>WP_052664505.1 NCBI__GCF_000969705.1:WP_052664505.1
MDFLLSEEQQAYVASVRAFAREHVAPGILERDRAGRWDQDVWEKVAGFGLAGLPLPTEYGGSGADVLTTGLALEALAYGGMDAGLNLSLGAHLTIGAMPIALHGTEEQKQRWLPRMATGASIGAFAITEPDAGSDTAGMKTSARREGDTFVLNGTKTFITNGSLADVVTVVARTDPDAPAGNAFTAFLVETDSPGFEVSKELKKLGNRTSPTVELSFTDVAVPESAILGDEGTALWAVGFECFDWERCCMIASAVGGMQRGLDDSIRYAKQREAFGKPIATFGAIQHKLAQMAIRLENARLLQRQAAWLKDNGHEHQMQASMAKAYVGEAAVESALDAIQLHGGWGYIDEFHVERGLRDAKLATIGGGTTEIQEMVISRLLLA
>SwissProt__P45867 Acyl-CoA dehydrogenase; EC 1.3.99.- (Bacillus subtilis (strain 168))
MNFSLSEEHEMIRKLVRDFAKHEVAPTAAERDEQERFDRELFREMANLGLTGIPWPEDYGGIGSDYLAYVIAVEELSKVCASTGVTLSAHISLCSWPLFAFGTEEQKTEYLTQLALGEKIGAFALTEAGSGSDAGSMKTTAERIGDDYVLNGSKVFITNGGVADIYIVFAVTDPEKKKKGVTAFIVEKDFEGFFTGKKEKKLGIRSSPTTEIMFEDCVVPASKRLGEEGEGFKIAMKTLDGGRNGIAAQAVGIAQGALDAALQYAKERKQFGKSIAEQQGIAFKLADMATMIEASRLLTYQAAWLESSGLPYGKASAMSKLMAGDTAMKVTTEAVQIFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQRLVISRMLAD
>biolip__4irnA Crystal structure of the prolyl acyl carrier protein oxidase anab
AWNSQQIQFRKKVIQFAQQSLISDLIKNDKEEIFNRDAWQKCSEFGVHGWPIPARYGGQELDILTTAYALQGLGYGCKDNGLIFAMNAHIWACEMPLLTFGTEEQKEKYLPLLCRGGWIASHAATEPQAGSDIYSLKTTAQKDGDKYILNGYKHYVTNGTIADLFIIFATIDPSLGKEGLTTFMIEKDTPGLILSKPISKMGMRTAEVPELRLENCEVSAANRLGEEGTGLAIFNHSMEWERGFILAAAVGTMERLLEQSIRYARSHKQFGQAIGKFQLVANKLVEMKLRLENAKAYLYKVAWMKENKQMALLEASMANLYISEAWVQSCLEAIEIHGAYGYLTNTELERELRDAIASKFYSGTSEIQRVVIAKFLGL
>metacyc__MONOMER-21351 butanoyl-CoA dehydrogenase monomer (Eubacterium oxidoreducens)
MDFALTEKHEMARTLFKEFAENEVKPLAQDVDEEERFPVETVEKMAKAGFMGIPIPKEYGGQGCDILTYAMCVEELSKVCGTTGVIVSAHTSLCCDPILTYGTEEQKKKYLPDLAAGKKIGAFGLTEPGAGTDAQGQQTKAVLDGDEWVLNGSKCFITNGSYADVYIVIAVTGKVEKRGRMQKEISAFIVEKGTPGFTFGTKEKKMGIRGSATYELIFQDCRIPKENLLGQKGKGFAVAMHTLDGGRIGIAAQALGLGEGALETTINYVKERKQFGRTISQFQNTQFQLADMATKMQAAQLLVYRAARAKDTQKNYGFEAAQAKLYAAEAAMEVTTKAVQLHGGYGYIREYDVERMMRDAKITEIYEGTSEVQRMVISANLLK
>BRENDA__D2RL84 butanoyl-CoA dehydrogenase complex (NAD+, ferredoxin) (subunit 1/3) (EC 1.3.1.109); short-chain acyl-CoA dehydrogenase (subunit 1/2) (EC 1.3.8.1) (Acidaminococcus fermentans)
MDFNLTEDQQMIKDMAAEFAEKFLAPTVEERDKAHIWDRKLIDKMGEAGFCGICFPEEYGGMGLDVLSYILAVEELSKVDDGTGITLSANVSLCATPIYMFGTEEQKQKYLAPIAEGTHVGAFGLTEPSAGTDASAQQTTAVLKGDKYILNGSKIFITNGKEADTYVVFAMTDKSQGVHGISAFILEKGMPGFRFGKIEDKMGGHTSITAELIFEDCEVPKENLLGKEGEGFKIAMETLDGGRIGVAAQALGIAEGALAAAVKYSKEREQFGRSISKFQALQFMMADMATKIEAARYLVYHAAMLKNEGKPYSEAAAMAKCFASDVAMEVTTDAVQIFGGYGYTVDYPAERYMRNAKITQIYEGTNQVMRIVTSRALLRDKKK
>biolip__4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation
MDFNLTEDQQMIKDMAAEFAEKFLAPTVEERDKAHIWDRKLIDKMGEAGFCGICFPEEYGGMGLDVLSYILAVEELSKVDDGTGITLSANVSLCATPIYMFGTEEQKQKYLAPIAEGTHVGAFGLTEPSAGTDASAQQTTAVLKGDKYILNGSKIFITNGKEADTYVVFAMTDKSQGVHGISAFILEKGMPGFRFGKIEDKMGGHTSITAELIFEDCEVPKENLLGKEGEGFKIAMETLDGGRIGVAAQALGIAEGALAAAVKYSKEREQFGRSISKFQALQFMMADMATKIEAARYLVYHAAMLKNEGKPYSEAAAMAKCFASDVAMEVTTDAVQIFGGYGYTVDYPAERYMRNAKITQIYEGTNQVMRIVTSRALLRD
>SwissProt__P45857 Acyl-CoA dehydrogenase; EC 1.3.99.- (Bacillus subtilis (strain 168))
MHVTQEQVMMRKMVRDFARKEIAPAAEIMEKTDEFPFQLIKKMGKHGLMGIPVPEQYGGAGADVVSYILAIHEISRISAAVGVILSVHTSVGTNPILYFGNEEQKMKYIPNLASGDHLGAFALTEPHSGSDAGSLRTTAIKKNGKYLLNGSKIFITNGGAADIYITFALTAPDQGRHGISAFIVEKNTPGFTVGKKERKLGLYGSNTTELIFDNAEVPEANLLGKEGDGFHIAMANLNVGRIGIAAQALGIAEAALEHAVDYAKQRVQFGRPIAANQGISFKLADMATRAEAARHLVYHAADLHNRGLNCGKEASMAKQFASDAAVKAALDAVQIYGGYGYMKDYPVERLLRDAKVTQIYEGTNEIQRLIISKYLLGGT
>biolip__1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
IDFSLTEEQRQLQALARRFAKEVILPVAQEYDEKEEVPWPVIEKLHEVGLLNAIIPEEYGGMGLKMLDEVIVGEELAYACMGIYTIPMASDLGITPVLLAGTEEQKERFLRPLTEKPALAAFALSEPGNGSDAAALKTRAIRQGDHYVLNGTKMWISNGGEAEWVVVFATVNPELRHKGVVALVVERGTPGFKAIKIHGKMGQRASGTYELVFEDVKVPVENRLGEEGEGFKIAMQTLNKTRIPVAAGSVGVARRALDEARKYAKEREAFGEPIANFQAIQFKLVDMLIGIETARMYTYYAAWLADQGLPHAHASAIAKAYASEIAFEAANQAIQIHGGYGYVREFPVEKLLRDVKLNQIYEGTNEIQRLIIARHILAA
>PDB_1ukw_B Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
IDFSLTEEQRQLQALARRFAKEVILPVAQEYDEKEEVPWPVIEKLHEVGLLNAIIPEEYGGMGLKMLDEVIVGEELAYAC
MGIYTIPMASDLGITPVLLAGTEEQKERFLRPLTEKPALAAFALSEPGNGSDAAALKTRAIRQGDHYVLNGTKMWISNGG
EAEWVVVFATVNPELRHKGVVALVVERGTPGFKAIKIHGKMGQRASGTYELVFEDVKVPVENRLGEEGEGFKIAMQTLNK
TRIPVAAGSVGVARRALDEARKYAKEREAFGEPIANFQAIQFKLVDMLIGIETARMYTYYAAWLADQGLPHAHASAIAKA
YASEIAFEAANQAIQIHGGYGYVREFPVEKLLRDVKLNQIYEGTNEIQRLIIARHILAA
>CharProtDB__CH_091788 acyl-CoA dehydrogenase (Bacillus subtilis)
MHVTQEQVMMRKMVRDFARKEIAPAAEIMEKTDEFPFQLIKKMGKHGLMGIPVPEQYGGAGADVVSYILAIHEISRISAAVGVILSVHTSVGTNPILYFGNEEQKMKYIPNLASGDHLGAFALTEPHSGSDAGSLRTTAIKKNGKYLLNGSKIFITNGGAADIYITFALTAPDQGRHGISAFIVEKNTPGFTVGKKERKLGLYGSNTTELIFDNAEVPEANLLGKEGDGFHIAMANLNVGRIGIAAQALGIAEAALEHAVDYAKQRVQFGRPIAANQGISFKLADMATRAEAARHLVYHAADLHNRGLNCGKEASMAKQFASDAAVKALDAVQIYGGYGYMKDYPVERLLRDAKVTQIYEGTNEIQRLIISKYLLGGT
>BRENDA__Q18AQ1 butanoyl-CoA dehydrogenase complex (NAD+, ferredoxin) (subunit 3/3) (EC 1.3.1.109); short-chain acyl-CoA dehydrogenase (EC 1.3.8.1) (Clostridioides difficile)
MDLNSKKYQMLKELYVSFAENEVKPLATELDEEERFPYETVEKMAKAGMMGIPYPKEYGGEGGDTVGYIMAVEELSRVCGTTGVILSAHTSLGSWPIYQYGNEEQKQKFLRPLASGEKLGAFGLTEPNAGTDASGQQTTAVLDGDEYILNGSKIFITNAIAGDIYVVMAMTDKSKGNKGISAFIVEKGTPGFSFGVKEKKMGIRGSATSELIFEDCRIPKENLLGKEGQGFKIAMSTLDGGRIGIAAQALGLAQGALDETVKYVKERVQFGRPLSKFQNTQFQLADMEVKVQAARHLVYQAAINKDLGKPYGVEAAMAKLFAAETAMEVTTKAVQLHGGYGYTRDYPVERMMRDAKITEIYEGTSEVQRMVISGKLLK
>biolip__5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
MHVQEQVMMRKMVRDFARKEIAPAAEIMEKTDEFPFQLIKKMGKHGLMGIPVPEQYGGAGADVVSYILAIHEISRISAAVGVILSVHTSVGTNPILYFGNEEQKMKYIPNLASGDHLGAFALTEPHSGSDAGSLRTTAIKKNGKYLLNGSKIFITNGGAADIYITFALTAPDQGRHGISAFIVEKNTPGFTVGKKERKLGLYGSNTTELIFDNAEVPEANLLGKEGDGFHIAMANLNVGRIGIAAQALGIAEAALEHAVDYAKQRVQFGRPIAANQGISFKLADMATRAEAARHLVYHAADLHNRLNCGKEASMAKQFASDAAVKALDAVQIYGGYGYMKDYPVERLLRDAKVTQIYEGTNEIQRLIISKYLLG
>PDB_1egc_A Structure of t255e, e376g mutant of human medium chain acyl-coa dehydrogenase complexed with octanoyl-coa
LGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAY
GCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITN
GGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAM
GAFDKERPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYA
SIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGTSQIQRLIVAREHIDKYKN
>biolip__4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
HMDELYTEDQRMIRDAARAFATEMLAPNAAQWDHDAHLPDAIVAQLGELGLLGMIVPQELGGSYTDYVAYALAMEEVAAGDAACATMMSVHNSVGCGPILGFGTPAQKDRWLADMAAGRVIGAFCLTEPHAGSEANNLRTRAELRDGQWVLNGAKQFVTNGQRAGVAIVFAMTDPEAGKRGISAFLVPTDTPGFIVGKPEKKMGIRASDTCPITFENCAIPEDNLLGNRGEGLKIALSNLEGGRIGIAAQALGIARAAFDKARRYAGERVQFGKPIAEHQAIQQKLADMAVQINAARLLVHHAAKLRTAGLPCLSEASQAKLFASEMAERVCSDAIQIHGGYGYLVDYEVERHYRDARITQIYEGTSEVQRMVIARQL
>SwissProt__P12007 Isovaleryl-CoA dehydrogenase, mitochondrial; IVD; Butyryl-CoA dehydrogenase; EC 1.3.8.4; EC 1.3.8.1 (Rattus norvegicus (Rat))
MATAVRLLGRRVSSWRLRPLPSPLAVPQRAHSMLPVDDDINGLNEEQKQLRHTISKFVQENLAPKAQEIDQSNDFKNLREFWKQLGSLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASAAVGLSYGAHSNLCINQIVRNGNEAQKEKYLPKLISGEFIGALAMSEPNAGSDVVSMRLKAEKKGDHYVLNGNKFWITNGPDADVLVVYAKTDLTAVPASRGITAFIVEKDMPGFSTSKKLDKLGMRGSNTCELVFEDCKVPAANILSQESKGVYVLMSGLDLERLVLAGGPLGIMQAVLDHTIPYLHVREAFGQKIGQFQLMQGKMADMYTRLMACRQYVYNVARACDEGHITAKDCAGVILYTAECATQVALDGIQCLGGNGYINDFPMGRFLRDAKLYEIGGGTSEVRRLVIGRAFNADFR
>reanno__pseudo13_GW456_L13_PfGW456L13_2983 2-methylbutanoyl-CoA dehydrogenase (EC 1.3.8.5) (Pseudomonas fluorescens GW456-L13)
MIPNDDQQQIRDMARDFAQERLKPFAAEWDREHRFPKEAIGEMAGLGFFGMLVPEQWGGCDTGYLAYAMALEEIAAGDGACSTIMSVHNSVGCVPILNYGTDEQKERFLKPLASGAMLGAFALTEPQAGSDASGLKTRARLEGDHYVLNGCKQFITSGQNAGVVIVFAVTDPSAGKRGISAFIVPTDSPGYKVARVEDKLGQHASDTCQILFEDVKVPLANRLGEEGEGYRIALANLEGGRVGIASQSVGMARAAFEAARDYARERESFGKPIIEHQAVAFRLADMATQIAVARQMVHYAAALRDSGKPALVEASMAKLFASEMAEKVCSSALQTLGGYGYLNDFPVERIYRDVRVCQIYEGTSDIQRMVISRNL
>biolip__3mddA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate
GFSFELTEQQKEFQATARKFAREEIIPVAAEYDRTGEYPVPLLKRAWELGLMNTHIPESFGGLGLGIIDSCLITEELAYGCTGVQTAIEANTLGQVPLIIGGNYQQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPASKAFTGFIVEADTPGVQIGRKEINMGQRCSDTRGIVFEDVRVPKENVLTGEGAGFKIAMGTFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLLAEHQGISFLLADMAMKVELARLSYQRAAWEIDSGRRNTYYASIAKAYAADIANQLATDAVQVFGGNGFNTEYPVEKLMRDAKIYQIYEGTAQIQRIIIAREHIGRYK
>SwissProt__P41367 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; EC 1.3.8.7 (Sus scrofa (Pig))
MAAMFRRSCRVLRSLSHFGWRSQHTKAVPQCEPGSGFSFELTEQQKEFQATARKFAREEIIPVAAEYDRTGEYPVPLLKRAWELGLMNTHIPESFGGLGLGIIDSCLITEELAYGCTGVQTAIEANTLGQVPLIIGGNYQQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPASKAFTGFIVEADTPGVQIGRKEINMGQRCSDTRGIVFEDVRVPKENVLTGEGAGFKIAMGTFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLLAEHQGISFLLADMAMKVELARLSYQRAAWEIDSGRRNTYYASIAKAYAADIANQLATDAVQVFGGNGFNTEYPVEKLMRDAKIYQIYEGTAQIQRIIIAREHIGRYKN
>PDB_3mde_A Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate
GFSFELTEQQKEFQATARKFAREEIIPVAAEYDRTGEYPVPLLKRAWELGLMNTHIPESFGGLGLGIIDSCLITEELAYG
CTGVQTAIEANTLGQVPLIIGGNYQQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNG
GKANWYFLLARSDPDPKAPASKAFTGFIVEADTPGVQIGRKEINMGQRCSDTRGIVFEDVRVPKENVLTGEGAGFKIAMG
TFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLLAEHQGISFLLADMAMKVELARLSYQRAAWEIDSGRRNTYYAS
IAKAYAADIANQLATDAVQVFGGNGFNTEYPVEKLMRDAKIYQIYEGTAQIQRIIIAREHIGRYK
>PDB_1udy_A Medium-chain acyl-coa dehydrogenase with 3-thiaoctanoyl-coa
GFSFELTEQQKEFQATARKFAREEIIPVAAEYDRTGEYPVPLLKRAWELGLMNTHIPESFGGLGLGIIDSCLITEELAYG
CTGVQTAIEANTLGQVPLIIGGNYQQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNG
GKANWYFLLARSDPDPKAPASKAFTGFIVEADTPGVQIGRKEINMGQRCSDTRGIVFEDVRVPKENVLTGEGAGFKIAMG
TFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLLAEHQGISFLLADMAMKVELARLSYQRAAWEIDSGRRNTYYAS
IAKAYAADIANQLATDAVQVFGGNGFNTEYPVEKLMRDAKIYQIYEGTAQIQRIIIAREHIGRYK
>PDB_1ivh_A Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity
VDDAINGLSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKNLREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEE
ISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKF
WITNGPDADVLIVYAKTDLAAVPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVY
VLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTA
KDCAGVILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRAFNAD
>biolip__8sgrA Human liver mitochondrial isovaleryl-coa dehydrogenase
SLLPVDDAINGLSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKNLREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAVPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRAFNADFH
>SwissProt__P45952 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; EC 1.3.8.7 (Mus musculus (Mouse))
MAAAFRRGCRVLRSVSHFECRTQHSKAAHKQEPGLGFSFELTEQQKEFQATARKFAREEIIPVAPEYDKSGEYPFPLIKRAWELGLINAHIPESCGGLGLGTFDACLITEELAYGCTGVQTAIEANSLGQMPVILAGNDQQKKKYLGRMTEQPMMCAYCVTEPSAGSDVAAIKTKAEKKGDEYVINGQKMWITNGGKANWYFLLARSNPDPKVPASKAFTGFIVEADTPGIHIGKKELNMGQRCSDTRGIAFEDVRVPKENVLIGEGAGFKIAMGAFDRTRPTVAAGAVGLAQRALDEATKYALDRKTFGKLLVEHQGVSFLLAEMAMKVELARLSYQRAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQIFGGYGFNTEYPVEKLMRDAKIYQIYEGTAQIQRLIIAREHIEKYKN
>SwissProt__P26440 Isovaleryl-CoA dehydrogenase, mitochondrial; IVD; Butyryl-CoA dehydrogenase; EC 1.3.8.4; EC 1.3.8.1 (Homo sapiens (Human))
MAEMATATRLLGWRVASWRLRPPLAGFVSQRAHSLLPVDDAINGLSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKNLREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAVPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRAFNADFH
>metacyc__MONOMER-17424 short-chain acyl-CoA dehydrogenase monomer (EC 1.3.8.1) (Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440))
MLVNDEQQQIADAVRAFAQERLKPFAEQWDKDHRFPKEAIDEMAELGLFGMLVPEQWGGSDTGYVAYAMALEEIAAGDGACSTIMSVHNSVGCVPILRFGNEQQKEQFLTPLATGAMLGAFALTEPQAGSDASSLKTRARLEGDHYVLNGSKQFITSGQNAGVVIVFAVTDPEAGKRGISAFIVPTDSPGYQVARVEDKLGQHASDTCQIVFDNVQVPVANRLGAEGEGYKIALANLEGGRIGIASQAVGMARAAFEVARDYANERQSFGKPLIEHQAVAFRLADMATKISVARQMVLHAAALRDAGRPALVEASMAKLFASEMAEKVCSDALQTLGGYGYLSDFPLERIYRDVRVCQIYEGTSDIQRMVIARNL
>biolip__2a1tC Structure of the human mcad:etf e165betaa complex
GLGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDKYKN
>metacyc__HS04089-MONOMER mitochondrial medium-chain acyl-CoA dehydrogenase monomer (EC 1.3.8.7) (Homo sapiens)
MAAGFGRCCRVLRSISRFHWRSQHTKANRQREPGLGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDKYKN
>biolip__4iv6B X-ray crystal structure of an isovaleryl-coa dehydrogenase from mycobacterium smegmatis
ALTAEEETIVKTVHDFVEKQVKPVVRELEHANTYPEELIETMKEIGIFGLAIPEPYGFGAVSMPCYVQVAEELARGWMSLAGAMGGHTVVSKLLLLFGTEEQKQKYLPRMATGELRATMALTEPGGGSDLQAMRTVARRDGDDYVINGSKTWISNARRSDLVALMCKTDPDAQPAHKGVSILLVEKVPGFDVSRDLPKLGYKGVESCELNFTDARVPVSSLLGDDEGRGFAQMMKGLEVGRLQVAARATGVARAAFEDALRYSQERESFGKPIWQHQSVGNMLADMGTKLYAARSLLLSAAEKFDAGQRCDMEAGMAKLFASETAMQIALDAVRVHGGYGYSTEYDVERYFRDAPLMIVGEGTNEIQRNVIAKQLVARGGLDI
>SwissProt__Q9VSA3 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; EC 1.3.8.7 (Drosophila melanogaster (Fruit fly))
MAFLNKLAAPALRQLVSQSRAYAAVSHVSPNGTSFALTEDQLQLQELARKFTREEIIPVAAQYDKSGEYPWPIIKKAWELGLMNNHIPADIGGLDLDVFTTCLSAEELAYGCTGIMTALEASGLGQTPVILSGNKEQKKKYLGRLLEEPLVAAYCVTEPGAGSDVSGIKTRAEKKGDEWVINGQKMWITNGGVANWYFVLARTNPDPKCPPSKAFTGFIVERDSPGLTPGRKELNMGQRASDTRGITFEDVRVPKENVLIGEGAGFKIAMGTFDKTRPPVAAGAVGLAQRCLDEALKYALERKTFGVPIAYHQAVQFMLADMAIGVETSRLAWRLSAWEIDQGRRNSYYASIAKCHAADMANKIASDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISRNMYEAAKGQA
>BRENDA__B5UB85 isovaleryl-CoA dehydrogenase (EC 1.3.8.4) (Bombyx mori)
MVVRLCVRRLLRKTANKTGHRCISHYPIDDHVFGLSEEQQQLRKMVFDFAQKELAPKAAEIDKENNFKELRPFWKKLGDLGLLGITASSDYGGTGGKYSDHCVIMEELSRASGGIALSYGAHSNLCVNQINRNGTEEQKSKYLPKLCSGEHIGALAMSEPGSGSDVVSMKLRAEKKGDYYVLNGNKFWITNGPDADVLVVYAKTNWSTSKQQHGISAFLIEKDYPGFSTAQKLDKLGMRGSNTGELVFEDCKVPAANLLGQENKGVYVLMSGLDLERLVLAAGPVGLMQAAIDTAFLYAHTRKQFGKNIGEFQLIQGKMADMYTTLSACRSYLYNVAKACDNGHVNSKDCAGVILYCAEKATQVALDAIQILGGNGYINDYPTGRILRDAKLYEIGAGTSEVRRMLIGRALNNEYK
>SwissProt__P08503 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; EC 1.3.8.7 (Rattus norvegicus (Rat))
MAAALRRGYKVLRSVSHFECRAQHTKPSLKQEPGLGFSFELTEQQKEFQTIARKFAREEIIPVAPDYDKSGEYPFPLIKRAWELGLINTHIPESCGGLGLGTFDACLITEELAYGCTGVQTAIEANSLGQMPVIIAGNDQQKKKYLGRMTEQPMMCAYCVTEPSAGSDVAGIKTKAEKKGDEYVINGQKMWITNGGKANWYFVLTRSNPDPKVPASKAFTGFIVEADTPGIHIGKKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDRTRPTVAAGAVGLAQRALDEATKYALDRKTFGKLLVEHQGVSFLLAEMAMKVELARLSYQRAAWEVDSGRRNTYFASIAKAFAGDIANQLATDAVQIFGGYGFNTEYPVEKLMRDAKIYQIYEGTAQIQRLIIAREHIEKYKN
>SwissProt__Q22347 Probable medium-chain specific acyl-CoA dehydrogenase 10, mitochondrial; MCAD; EC 1.3.8.7 (Caenorhabditis elegans)
MLSRIATSSLGLSRSATGVIATQSRQISFDLSETQKEIQDAALKFSKDVLVPNAAKFDESGEFPWEIVRQAHSLGLMNPQIPEKYGGPGMTTLETALIVEALSYGCTGIQLGIMGPSLAIAPVYISGNEEQKKKYLGALAAEPIIASYCVTEPGAGSDVNGVKTKCEKKGDEYIINGSKAWITGGGHAKWFFVLARSDPNPKTPAGKAFTAFIVDGDTPGITRGKKEKNMGQRCSDTRVITFEDVRVPAENVLGAPGAGFKVAMEAFDMTRPGVAAGALGLSWRCLDESAKYALERKAFGTVIANHQAVQFMLADMAVNLELARLITYKSANDVDNKVRSSYNASIAKCFAADTANQAATNAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRIVISRMLLGHFAQNGTSRI
>reanno__pseudo1_N1B4_Pf1N1B4_4787 2-methylbutanoyl-CoA dehydrogenase (EC 1.3.8.5) (Pseudomonas fluorescens FW300-N1B4)
MIPNDEQLQISDAARQFAQERLKPFAAEWDREHRFPKEAIGEMAGLGFFGMLVPEQWGGCDTGYLAYAMALEEIAAGDGACSTIMSVHNSVGCVPILKFGNDDQKERFLKPLASGAMLGAFALTEPQAGSDASSLKTRARLDGDHYVLNGCKQFITSGQNAGVVIVFAVTDPSAGKRGITALIVPTDSPGYKVARVEDKLGQHASDTCQILFEDVKVPVANRLGEEGEGYKIALANLEGGRVGIASQSVGMARAAFEAARDYARERESFGKPIIEHQAVAFRLADMATQIAVARQMVHYAAALRDSGKPALVEASMAKLFASEMAEKVCSSALQTLGGYGYLNDFPLERIYRDVRVCQIYEGTSDIQRMVISRNL
>SwissProt__P52042 Acyl-CoA dehydrogenase, short-chain specific; Butyryl-CoA dehydrogenase; SCAD; EC 1.3.8.1 (Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W))
MDFNLTREQELVRQMVREFAENEVKPIAAEIDETERFPMENVKKMGQYGMMGIPFSKEYGGAGGDVLSYIIAVEELSKVCGTTGVILSAHTSLCASLINEHGTEEQKQKYLVPLAKGEKIGAYGLTEPNAGTDSGAQQTVAVLEGDHYVINGSKIFITNGGVADTFVIFAMTDRTKGTKGISAFIIEKGFKGFSIGKVEQKLGIRASSTTELVFEDMIVPVENMIGKEGKGFPIAMKTLDGGRIGIAAQALGIAEGAFNEARAYMKERKQFGRSLDKFQGLAWMMADMDVAIESARYLVYKAAYLKQAGLPYTVDAARAKLHAANVAMDVTTKAVQLFGGYGYTKDYPVERMMRDAKITEIYEGTSEVQKLVISGKIFR
>reanno__WCS417_GFF2715 2-methylbutanoyl-CoA dehydrogenase (EC 1.3.8.5) (Pseudomonas simiae WCS417)
MLPNEEQLQISDAARQFAQERLKPFAAEWDREHRFPKEAIGEMAELGFFGMLVPEQWGGCDTGYLAYAMALEEIAAGDGACSTIMSVHNSVGCVPVLKFGNDQQKEQFLKPLASGAMLGAFALTEPQAGSDASSLKTRARLEGDHYVLNGCKQFITSGQNAGVVIVFAVTDPAAGKRGISAFIVPTDSPGYSVARVEDKLGQHASDTCQILFEDVKVPVANRLGEEGEGYKIALANLEGGRVGIASQAVGMARAAFEAARDYARERESFGKPIIEHQAVAFRLADMATQIAVARQMVHYAAALRDSGKPALVEASMAKLFASEMAEKVCSAALQTLGGYGYLSDFPLERIYRDVRVCQIYEGTSDIQRMVISRNL
>metacyc__MONOMER-11693 acyl-CoA dehydrogenase subunit (EC 1.3.8.4; EC 1.3.8.5) (Streptomyces avermitilis)
MDHRLTPELEELRRTVEEFAHDVVAPKIGDFYERHEFPYEIVREMGRMGLFGLPFPEEYGGMGGDYLALGIALEELARVDSSVAITLEAGVSLGAMPIHLFGTDAQKAEWLPRLCSGEILGAFGLTEPDGGSDAGATRTTARLDESTNEWVINGTKCFITNSGTDITGLVTVTAVTGRKPDGKPLISSIIVPSGTPGFTVAAPYSKVGWNASDTRELSFADVRVPAANLLGEQGRGYAQFLRILDEGRIAISALATGLAQGCVDESVKYAGERHAFGRNIGAYQAIQFKIADMEMKAHMARVGWRDAASRLVAGEPFKKEAAIAKLYSSTVAVDNAREATQIHGGYGFMNEYPVARMWRDSKILEIGEGTSEVQRMLIARELGLVG
>reanno__pseudo3_N2E3_AO353_25680 2-methylbutanoyl-CoA dehydrogenase / butanoyl-CoA dehydrogenase / isobutyryl-CoA dehydrogenase (EC 1.3.8.1; EC 1.3.8.5) (Pseudomonas fluorescens FW300-N2E3)
MLPTDEQLQISDAARQFAQERLKPFAAEWDREHRFPKEAIGEMAELGFFGMLVPEQWGGCDTGYLAYAMALEEIAAGDGACSTIMSVHNSVGCVPILKFGNDDQKERFLKPLASGAMLGAFALTEPQAGSDASSLKTRARLNGDHYVLNGCKQFITSGQNAGVVIVFAVTDPSAGKRGISAFIVPTDSPGYKVARVEDKLGQHASDTCQILFEDVQVPVANRLGEEGEGYKIALANLEGGRVGIASQSVGMARAAFEAARDYARERESFGKPIIEHQAVAFRLADMATQIAVARQMVHYAAALRDSGKPALVEASMAKLFASEMAEKVCSTALQTLGGYGYLSDFPLERIYRDVRVCQIYEGTSDIQRMVISRNL
>SwissProt__O54143 L-prolyl-[peptidyl-carrier protein] dehydrogenase; EC 1.3.8.14 (Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145))
MNFDFDAGFDTETRELRDMVVRFARRELDSSGRFDDAEDFRRRWLLAGKQGLTGTTVPGEYGGSGLDAVSAAATMEALGYGCADTGFAFSVAAHLFAAVMPIVEFGTGEQRAAWLPALCSGERIAAHAITEPEAGSDALHLRTRARPVDDGHVLSGSKCFITNAPVADVFVVQAATDPRGGFFGLTTFLVEASTPGLTVGRPYDKVGLRGSPTADVHFDDCYVPAGAVLGAEGSGASIFSSSMKWERTCLFAAYLGAMRRVLESTVDHVRDREQFGSPIGGFQAVSHRIVDMLGRYEGARLLLYRAARSLSDGTADEVGPALAKIAVSEAAVQLGLDAVQLRGGLGIMDGEAETLLRDALPARIFSGTNEIQKNNVARALGLGRRRPAARR
>reanno__pseudo6_N2E2_Pf6N2E2_1146 2-methylbutanoyl-CoA dehydrogenase (EC 1.3.8.5) (Pseudomonas fluorescens FW300-N2E2)
MLATEEQTQIRDMARQFAEERLKPFAAEWDREHRFPREAIDEMAELGFFGMLVPEQWGGCDTGYLAYAMTLEEIAAGDGACSTIMSVHNSVGCVPILKFGNDEQKAKFLTPLASGAMLGAFALTEPQAGSDASSLKTRARLEGDHYVLNGCKQFITSGQNAGVVIVFAVTDPSAGKRGISAFIVPTDSPGYSVARVEDKLGQHASDTCQILFEDLKVPVGNRLGEEGEGYKIALANLEGGRVGIAAQAVGMARAAFEAARDYARERSSFGKPIIEHQAVAFRLADMATQIAVARQMVHYAAALRDSGQPALVEASMAKLFASEMAEKVCSMALQTLGGYGYLNDFPLERIYRDVRVCQIYEGTSDIQRMVISRNL
>metacyc__MONOMER-18830 L-prolyl-S-[peptidyl-carrier protein] dehydrogenase (EC 1.3.8.14) (Serratia marcescens)
MDFNLSSEQQALSESAQRFAREVLDQDAHARLSRQVLSLDLWQQAAAYGFTRAPVTTAFGGLGMNALDTALMIEALGKGSRDIGMSFSLCAHLCACVIPLSRFGSEALKARYLEALAAGKLIAANAATEPDAGSDIYAMKSTAQPCEGGYRLNGNKIFITNAPIADIFIVYAKTHPEHGFMGVSAFVLEKGMPGLNVGAVSPKDCLSNCPWSELTFNDVFIPETQRIGMPGAGGAIFHDSMIWEKGCLSALFIGAMERVFDSALDYAKQRRQFGKAIGQFQSVSNRIIDMKLRLEQCRLMLYRACWKHDRGQDAEIDIAMSKLLISEYAVQSALDAIQIFGGAGMDQELGLVRHLLNVIPSRIFSGTNEIQKEIVARKLGLRGGA
>reanno__psRCH2_GFF2397 2-methylbutanoyl-CoA dehydrogenase (EC 1.3.8.5) (Pseudomonas stutzeri RCH2)
MLPNEDQNAIAEMARQFAQERLKPFAEQWSREHRYPAEAIGEMAALGFFGMLVPEQWGGSDTGYLAYAMALEEIAAGDGACSTIMSVHNSVGCVPILRFGNEQQKSDFLTPLARGEQIGAFALTEPQAGSDASSLRTRARRDGDHYVLNGAKQFITSGKHAGTVIVFAVTDPDAGKGGISAFIVPTDSPGYQVVRVEDKLGQHASDTCQIAFEDLRVPVANRLGEEGEGYRIALANLEGGRIGIAAQAVGMARAAFEAARDYARDRETFGKPIIEHQAVAFRLADMATQIAVARQMVHHAAALREVGRPALVEASMAKLFASEMAEKVCSAAIQTLGGYGYLADFPVERIYRDVRVCQIYEGTSDIQRLVISRNLGGPV
>reanno__pseudo5_N2C3_1_AO356_26355 2-methylbutanoyl-CoA dehydrogenase (EC 1.3.8.5) (Pseudomonas fluorescens FW300-N2C3)
MLPTEEQTQIRDMARQFAQERLKPFAAEWDREHRFPREAIAEMAELGFFGMLVPEQWGGCDTGYLAYAMTLEEIAAGDGACSTIMSVHNSVGCVPILKFGNDEQKAKFLTPLASGAMLGAFALTEPQAGSDASSLKTRARLEGDHYVLNGCKQFITSGQNAGVVIVFAVTDPSAGKRGISAFIVPTDSPGYSVARVEDKLGQHASDTCQILFEEVKVPVGNRLGEEGEGYKIALANLEGGRVGIAAQAVGMARAAFEAARDYARERSSFGKPIIEHQAVAFRLADMATQIAVARQMVHYAAALRDSGQPALVEASMAKLFASEMAEKVCSMALQTLGGYGYLNDFPLERIYRDVRVCQIYEGTSDIQRMVISRNL
>metacyc__MONOMER-21930 5-carboxy-2-pentenoyl-CoA reductase (Thermobifida fusca (strain YX))
MSDFDLYRPTEEHEALREAIRSVAEDKIAPHAADVDEQSRFPQEAYEALRASDFHAPHVAEEYGGVGADALATCIVIEEIARVCASSSLIPAVNKLGSMPLILSGSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRDGDDWILNGQKSWITNAGISKYYTVMAVTDPDGPRGRNISAFVVHIDDPGFSFGEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVGEGLRTALRTLDHTRVTIGAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYVAAAKSERDDADLSFYGAAAKCFASDVAMEITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMARQLLKK
>biolip__7w0jE Acyl-coa dehydrogenase, tfu_1647
DFDLYRPTEEHEALREAIRSVAEDKIAPHAADVDEQSRFPQEAYEALRASDFHAPHVAEEYGGVGADALATCIVIEEIARVCASSSLIPAVNKLGSMPLILSGSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRDGDDWILNGQKSWITNAGISKYYTVMAVTDPDGPRGRNISAFVVHIDDPGFSFGEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVGEGLRTALRTLDHTRVTIGAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYVAAAKSERDDADLSFYGAAAKCFASDVAMEITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMARQLLK
>PDB_8i4r_A Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
FDLYRPTEEHEALREAIRSVAEDKIAPHAADVDEQSRFPQEAYEALRASDFHAPHVAEEYGGVGADALATCIVIEEIARV
CASSSLIPAVNKLGSMPLILSGSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRDGDDWILNGQKSWITNA
GISKYYTVMAVTDPDGPRGRNISAFVVHIDDPGFSFGEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVGEGLRTALRTL
DHTRVTIGAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYVAAAKSERDDADLSFYGAA
AKCFASDVAMEITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMARQLLK
>PDB_8i4p_A Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
FDLYRPTEEHEALREAIRSVAEDKIAPHAADVDEQSRFPQEAYEALRASDFHAPHVAEEYGGVGADALATCIVIEEIARV
CASSSLIPAVNKLGSMPLILSGSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRDGDDWILNGQKSWITNA
GISKYYTVMAVTDPDGPRGRNISAFVVHIDDPGFSFGEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVGEGLRTALRTL
DHTRVTIGAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYVAAAKSERDDADLSFYGAA
AKCFASDVAMEITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMARQLLK
>reanno__ANA3_7024494 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) (Shewanella sp. ANA-3)
MNSLYTSLNFGLGEEVDMLRDAVQDFAKHEIAPIAAKVDHDNAFPNEIWPVLGGMGLLGVTVPEEYGGANMGYLAHVVAMEEISRASASIGLSYGAHSNLCVNQINRNGNAEQKAKYLPKLVSGEHIGALAMSEPNAGSDVVSMKLHARKEGDRYILNGNKMWITNGPDANTYVIYAKTDLTKGAHGITAFIVERGFKGFSQAQKLDKLGMRGSNTCELVFEDVEVPEENILGGLNNGVKVLMSGLDYERVVLSGGPLGIMNACMDIVVPYIHEREQFGKSIGEFQLVQGKLADMYTGMNAAKAYVYSVAKSCDRGETTRKDAAGAILYSAELATKMALDAIQLLGGNGYVNEYATGRLLRDAKLYEIGAGTSEIRRMLIGRELFNESK
>reanno__Smeli_SM_b21121 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) (Sinorhizobium meliloti 1021)
MFEAGLNFALGEEIDALRASVRRFASERIAPLADDADRSNAFPMSLWREMGELGLLGITADEAHGGAGLGYLAHCVAMEEISRASASVGLSYGAHSNLCVNQINRNGKPAQKSRYLPKLISGEHVGALAMSEPGAGSDVVSMKLKADKRGDRYVLNGSKMWITNGPDADVLVVYAKTDPAAGPRGITAFLVEKAFPGFSAGQKLDKLGMRGSNTSELIFTDCEVPEENVLGGVGEGVKVLMSGLDYERVVLSAGPLGIMAACLDVVVPYLHERKQFGQPIGEFQLMQGKLADMYVTMNAARAYVYAVAAACDRGETARKDAAGCILYAAEKATAMALEAIQALGGNGYTNDYPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFAETK
>SwissProt__Q06319 Acyl-CoA dehydrogenase, short-chain specific; Butyryl-CoA dehydrogenase; BCAD; SCAD; EC 1.3.8.1 (Megasphaera elsdenii)
MDFNLTDIQQDFLKLAHDFGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDGGDVLSYILAVEELAKYDAGVAITLSATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGTYTLNGSKIFITNGGAADIYIVFAMTDKSKGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIAMMTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVDAAIAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGALLR
>biolip__6cxtB Crystal structure of fad-dependent dehydrogenase
MNFEWTHEQAELFEHALRFGKELGFPRDNWNALGDFGYFGLPIPEKYAKDGSGFDILTTIKIIEGLGQSCTDTGLLFAGAAHTFACSMPILEHGSETLKHQLLPDLATGRKIAANAISEASAGSDISNLATTAQKEGDYYVLNGGKSYVTNGSIADYYVVYATTNKKHGYLGQTAFVVPRNTPGISVGNDYHKLGLRSAPLNQVFFDNCTIHKDYALGREGQGARIFAASMDWERCCLFAIFVGAMQRDLNQCIEYANTRMQGDKTISRFQAVSHRIADMGVRLESARLMLYYAAWQKSQDVDNTKAVAMSKLAISEAFVQSGIDSIRVHGALGYLDEGRVNNSIKDALGSVLFSGTSDIQRELICNRLGLL
>reanno__pseudo3_N2E3_AO353_20350 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) (Pseudomonas fluorescens FW300-N2E3)
MSYPTLNFALGETIDMLRDQVRAFVSKEIAPRAAQIDIDNLFPADLWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSASVALSYGAHSNLCVNQINRNGTHEQKAKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRADKRGDHYVLNGSKTWITNGPDANTYVIYAKTDLEKGPHGITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVEVPEENILGVLNGGVKVLMSGLDYERVVLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGVILYSAERATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFNETR
>biolip__7szvA Crystal structure of acyl-coa dehydrogenase from mycobacterium marinum in complex with fda
TLPKEYQDLRDTVADFARSVVAPVSAKHDEEHSFPYEVVAKMGEMGLFGLPFPEEYGGMGGDYFALALALEELGKVDQSVAITLEAGVGLGAMPIYRFGNEEQKSKWLPDLLAGRALAGFGLTEPGAGSDAGSTRTTARLDGGEWVVNGSKQFITNSGTDITSLVTITAVTKEISTIIVPSGTPGFIVEPVYNKVGWNASDTHPLSFDDARVPEENLLGIRGKGYANFLSILDEGRIAIAALATGVAQGCVDESVKYAKERQSFGQPIGSYQAISFKIARMEARAHVARTAYYEAAAKMLAGKPFKKEAAIAKMISSEAAMDNARDATQVHGGYGFMNEYPVARHYRDSKILEIGEGTTEVQLMLIARSLGL
>metacyc__MONOMER-20595 cinnamate reductase monomer (EC 1.3.8.15) (Clostridium sporogenes (strain ATCC 15579))
MFFTEQHELIRKLARDFAEQEIEPIADEVDKTAEFPKEIVKKMAQNGFFGIKMPKEYGGAGADNRAYVTIMEEISRASGVAGIYLSSPNSLLGTPFLLVGTDEQKEKYLKPMIRGEKTLAFALTEPGAGSDAGAVATTAREEGDYYILNGRKTFITGAPISDNIIVFAKTDMSKGTKGITTFIVDSKQEGVSFGKPEDKMGMIGCPTSDIILENVKVHKSDILGELNKGFITAMKTLSVGRIGVAAQALGIAQAAVDEAVKYAKQRKQFNRPIAKFQAIQFKLANMETKLNAAKLLVYNAAYKMDCGEKADKEASMAKYFAAESAIQIVNDALQIHGGYGYIKDYKIERLYRDVRVIAIYEGTSEVQQMVIASNLLK
>reanno__pseudo5_N2C3_1_AO356_01580 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) (Pseudomonas fluorescens FW300-N2C3)
MSYPSLNFALGETIDMLRDQVQAFVKAELAPRAAQIDIDNLFPADMWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSASVALSYGAHSNLCVNQINRNGNHEQKTKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRADKRGDHYVLNGSKTWITNGPDANTYVIYAKTDLEKGPHGITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVEVPEENILGALNGGVKVLMSGLDYERVVLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGVILYSAERATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFNETR
>ENA__CAC08233.1 isovaleryl-CoA dehydrogenase (Solanum tuberosum)
MHKLFAVRSLSSAIAKNFKSLQNQQAAFSTSLLLDDTQKQFKESVAKFAQENIAPYAEKIDRTNSFPKEINLWKLMGDFNLHGITAPEEYGGLNLGYLYHCIALEEISRASGAVAVSYGVQSNVCINQLVRNGTPDQKQKYLPKLISGDHIGALAMSEPNAGSDVVSMKCRADRVDGGYVLNGNKMWCTNGPVANTLIVYAKTDTTAGSKGITAFIIEKEMPGFSTAQKLDKLGMRGSDTCELVFENCFVPKENVLGQEGKGVYVLMSGLDLERLVLAAGPVGIMQACMDIVIPYVRQREQFGRPIGEFQLIQGKLADMYTALQSSRSYVYAVAKDCDNGKIDPKDCSGTILLAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKMYEIAAGTSEIRRLVIGRELFKHQ
>SwissProt__Q9FS88 2-methylacyl-CoA dehydrogenase, mitochondrial; 2-methylbutanoyl-CoA dehydrogenase; 2-methylbutyryl-CoA dehydrogenase; 2MBCD; Isovaleryl-CoA dehydrogenase 1; St-IVD1; EC 1.3.8.5 (Solanum tuberosum (Potato))
MHKLFAVRSLSSAIVKSFKSLQNQQAAFSTSLLLDDTQKQFKESVAKFAQENIAPYAEKIDRTNSFPKEINLWKLMGDFNLHGITAPEEYGGLNLGYLYHCIALEEISRASGAVAVSYGVQSNVCINQLVRNGTPDQKQKYLPKLISGDHIGALAMSEPNAGSDVVSMKCRADRVDGGYVLNGNKMWCTNGPVANTLIVYAKTDTTAGSKGITAFIIEKEMPGFSTAQKLDKLGMRGSDTCELVFENCFVPNENVLGQEGKGVYVLMSGLDLERLVLAAGPVGIMQACMDIVIPYVRQREQFGRPIGEFQLIQGKLADMYTALQSSRSYVYAVAKDCDNGKIDPKDCSGTILLAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKMYEIAAGTSEIRRLVIGRELFKHQ
>reanno__WCS417_GFF3325 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) (Pseudomonas simiae WCS417)
MSYPSLNFALGETIDMLRDQVQSFVSKEIAPRAAQIDRDNLFPADLWQKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSASVALSYGAHSNLCVNQINRNGNHSQKLKYLPKLISGEHVGALAMSEPNAGSDVVSMKLRADKRGDHYVLNGSKTWITNGPDASTYVIYAKTDLEKGPHGITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVEVPEENILGTLNGGVKVLMSGLDYERVVLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGVILYSAERATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFNETR
>reanno__Phaeo_GFF1011 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) (Phaeobacter inhibens BS107)
MFNASMTFDLGEDVNALRDMVHRWAQERVRPMAQEIDQKNEFPAELWQEMGELGLLGITVPEEFGGAGMSYLAHTVAVEEIARASASVSLSYGAHSNLCVNQIKLNGNAEQKAKYLPRLVSGEHVGALAMSEAGAGSDVVSMSLRAEKRNDHYRLNGNKYWITNGPDADTLVVYAKTDPDAGSKGMTAFLIEKEFKGFSTSQHFDKLGMRGSNTAELVFEDVEVPFENVLGEEGKGVRVLMSGLDYERVVLAGIGTGIMAACMDEMMPYMKERKQFGQPIGNFQLMQGKIADMYTAMNTARAYVYEVAKACDKGTVTRQDAAACCLYASEVAMTQAHQAVQAFGGAGYLSDNPVGRIFRDAKLMEIGAGTSEIRRMLIGRELMSQM
>reanno__pseudo6_N2E2_Pf6N2E2_2191 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) (Pseudomonas fluorescens FW300-N2E2)
MSYPSLNFALGETIDMLRDQVQAFVNAELAPRAAQIDIDNLFPADMWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSASVALSYGAHSNLCVNQINRNGNHEQKTKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRADKRGDKYVLNGSKTWITNGPDANTYVIYAKTDLEKGPHGITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVEVPEDNILGALNGGVKVLMSGLDYERVVLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGVILYSAERATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFNETR
>reanno__psRCH2_GFF1051 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) (Pseudomonas stutzeri RCH2)
MNYSSLNFALGETIDMLREQVQAFVAAEIAPRAEAIDQENLFPADMWRKFGEMGLLGVTVSEEYGGAGLGYLAHVVAMEEISRGSASVALSYGAHSNLCVNQINRNGNPEQKARYLPKLISGEHVGALAMSEPNAGSDVVSMKLRAEKRGDRYVLNGSKTWITNGPDANTYVIYAKTDLDKGAHGITAFIVERDWKGFSRGNKFDKLGMRGSNTCELFFDDVEVPQENVLGAENGGVKVLMSGLDYERVVLAGGPTGIMQSCLDVVVPYIHDRKQFGQSIGEFQFIQGKVADMYTQLNASRAYLYAVAQACDRGETTRKDAAGVILYTAENATQMALQAIQILGGNGYINEFPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFNESR
>biolip__4m9aB Crystal structure of acyl-coa dehydrogenase from burkholderia thailandensis e264
DDLYTEDQRMILDAARAFCAEVLAPNAAQWDRESHLPDEVVAQMGELGFLGMIVPADWGGSYTDYVAYALALEEIAAGCASCATLVSVHNSVGCGPVLNYGTTEQKERWLRDLASGKTVGAFSLTEPHAGSEAHNLRTRAELRDGKWILNGSKQFVTNGARAGLAIVFAMTDPDEGKRGLSAFVVPTDTPGFIVGKPEKKMGIRASDTCPITLENCAIPQENLLGKRGEGLKIALSNLEGGRIGIAAQATGIARAAFDRARRYARERVQFGKPIAEHQAIAEKLANMATQINAARLLTHHAARLRTAGLPCLSEASQAKLFASEMAEAVCSDAIQIHGGYGFLVDYEVERHYRDARITQIYEGTSEVQRMVIARQL
>metacyc__HS04619-MONOMER short-chain acyl-CoA dehydrogenase monomer (EC 1.3.8.1) (Homo sapiens)
MAAALLARASGPARRALCPRAWRQLHTIYQSVELPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAWEASAAVVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYRS
>biolip__7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
LHTIYQSVELPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAWEASAAVVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYR
>PDB_7y0b_A Crystal structure of human short-chain acyl-coa dehydrogenase
IYQSVELPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISR
GCASTGVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWIT
NAWEASAAVVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQT
LDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAM
AKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYRS
>PDB_8sgs_A Human liver mitochondrial short-chain specific acyl-coa dehydrogenase
SVELPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCA
STGVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAW
EASAAVVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDM
GRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKL
AASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYR
>PDB_6cy8_B Crystal structure of fad-dependent dehydrogenase
MNFEWTHEQAELFEHALRFGKELGFPRDNWNALGDFGYFGLPIPEKYAKDGSGFDILTTIKIIEGLGQSCTDTGLLFAGA
AHTFACSMPILEHGSETLKHQLLPDLATKIAANAISEASAGSDISNLATTAQKEGDYYVLNGGKSYVTNGSIADYYVVYA
TTNKKHGYLGQTAFVVPRNTPGISVGNDYHKLGLRSAPLNQVFFDNCTIHKDYALGREGQGARIFAASMDWERCCLFAIF
VGAMQRDLNQCIEYANTRMQGDKTISRFQAVSHRIADMGVRLESARLMLYYAAWQKSQDVDNTKAVAMSKLAISEAFVQS
GIDSIRVHGALGYLDEGRVNNSIKDALGSVLFSGTSDIQRELICNRLGLL
>reanno__Putida_PP_3492 isobutyryl-CoA dehydrogenase (EC 1.3.8.5) (Pseudomonas putida KT2440)
MQDLELSEEQIMIRDMARDFARGEIAPHAQAWEKAGWIDDGVVRKMGELGLLGMVVPEDFGGSYTDYVAYALAVEEISAGCGATGAMMSIHNSVGCGPLLAYGTAEQQQQWLPRLASGEVIGCFCLTEPQAGSEAHNLRTRAELVDGQWVINGAKQFVSNARRAGLAIVFAVTDPELGKKGLSAFLVPTDNPGFKVDRSEHKMGIRASDTCAVTFDNCRIPAANILGERGKGLAIALSNLEGGRIGIAAQALGIARAAFEAALVYSRDRIQFGKPINEHQSIANLLADMQVQVNAARLLILHAARLRSAGKPCLSEASQAKLFASEMAERVCSMAIQVHGGYGYLEDYPVERYYRDARITQIYEGSSEIQRMLIARELKNYPL
>BRENDA__D4QEZ8 short-chain acyl-CoA dehydrogenase (EC 1.3.8.1) (Homo sapiens)
MAAALLARASGPARRALCPRAWRQLHTIYQSVELPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRDCASTGVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAWEASAAVVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYRS
>biolip__2d29A Structural study on project id tt0172 from thermus thermophilus hb8
GLWFEEGAEERQVLGPFREFLKAEVAPGAAERDRTGAFPWDLVRKLAEFGVFGALVPEAYGGAGLSTRLFARMVEAIAYYDGALALTVASHNSLATGHILLAGSEAQKEAFLPKLASGEALGAWGLTEPGSGSDAAALKTKAEKVEGGWRLNGTKQFITQGSVAGVYVVMARTDPPPSPERKHQGISAFAFFRPERGLKVGRKEEKLGLTASDTAQLILEDLFVPEEALLGERGKGFYDVLRVLDGGRIGIAAMAVGLGQAALDYALAYAKGREAFGRPIAEFEGVSFKLAEAATELEAARLLYLKAAELKDAGRPFTLEAAQAKLFASEAAVKACDEAIQILGGYGYVKDYPVERYWRDARLTRIGEGTSEILKLVIARRLLEAV
>biolip__8w0tA Human lcad
EERLETPSAKKLTDIGIRRIFSPEHDIFRKSVRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNIAEHLGGIGGDLYSAAIVWEEQAYSNCSGPGFSIHSGIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSDLQGIKTNAKKDGSDWILNGSKVFISNGSLSDVVIVVAVTNHEAPSPAHGISLFLVENGMKGFIKGRKLHKMGLKAQDTAELFFEDIRLPASALLGEENKGFYYIMKELPQERLLIADVAISASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRLDSATACMAKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAREIVFDK
>metacyc__MONOMER-21331 (4S)-homoplatensicyl-CoA dehydrogenase (Streptomyces platensis)
MRRTLFTPEHEQFRETARAYYLRECVPHAEEWEQAGIVSREAWSAAGAAGLIGWEFPEEFGGQGIRDFRYNAIMAEEMAATGTVGIGLGLQNDVLPSYLSHLTEEQQHRWLPGIVSGRTICALALSEPDAGSDLAAMRTTARREGDHYVLSGQKTFITNGILADFVIVACKTDPDARHKGISLLVVERGMPGFERGRRLDKVGLKAQDTAELFFHDVRVPAANLLGAEGRGFAYMMENLPTERIAIAVSALGGAQRAFELALEYAKTRTAFGQPIGTFQANRFALADMRAKLDAARTYVDGCIMALVEGHLTAVDAAAAKYWTTETAWQIIDRCVQLFGGYGYINEYEIARIWRDNRIERIFGGTSEIMQEIVGRSLGLTSATVRKQE
>SwissProt__H6LGM6 Caffeyl-CoA reductase-Etf complex subunit CarC; Caffeoyl-CoA reductase CarC; NADH-dependent caffeyl-CoA reduction; EC 1.3.1.108 (Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1))
MYFSEQNKMIRKLARDFAEKELTTEILDEVEESGEFPQEILDKMAKFGFFGIKIPKSLGGSGGDHMSYVICMEEFARVSGVASVYLSSPNSLAGGPLLLSGTEEQIEKYLKPIITGKKKLAFALTEPGAGSDAGGMSTTAVDMGDYYLLNGRKTFITMAPLCDDAVIYAKTDMSKGTRGISAFIVDLKSEGVSMGKNEHKMGLIGCATSDIIMEDVKVPKENRLGEVNKGFSNAMKTLDVGRLGVASQSIGVAQGALDEAIKYAKERKQFGKRIADFQAIAFMIADMATKLEAAKLLVYNAASLMDNKKNATKEASMAKFYASEICNEICAKAVQIHGGYGYIKEYKVERMYRDCRVFTIYEGTSQVQQMVISGMLLKK
>PDB_8w0u_A Human lcad complexed with acetoacetyl coenzyme a
EERLETPSAKKLTDIGIRRIFSPEHDIFRKSVRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNIAEHLGGIGG
DLYSAAIVWEEQAYSNCSGPGFSIHSGIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSDLQGIKTNAKKDG
SDWILNGSKVFISNGSLSDVVIVVAVTNHEAPSPAHGISLFLVENGMKGFIKGRKLHKMGLKAQDTAELFFEDIRLPASA
LLGEENKGFYYIMKELPQERLLIADVAISASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCL
QLHEAKRLDSATACMAKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAREIVFDK
>PDB_2vig_B Crystal structure of human short-chain acyl coa dehydrogenase
LPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTG
VIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAWEAS
AAVVFASTSISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGIASQAL
GIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLAASEAATAIS
HQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYR
>biolip__3pfdC Crystal structure of an acyl-coa dehydrogenase from mycobacterium thermoresistibile bound to reduced flavin adenine dinucleotide solved by combined iodide ion sad mr
HIALREAIRALAEKEIAPYAAEVDEKARFPEEALAALNSSGFSAIHVPEEYGGQGADSVATCIVIEEVARVDCSASLIPAVNKLGTMGLILRGSEELKKQVLPAVASGEAMASYALSEREAGSDAASMRTRAVADGDDWILNGSKCWITNGGKSTWYTVMAVTDPDKGANGISAFMVHKDDEGFTVGPKERKLGIKGSPTTELYFENCRIPGDRIIGEPGTGFKTALATLDHTRPTIGAQAVGIAQGALDAAIAYTKERKQFGRPVSDNQGVQFMLADMAMKIEAARLMVYSAAARAERGDLGFISAASKCFASDVAMEVTTDAVQLFGGYGYTQDFPVERMMRDAKITQIYEGTNQIQRVVMSRALLR
>metacyc__HS03876-MONOMER long-chain-acyl-CoA dehydrogenase monomer (EC 1.3.8.8; EC 1.3.8.7) (Homo sapiens)
MAARLLRGSLRVLGGHRAPRQLPAARCSHSGGEERLETPSAKKLTDIGIRRIFSPEHDIFRKSVRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNIAEHLGGIGGDLYSAAIVWEEQAYSNCSGPGFSIHSGIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSDLQGIKTNAKKDGSDWILNGSKVFISNGSLSDVVIVVAVTNHEAPSPAHGISLFLVENGMKGFIKGRKLHKMGLKAQDTAELFFEDIRLPASALLGEENKGFYYIMKELPQERLLIADVAISASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRLDSATACMAKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAREIVFDK
>metacyc__MONOMER-16063 isovaleryl-CoA dehydrogenase subunit (EC 1.3.8.4) (Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1))
MTYPSLNFALGETIDMLRDQVRGFVAAELQPRAAQIDQDNQFPMDMWRKFGEMGLLGITVDEEYGGSALGYLAHAVVMEEISRASASVALSYGAHSNLCVNQIKRNGNAEQKARYLPALVSGEHIGALAMSEPNAGSDVVSMKLRADRVGDRFVLNGSKMWITNGPDAHTYVIYAKTDADKGAHGITAFIVERDWKGFSRGPKLDKLGMRGSNTCELIFQDVEVPEENVLGAVNGGVKVLMSGLDYERVVLSGGPVGIMQACMDVVVPYIHDRRQFGQSIGEFQLVQGKVADMYTALNASRAYLYAVAAACDRGETTRKDAAGVILYSAERATQMALDAIQILGGNGYINEFPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFNETR
>ENA__CAC08234.1 isovaleryl-CoA dehydrogenase, partial (Solanum tuberosum)
SALFRIKNHQKPQFAAFSTSLLFDDTQKQFKESVAQFAQENIAPHAEKIDRTNYFPQDVNLWKLMGDFNLLGITVPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHTNLCINQLVRNGTHEQKQKYLPKLISGEHVGALAMSEPDAGSDVVSMKCKADRVEGGYVLNGNKMWCTNGPTAQTLVVYAKTDVTASSKGITAFIIEKGMTGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQVGKGVYVLMSGLDLERLVLASGPVGIMQACLDVVLPYVKQREQFGRPIGEFQFVQGKVADMYTSMQSSRSYLYSVARECDSGTINTKDCAGVILSAAERATQVALQAIQCLGGNGYVNEYPTGRFLRDAKLYEIGAGTSEIRRMIIGRELFKEQ
>SwissProt__P51174 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 (Mus musculus (Mouse))
MAARLLLRSLRVLKARSAPRPPPSARCSHSGAEARLETPSAKKLTDVGIRRIFSSEHDIFRESVRKFFQEEVIPHHTEWEKAGEVSREVWEKAGKQGLLGINIAEKHGGIGGDLLSTAVTWEEQAYSNCTGPGFSLHSDIVMPYIANYGTKEQIEKFIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNAKRSGSDWILNGSKVFITNGWLSDLVIVVAVTNREARSPAHGISLFLVENGMKGFIKGRKLHKMGMKAQDTAELFFEDVRLPANALLGEENKGFYYLMQELPQERLLIAELAISACEFMFEETRNYVKQRKAFGKTVAHIQTVQHKLAELKTHICVTRAFVDSCLQLHETKRLDSGSASMAKYWASELQNSVAYECVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIARQIVSDS
>SwissProt__Q5W271 L-prolyl-[peptidyl-carrier protein] dehydrogenase; Flavoprotein desaturase PigA; L-prolyl-PCP dehydrogenase; EC 1.3.8.14 (Serratia sp. (strain ATCC 39006) (Prodigiosinella confusarubida))
MDFNLSNSQSDIYESAYRFACDVLDQDAQTRISQKILSTELWKKAAAYGFAHGPVSHQFGGSELGALDTALMIEALGKGSRDIGLSFSLCAHLCACVIPLYRFGSSELKDKYLESLVTGKLIAANAATEPDAGSDIYNMQATAQPCEGGYILNGKKIFITNAPIADVFIIYAKTNPDHGFLGVSAFLIEKGTPGLNVGEVIPKDCLSNCPWSEIVFNDIFIPQSQRIGMEGAGGAIFHDSMIWEKGCLSALFVGGLARLLETTLEYAKARQQFGKAIGQFQSVSNRIIDMKLRLEQCRLMLYRACWKHDQGQDAEADIAMSKLLISEYAVQSGLDAIQTFGGAAMDQELGLVRHLLNMIPSRIFSGTNDIQKEIIARKLGLRGTSS
>SwissProt__P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 (Rattus norvegicus (Rat))
MAAALLARAGGSLGRALRARDWRRLHTVYQSVELPETHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCASTGVIMSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASATVVFASTDRSRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLLRSYRS
>PDB_1jqi_A Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa
VYQSVELPETHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISR
GCASTGVIMSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWIT
NSWEASATVVFASTDRSRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQT
LDMGRIGIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAM
AKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLLRSYR
>SwissProt__Q9FS87 Isovaleryl-CoA dehydrogenase, mitochondrial; IVD; Isovaleryl-CoA dehydrogenase 2; St-IVD2; EC 1.3.8.4 (Solanum tuberosum (Potato))
MHKLFVARSVKSALFRIKNHQKPQFAAFSTSLLFDDTQKQFKESVAQFAQENIAPHAEKIDRTNYFPQDVNLWKLMGNFNLLGITVPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHTNLCINQLVRNGTHEQKQKYLPKLISGEHVGALAMSEPNAGSDVVSMKCKADRVEGGYVLNGNKMWCTNGPTAQTLVVYAKTDVTAGSKGITAFIIEKGMTGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQVGRGVYVLMSGLDLERLVLASGPVGIMQACLDVVLPYVKQREQFGRPIGEFQFVQGKVADMYTSMQSSRSYLYSVARECDSGTINTKDCAGVILSAAERATQVALQAIQCLGGNGYVNEYPTGRFLRDAKLYEIGAGTSEIRRMIIGRELFKEQ
>SwissProt__P15650 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 (Rattus norvegicus (Rat))
MAARLLLRSLRVLSARSATLPPPSARCSHSGAEARLETPSAKKLTDIGIRRIFSSEHDIFRESVRKFFQEEVIPYHEEWEKAGEVSRELWEKAGKQGLLGINIAEKHGGIGGDLLSTAVTWEEQAYSNCTGPGFSLHSDIVMPYIANYGTKEQIEQFIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNAKRSGSDWILNGSKVFITNGWLSDLVIVVAVTNREARSPAHGISLFLVENGMKGFIKGKKLHKMGMKAQDTAELFFEDVRLPASALLGEENKGFYYLMQELPQERLLIADLAISACEFMFEETRNYVRQRKAFGKTVAHIQTVQHKLAELKTNICVTRAFVDSCLQLHETKRLDSASASMAKYWASELQNTVAYQCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIARQIVSDS
>SwissProt__Q39QF5 Cyclohex-1-ene-1-carbonyl-CoA dehydrogenase; CHeneCoA dehydrogenase; EC 1.3.8.10 (Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15))
MKHLTEEQKLTLDMVRDVATREIAPRALELDEKSLFPEYARDLFAKLGLLNPLLPAAYGGTEMGVLTLALILEELGRVCASTALLLIAQTDGMLPIIHGGSPELKERYLRRFAGESTLLTALAATEPAAGSDLLAMKTRAVRQGDKYVINGQKCFITNGSVADVIVVYAYTDPEKGSKGISAFVVEKGTPGLVYGRNESKMGMRGSINSELFFENMEVPAENIIGAEGTGFANLMQTLSTNRVFCAAQAVGIAQGALDIAVRHTQDRVQFGKPIAHLAPVQFMVADMATAVEASRLLTRKAAELLDDGDKKAVLYGSMAKTMASDTAMRVTTDAVQVLGGSGYMKENGVERMMRDAKLTQIYTGTNQITRMVTGRALLFP
>reanno__SB2B_6937192 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) (Shewanella amazonensis SB2B)
MSHLYSTLNFGLGEDVDMLRDAVYEFAKGEIAPLAEKVDRDNAFPNELWAKFGDMGLLGVTVAEEYGGVNMGYLAHVVAMEEISRASASIGLSYGAHSNLCVNQIYRNGNEAQRAKYLPKLISGEHIGALAMSEPNAGSDVVSMKLHARKEGDRYILNGNKMWITNGPDAHTYVIYAKTDLDKGPHGITAFIVERGFKGFSQAQKLDKLGMRGSNTCELVFEDCEVPEENILGGLNNGVKVLMSGLDYERVVLSGGPLGIMTACMDIVVPYVHERVQFGKSIGEFQLVQGKLADMYTGMNAAKSYVYNVARACDRGETTRKDAAGVILYAAELATKMALDAIQLLGGNGYVNEYATGRLLRDAKLYEIGAGTSEIRRMLIGRELFNETK
>ENA__AAL09094.1 DcaA (Acinetobacter baylyi)
MIRDEGMLQQLLSTIRDFVKNELIPREHEVAEKDCIPEDIIQQMRELGLFGLTIPEEYGGLGITMEEEVNVAFELGQTSPAFRSLIGTNNGIGSSGLIIDGTEEQKQKYLPRYASGEIIGSFCLTEPEAGSDAASLKTTAVKDGDFYILNGTKRFITNAPHAATFTVMARTNPAIKGAGGISAFLVEANTPGITLGKIDQKMGQKGSHTCDVIFENCRVPASALIGGVEGVGFKTAMKVLDKGRLHIGAYSVGVAERMLNDALHYAVERKQFGQPIANFQLIQAMLADSKAEIYAAKCMVLDAARRRDEGQNISTEASCAKMFATEMCGRVADRCVQIHGGAGYISEYSIERFYRDVRLFRLYEGTTQVQQIIIAKNMIKEVTS
>reanno__psRCH2_GFF2392 isobutyryl-CoA dehydrogenase (EC 1.3.8.5) (Pseudomonas stutzeri RCH2)
MHDLELSEDQRMIRDMARDFARREIAPHAQAWEKAGWIDDTLVAQMGELGLLGMVVPEEWGGSYIDYVAYALAVEEISAGDGATGALMSIHNSVGCGPVLNYGSQAQKDEWLTELASGRAIGCFALTEPQAGSEAHNLRTRAELVDGHWVLNGSKQFCSNAKRSKLAIVFAVTDPELGKKGLSAFLVPTDTPGFAVERSEHKMGIRASDTCGVSLSDCRIPEANLLGERGKGLAIALSNLEGGRIGIGAQALGIARAAFEAALLYARERVQFGKPIAEHQSIANMLADMQTQLNAARLLILHAARLKSAGLPCLSEASQAKLFASEMAEKVCSQAVQIHGGYGYLEDYPVERYYRDARITQIYEGSSEIQRLLIARELANYAL
>metacyc__MONOMER-12757 propionyl-CoA dehydrogenase (Anaerotignum propionicum)
MFLLKIKKERMKRMDFSLTREQEMLKKLARQFAEIELEPVAEEIDREHVFPAENFKKMAEIGLTGIGIPKEFGGSGGGTLEKVIAVSEFGKKCMASASILSIHLIAPQAIYKYGTKEQKETYLPRLTKGGELGAFALTEPNAGSDAGAVKTTAILDSQTNEYVLNGTKCFISGGGRAGVLVIFALTEPKKGLKGMSAIIVEKGTPGFSIGKVESKMGIAGSETAELIFEDCRVPAANLLGKEGKGFKIAMEALDGARIGVGAQAIGIAEGAIDLSVKYVHERIQFGKPIANLQGIQWYIADMATKTAAARALVEFAAYLEDAGKPFTKESAMCKLNASENARFVTNLALQIHGGYGYMKDYPLERMYRDAKITEIYEGTSEIHKVVIAREVMKR
>PDB_7p9x_A Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1-ene-1-carboxyl-coa
HLTEEQKLTLDMVRDVATREIAPRALELDEKSLFPEYARDLFAKLGLLNPLLPAAYGGTEMGVLTLALILEELGRVCAST
ALLLIAQTDGMLPIIHGGSPELKERYLRRFAGESTLLTALAATEPAAGSDLLAMKTRAVRQGDKYVINGQKCFITNGSVA
DVIVVYAYTDPEKGSKGISAFVVEKGTPGLVYGRNESKMGMRGSINSELFFENMEVPAENIIGAEGTGFANLMQTLSTNR
VFCAAQAVGIAQGALDIAVRHTQDRVQFGKPIAHLAPVQFMVADMATAVEASRLLTRKAAELLDDGDKKAVLYGSMAKTM
ASDTAMRVTTDAVQVLGGSGYMKENGVERMMRDAKLTQIYTGTNQITRMVTGRALLFP
>biolip__6af6A Piga with fad and proline
MDFNLSNSQSDIYESAYRFACDVLDQDAQTRISQKILSTELWKKAAAYGFAHGPVSHQFGGSELGALDTALMIEALGKGSRDIGLSFSLCAHLCACVIPLYRFGSSELKDKYLESLVTGKLIAANAATEPDAGSDIYNMQATAQPCEGGYILNGKKIFITNAPIADVFIIYAKTNPDHGFLGVSAFLIEKGTPGLNVGEVIPKDCLSNCPWSEIVFNDIFIPQSQRIGMEGAGGAIFHDSMIWAKGCLSALFVGGLARLLETTLEYAKARQQFGKAIGQFQSVSNRIIDMKLRLEQCRLMLYRACWKHDQGQDAEADIAMSKLLISEYAVQSGLDAIQTFGGAAMDQELGLVRHLLNMIPSRIFSGTNDIQKEIIARKLGLRG
>biolip__4ktoA Crystal structure of a putative isovaleryl-coa dehydrogenase (psi- nysgrc-012251) from sinorhizobium meliloti 1021
MFEAGLNFALGEEIDALRASVRRFASERIAPLADDADRSNAFPMSLWREMGELGLLGITADEAHGGAGLGYLAHCVAMEEISRASASVGLSYGAHSNLCVNQINRNGKPAQKSRYLPKLISGEHVGALAMSEPGVSMKLKADKRGDRYVLNGSKMWITNGPDADVLVVYAKTDPPRGITAFLVEKAFPGFSAGQKLDKLGMRGSNTSELIFTDCEVPEENVLGGVGEGVKVLMSGLDYERVVLSAGPLGIMAACLDVVVPYLHERKQFGQPIGEFQLMQGKLADMYVTMNAARAYVYAVAAACDRGETARKDAAGCILYAAEKATAMALEAIQALGGNGYTNDYPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFAE
>reanno__pseudo3_N2E3_AO353_25670 isobutyryl-CoA dehydrogenase (EC 1.3.8.5) (Pseudomonas fluorescens FW300-N2E3)
MHDIELTEEQVMIRDMARDFARGEIAPHAQAWEKAGWIDDALVAKMGELGLLGMVVPEEWGGTYVDYVAYALAVEEISAGDGATGALMSIHNSVGCGPVLNYGTEEQKQTWLADLASGQAIGCFCLTEPQAGSEAHNLRTRAELRDGQWVINGAKQFVSNGRRAKLAIVFAVTDPDLGKKGLSAFLVPTDTPGFIVDRSEHKMGIRASDTCAVTLNNCTIPEANLLGERGKGLAIALSNLEGGRIGIAAQALGIARAAFEAALAYARDRVQFDKPIIEHQSVANMLADMHTRLNAARLLILHAARLRSAGKPCLSEASQAKLFASEMAEKVCSSAIQIHGGYGYLEDYPVERYYRDARITQIYEGSSEIQRMVIARELKNYLV
>metacyc__MONOMER-18319 cyclohex-1-ene-1-carbonyl-CoA dehydrogenase monomer (EC 1.3.8.10) (Syntrophus aciditrophicus (strain SB))
MKGPIKFNALSLQGRSVMSNQSNDTTITQRRDTMNELTEEQKLLMEMVRNLAVREIAPRAIEIDENHSFPVHARDLFADLGLLSPLVPVEYGGTGMDITTFAMVLEEIGKVCASTALMLLAQADGMLSIILDGSPALKEKYLPRFGEKSTLMTAFAATEPGAGSDLLAMKTRAVKKGDKYVINGQKCFITNGSVADILTVWAYTDPSKGAKGMSTFVVERGTPGLIYGHNEKKMGMRGCPNSELFFEDLEVPAENLVGEEGKGFAYLMGALSINRVFCASQAVGIAQGALERAMQHTREREQFGKPIAHLTPIQFMIADMATEVEAARLLVRKATTLLDAKDKRGPLIGGMAKTFASDTAMKVTTDAVQVMGGSGYMQEYQVERMMREAKLTQIYTGTNQITRMVTGRSLLFPS
>metacyc__MONOMER-20314 L-prolyl-[peptidyl-carrier protein] dehydrogenase (EC 1.3.8.14) (Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5))
MDFNYDDTQKKHAAMIAQVCAEQLAACGNEHSRYFTARQWAICGEAGLLGLSIPREYGGQGLGALSTAIAMHAFGLGCTDMGLVFAAAAHQFACAMPIVEFATAETKRDVLPKLASGEFIGSNAITEPEAGSDSSNLKSRAWPQADGSYRLDGHKSFAGNAPIADIFVTYATTQPEYGALGVSGFIVHRSSAGLRVSEPLDKVCLRSCPAGEVFFDDCRVPEVNRLGEEGQGRQVFQSSMGWERACLFAAFLGMMERQLEQTIEHARTRRQFGKPIGDNQAVSHRIAQMKLRLESARLLLFRACWGMDQGDPGQLNIALSKLAISEGALASSIDAVRIFGGRGCLESFGIEAMLRDSIGTTIFSGTSDMQHEIIARELKL
>metacyc__HS10828-MONOMER Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial (EC 1.3.8.5) (Homo sapiens)
MEGLAVRLLRGSRLLRRNFLTCLSSWKIPPHVSKSSQSEALLNITNNGIHFAPLQTFTDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLSTVLVIEELAKVDASVAVFCEIQNTLINTLIRKHGTEEQKATYLPQLTTEKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWISSAEHAGLFLVMANVDPTIGYKGITSFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIGHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAGKPFIKEASMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHIDAEY
>biolip__2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
APLQTFTDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLSTVLVIEELAKVDASVAVFCEIQNTLINTLIRKHGTEEQKATYLPQLTTEKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWISSAEHAGLFLVMANVDPTIGYKGITSFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIGHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAGKPFIKEASMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHIDAEY
>biolip__2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
TARYLREEHHMFRAAFRKFLEKEAYPHYNDWEKRGIIPRSFWAKMGENGFLCPWVDEKYGGLNADFAYSVVINEELEKVGSSLVGIGLHNDIVTPYIASYGTEEQKQKWLPKCVTGELITAIAMTEPGAGSDLANISTTAVKDGDYYIVNGQKTFITNGIHADLIVVACKTDPQAKPPHRGISLLVVERDTPGFTRGRKLEKVGLHAQDTAELFFQDAKVPAYNLLGEEGKGFYYLMEKLQQERLVVAIAAQTAAEVMFSLTKQYVKQRTAFGKRVSEFQTVQFRLAEMATEIALGRTFVDRVIEEHMAGKQIVTEVSMAKWWITEMAKRVAAEAMQLHGGYGYMEEYEIARRYRDIPVSAIYAGTNEMMKTIIARQLDL
>biolip__2z1qB Crystal structure of acyl coa dehydrogenase
KKLWQKGGGWLLEVPERVYTPEDFDESVKEIARTTRTFVEREVLPLLERMEHGELELNVPLMRKAGELGLLAIDVPEEYGGLDLPKVISTVVAEELSGSGGFSVTYGAHTSIGTLPLVYFGTEEQKRKYLPKLASGEWIAAYCLTEPGSGSDALAAKTRATLSEDGKHYILNGVKQWISNAGFAHLFTVFAKVDGEHFTAFLVERDTPGLSFGPEEKKMGIKASSTRQVILEDVKVPVENVLGEIGKGHKIAFNVLNVGRYKLGAGAVGGAKRALELSAQYATQRVQFGRPIGRFGLIQQKLGEMASRIYAAESAVYRTVGLIDEALLGKKGPEAVMAGIEEYAVEASIIKVLGSEVLDYVVDEGVQIHGGYGYSQEYPIERAYRDARINRIFEGTNEINRLLIPGMLLRRAEPEDLELHQVQNLKKLALMVAGLAVQKYGQGVEEEQEVLGAVADILIDAYAAESALLRARRLGGLAPVLARIYLAQALDRAQAGALSVLPRLVEGDEARVVYSAARRLTKREPGDLVALRRQAAEAVLEAGGYPIPR
>biolip__3r7kA Crystal structure of a probable acyl coa dehydrogenase from mycobacterium abscessus atcc 19977 / dsm 44196
PEAWTTPERRALSQMARSFVEREIAPKLAEWEHVGEIPRDLHLNAAEVGLLGIGFPEEVGGSGGNAIDSALVTEAILAAGGSTGVCAALFTHGIALPHIAANGSDALIERYVRPTLAGKMIGSLGVTEPGAGSDVANLRTRAVREGDTYVVNGAKTFITSGVRADFVTTAVRTGGPGYGGVSLLVIDKNSPGFEVSRRLDKMGWRCSDTAELSFVDVRVPADNLVGAENSGFLQIMQQFQAERLGIAVQAYATAGRALDLAKSWARERETFGRPLTGRQIIRHKLAEMARQVDVACTYTRAVMQRWLAGEDVVAEVSMAKNTAVYACDYVVNEAVQIFGGMGYMRESEIERHYRDCRILGIGGGTNEIMNEVIAKRIG
>biolip__3owaC Crystal structure of acyl-coa dehydrogenase complexed with fad from bacillus anthracis
AVKGGSFLVDEITIDQVFTPEDFSSEHKMIAKTTEDFIVNEVLPELEYLEQHEFDRSVRLLKEAGELGLLGADVPEEYGGIGLDKVSSALIAEKFSRAGGFAITHGAHVGIGSLPIVLFGNEEQKKKYLPLLATGEKLAAYALTEPGSGSDALGAKTTARLNAEGTHYVLNGEKQWITNSAFADVFIVYAKIDGEHFSAFIVEKDYAGVSTSPEEKKMGIKCSSTRTLILEDALVPKENLLGEIGKGHIIAFNILNIGRYKLGVGTVGSAKRAVEISAQYANQRQQFKQPIARFPLIQEKLANMAAKTYAAESSVYRTVGLFESRMSTLSEEEVKDGKAVAASIAEYAIECSLNKVFGSEVLDYTVDEGVQIHGGYGFMAEYEIERMYRDSRINRIFEGTNEINRLIVPGTFLRKAMKGELPLLQKAQKLQEELMMMMPEEVGDEPLALQKYLVNNAKKIGLMVAGLAAQKYGKALDKEQEILVNIADIVSNLYAMESAVLRTEKAIKTTGLEKNKQKVLYTEVFCQEAFNEIEAHAKETLIAVENGDMLRMMLSSLRKLTRHTPLNVIPKKREIAAKILEDERYTV