLGQMAEPLRFPERAVEHRPDTSWAVCGSRETMKNLVTSIFLDFDELEEFNFYLQEKYAAVEENEVRYEEYMVEDAEIVLVAYGISSRVAKSAVDTARADGIKVGLLRPITLFPFPSERIRELAEGGCTFISVEMSSGQMREDIKMASGCRDVELVNRMGGNLIELRDILRKIREIAGESND vorC ignore SwissProt::S0EGG0 Ketoisovalerate reductase BEA2; KIVR; Beauvericin biosynthesis cluster protein 2; EC 1.2.7.7 MASQEHPNWLTALLADTRPPPKLFAWSPANIQPKLDEGIDMGSSNSDEEYDNDACVCPSTDSDQRIYIIGPGNIGRLYATHMARHPNALPITLVVHRKELLSQWAACEGVGLADLTSGKIFLNKRFTVEWWTETRPPYGPVKEVADGKKLHNVFISTKAEAGLSEADRIRRYLGRCSSVVFAQNGVCKLWPPHGPLYISHRYPSGDTPTFSACVVSHGVASAGPFLSVHAAPADAYIGPVFWASDPESPWRQPSDDFFIRHIATTPLVNTKQVSSGEIWLLQLEKLVMNAAINPLTALLRYKTGELFTSYGSDDPLARVIDKLLWQTSAVIQGLIDHETSHSVITSYAEQMSQPGTSCSVPKVRKKLTERFSQPILKAKLYAFGLKIFEHRSSMLQDIEAGRKTEIRDFNGWIVDTACFLGTGLDVSVHSGLTGLIERCERFDKMELGRALL vorC ignore reanno::Cup4G11:RR42_RS19540 3-methyl-2-oxobutanoate:ferredoxin oxidoreductase (EC 1.2.7.7) MNAPLTPPVSDAIRRALANVSLEDKYTLERGRVYISGTQALVRLPMLQRERDRAAGLNTAGFISGYRGSPLGALDQSLWKAKQHLAAHDIVFQAGLNEDLAATSVWGSQQVNMYPDARFEGVFGMWYGKGPGVDRTSDVFKHANSAGSSRHGGVLVLAGDDHAAKSSTLAHQSEHIFKACGLPVLYPSNVQEYLDYGLHAWAMSRYSGLWVSMKCVTDVVESSASVELDPHRVEIVLPQDFILPPGGLNIRWPDPPLEQEARLLDYKWYAGLAYVRANKIDRIEIDSPHARFGIMTGGKAYLDTRQALANLGLDDETCARIGIRLYKVGCVWPLEAHGARAFAEGLQEILVVEEKRQIMEYALKEELYNWRDDVRPKVYGKFDEKDNAGGEWSIPQSNWLLPAHYELSPAIIARAIATRLDKFELPADVRARIAARIAVIEAKEKAMAVPRVAAERKPWFCSGCPHNTSTNVPEGSRALAGIGCHYMTVWMDRSTSTFSQMGGEGVAWIGQAPFAGDKHVFANLGDGTYFHSGLLAIRASIAAGVNITYKILYNDAVAMTGGQPIDGKLSVQDVANQVAAEGARKIVVVTDEPEKYSAAIKLPQGVEVHHRDELDRIQRELREVPGATILIYDQTCATEKRRRRKRGTYPDPAKRAFINDAVCEGCGDCSVKSNCLSVEPLETELGTKRQINQSSCNKDFSCVNGFCPSFVTAEGAQVKKPERHGVSMDNLPALPQPALPGLEHPYGVLVTGVGGTGVVTIGGLLGMAAHLENKGVTVLDMAGLAQKGGAVLSHVQIAAHPDQLHATRIAMGEADLVIGCDAIVSAIDDVISKTQVGRTRAIVNTAQTPTAEFIKNPKWQFPGLSAEQDVRNAVGEACDFINASGLAVALIGDAIFTNPLVLGYAWQKGWLPLSLDALVRAIELNGTAVEKNKAAFDWGRHMAHDPEHVLSLTGKLRNTAEGAEVVKLPTSSGALLEKLIAHRAEHLTAYQDAAYAQTFRDTVSRVRAAESALVGNGKPLPLTEAAARNLSKLMAYKDEYEVARLYTDPIFLDKLRNQFEGEPGRDYQLNFWLAPPLMAKRDEKGHLVKRRFGPSTMKLFGVLAKLKGLRGGVFDVFGKTAERRTERALIGEYRALLEELTRGLSAANHATAITLASLPDDIRGFGHVKDDNLAKVRTRWTALLEQFRHPETAQRVA vorC ignore reanno::psRCH2:GFF3452 branched-chain ketoacid ferredoxin reductase (EC 1.2.7.7) active on 4-methyl-2-oxopentanoate, (S)-3-methyl-2-oxopentanoate, or 3-methyl-2-oxobutanoate MSLAEIRLDDKYRLATGHLYLTGTQALTRLPMLQHQRDQARGLNTGGFISGYRGSPLGGLDKSLWEARDYLKQHAIHFQPGVNEELAATAVWGSQQTNLFPGAKYDGVFAMWYGKGPGVDRAGDVFKHANAAGVSPQGGVLLLAGDDHGCKSSTLPHQSEHAFIAASIPVLNPANVQEILDYGIIGWELSRYSGCWVALKTIAENVDSSAVVEVDPLRVQTRIPEDFELPEDGVHIRWPDPPLAQEKRLNLYKIYAARAFARANNLNRVMLDSPNPRLGIITTGKSYLDVRQALDDLGLDEALCASVGLRVLKVGMSWPLEPVSVHEFAQGLDEILVVEEKRSIIEDQLTGQLYNWPVSKRPRVVGEFDEQGNSLLPNLSELTPAMIARVIAKRLAPIYTSDSIQARLAFLAAKEKALAARSYSTVRTPHYCSGCPHNSSTKVPEGSRASAGIGCHYMVQWMDRRTETFTQMGGEGVNWIGQAPFTDTPHMFQNLGDGTYFHSGSLAVRAAVAAGVNVTYKILYNDAVAMTGGQPIDGELRVDQLSRQIFHEGVKRIALVSDEPDKYPSRDTFAPITSFHHRRELDAVQRELREFKGVSVIIYDQTCATEKRRRRKRGKMEDPAKRAFINPAVCEGCGDCGEKSNCLAVLPLETELGRKREIDQNACNKDFSCVEGFCPSFVTVHGGGLRKPEAVAGGIEAATLPEPQHPTLDRPWNVLIPGVGGSGVTTLGALLGMAAHLEGKGCTVLDQAGLAQKFGPVTTHVRIAAKQSDIYAVRIAAGEADLLLGCDLIVAAGDESLTRLNEQISNAVVNSHESATAEFTRNPDAQVPGAAMRQAISDAVGADKTHFVDATRLATRLLGDSIATNLFLLGFAYQQGLLPISAEAIEKAIELNGVSAKLNLQAFRWGRRAVLEREAVEQLARPVDMVEPICKTLEEIVDWRVDFLTRYQSAGLARRYRQLVERVRDADSADDLALSKAVARYYFKLLAYKDEYEVARLYSEPEFRQQLEAQFEGDYKLQFHLAPAWLAKRDPVTGEPRKRELGPWVLNLFGVLAKFRFLRGTPLDPFGYGHDRRVERQLISEYEKTVDELLAQLKPTNYRTAVAIAALPEQIRGYGPVKERSIAKARQQEKLLREQLAKGDEVQSVRLFQPAA