>WP_010877025.1 NCBI__GCF_000008645.1:WP_010877025.1
MFENVISIKDFKREDIEFILREAEKMEPFASGEKSSSALRGKILGMMFYEPSTRTRLSFETAMKRLGGDVVGFADTGATSAVKGESLADTAMMLSAYSDAIVIRHNLEGAARYISDVVDVPVINAGDGAGQHPTQTLLDLYTMKRFFGRIGSLRVALVGDLKYGRTVHSLAYALAVFGASMSFVSPPVLRMPDNIIHDLRRAGVEVKETERLDDVIDEVDVLYVTRIQKERFPDPEEYSRIRGAYHIDGSTVADRDLIVMHPLPRIDEISPEVDSLPQAMYFRQAFYGVPVRMALLRLLISERRGSENQKIV
>SwissProt__P77918 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 (Pyrococcus abyssi (strain GE5 / Orsay))
MDWKGRDVISIRDFSKEDIETVLATAERLERELKEKGQLEYAKGKILATLFFEPSTRTRLSFESAMHRLGGAVIGFAEASTSSVKKGESLRDTIKTVEQYCDVIVIRHPKEGAARLAAEVAEVPVINAGDGSNQHPTQTLLDLYTIKKEFGRIDGLKIGLLGDLKYGRTVHSLAEALTFYDVELYLISPELLRMPRHIVEELREKGMKVVETTTLEDVIGKLDVLYVTRIQKERFPDEQEYLKVKGSYQVNLKVLEKAKDELRIMHPLPRVDEIHPEVDNTKHAIYFRQVFNGVPVRMALLALVLGVI
>biolip__1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi
DWKGRDVISIRDFSKEDIETVLATAERLERELKEKGQLEYAKGKILATLFFEPSTRTRLSFESAMHRLGGAVIGFAEASTSSVKKGESLRDTIKTVEQYCDVIVIRHPKEGAARLAAEVAEVPVINAGDGSNQHPTQTLLDLYTIKKEFGRIDGLKIGLLGDLKYGRTVHSLAEALTFYDVELYLISPELLRMPRHIVEELREKGMKVVETTTLEDVIGKLDVLYVTRIQKERFPDEQEYLKVKGSYQVNLKVLEKAKDELRIMHPLPRVDEIHPEVDNTKHAIYFRQVFNGVPVRMALLALVLGVI
>SwissProt__Q58976 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 (Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii))
MKHLISMKDIGKEEILEILDEARKMEELLNTKRPLKLLEGKILATVFYEPSTRTRLSFETAMKRLGGEVITMTDLKSSSVAKGESLIDTIRVISGYADIIVLRHPSEGAARLASEYSQVPIINAGDGSNQHPTQTLLDLYTIMREIGRIDGIKIAFVGDLKYGRTVHSLVYALSLFENVEMYFVSPKELRLPKDIIEDLKAKNIKFYEKESLDDLDDDIDVLYVTRIQKERFPDPNEYEKVKGSYKIKREYVEGKKFIIMHPLPRVDEIDYDVDDLPQAKYFKQSFYGIPVRMAILKKLIEDNEGE
>biolip__4eknB Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form
MKHLISMKDIGKEEILEILDEARKMEELLNTKRPLKLLEGKILATVFYEPSTRTRLSFETAMKRLGGEVITMTDLKSSSVAKGESLIDTIRVISGYADIIVLRHPSEGAARLASEYSQVPIINAGDGSNQHPTQTLLDLYTIMREIGRIDGIKIAFVGDLKYGRTVHSLVYALSLFENVEMYFVSPKELRLPKDIIEDLKAKNIKFYEKESLDDLDDDIDVLYVTRIQKERFPDPNEYEKVKGSYKIKREYVEGKKFIIMHPLPRVDEIDYDVDDLPQAKYFKQSFYGIPVRMAILKKLIEDNE
>PDB_2ipo_A E. Coli aspartate transcarbamoylase complexed with n-phosphonacetyl-l- asparagine
ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTS
LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSGNVPVLNAGDGSNQHPTQTLLDLFTIQETQGRLDNLHVAMV
GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPQYILDMLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY
ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQALLALVLNRDLVL
>PDB_2h3e_A Structure of wild-type e. Coli aspartate transcarbamoylase in the presence of n-phosphonacetyl-l-isoasparagine at 2.3a resolution
ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTS
LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSGNVPVLNAGDGSNQHPTQTLLDLFTIQETQGRLDNLHVAMV
GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPQYILDMLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY
ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQALLALVLNRDLVL
>PDB_2fzk_A The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.50 resolution
ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTS
LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSGNVPVLNAGDGSNQHPTQTLLDLFTIQETQGRLDNLHVAMV
GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPQYILDMLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY
ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQALLALVLNRDLVL
>PDB_2fzg_A The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.25 resolution
ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTS
LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSGNVPVLNAGDGSNQHPTQTLLDLFTIQETQGRLDNLHVAMV
GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPQYILDMLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY
ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQALLALVLNRDLVL
>PDB_2fzc_A The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.10 resolution
ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTS
LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSGNVPVLNAGDGSNQHPTQTLLDLFTIQETQGRLDNLHVAMV
GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPQYILDMLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY
ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQALLALVLNRDLVL
>PDB_2air_A T-state active site of aspartate transcarbamylase:crystal structure of the carbamyl phosphate and l-alanosine ligated enzyme
ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTS
LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSGNVPVLNAGDGSNQHPTQTLLDLFTIQETQGRLDNLHVAMV
GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPQYILDMLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY
ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQALLALVLNRDLVL
>PDB_1za2_A Structure of wild-type e. Coli aspartate transcarbamoylase in the presence of ctp, carbamoyl phosphate at 2.50 a resolution
ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTS
LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSGNVPVLNAGDGSNQHPTQTLLDLFTIQETQGRLDNLHVAMV
GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPQYILDMLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY
ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQALLALVLNRDLVL
>PDB_1r0c_A Products in the t state of aspartate transcarbamylase: crystal structure of the phosphate and n-carbamyl-l-aspartate ligated enzyme
ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTS
LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSGNVPVLNAGDGSNQHPTQTLLDLFTIQETQGRLDNLHVAMV
GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPQYILDMLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY
ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQALLALVLNRDLVL
>PDB_1r0b_A Aspartate transcarbamylase (atcase) of escherichia coli: a new crystalline r state bound to pala, or to product analogues phosphate and citrate
ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTS
LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSGNVPVLNAGDGSNQHPTQTLLDLFTIQETQGRLDNLHVAMV
GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPQYILDMLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY
ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQALLALVLNRDLVL
>PDB_2at1_A Crystal structures of phosphonoacetamide ligated t and phosphonoacetamide and malonate ligated r states of aspartate carbamoyltransferase at 2.8-angstroms resolution and neutral ph
ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFEASTRTRLSFQTSMHRLGASVVGFSDSANTS
LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSGNVPVLNAGDGSNQHPTQTLLDLFTIQQTEGRLDNLHVAMV
GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPEYILDMLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY
ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQALLALVLNRDLVL
>PDB_1at1_A Crystal structures of phosphonoacetamide ligated t and phosphonoacetamide and malonate ligated r states of aspartate carbamoyltransferase at 2.8-angstroms resolution and neutral p H
ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFEASTRTRLSFQTSMHRLGASVVGFSDSANTS
LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSGNVPVLNAGDGSNQHPTQTLLDLFTIQQTEGRLDNLHVAMV
GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPEYILDMLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY
ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQALLALVLNRDLVL
>SwissProt_P20054 Multifunctional protein pyr1-3; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Dictyostelium discoideum (Social amoeba)
MDILNRKKGCLVLEDGTKLSGYSFGSERSVAGECVFSTGMVGYNESISDPSYTGQILVFSFPLIGNYGVPSFRERDPESG
LAVNFESDKAHVQAIICSEYCDEYSHWAAEKSLSEWLKESNIPGLYGIDTRALITKIREKGSLKGKVIIGDFDESKLEFE
DINLRNLVAEVSTKEIKEYKAAENNKKTGEKRKNKKVIVLDCGIKNNQIRCLLNRGVDLKVVPWDYDVVANESINDYDGV
FISNGPGDPSLCGKAIENIRKVLALPVAKAVFGVCMGNQLLGLAAGAQTHKMAFGNRGLNQPCVDQISGRCHITSQNHGF
VIDSNSLPAGSGWKTYFINANDASNEGIYHESKPWFSVQFHPEAMAGPTDTEYLFDNFVDNVCGEQQHKSPMNKSKIIDC
PKGINKVLILGSGGLSIGQAGEFDYSGSQAIKALKEEGIKTILINPNIATVQTSPGLADKVYFLPVNASSVQKVIENENP
DGILVTFGGQTALNCGIELYKSGILEKYNCKVLGTPIETIIATEDRGIFAEKLSEINERIAPSMACNSLEESLIEAEKIG
YPVIVRAAYCLGGLGSGFADNKEQLTALVTEAMATSSQVLVEKSLKGWKEIEYEVLRDSKDNCITVCNMENFDPLGIHTG
ESIVVAPSQTLSDREYQMLRETAIKTVRHLGVIGECNIQYSLNPYSEEYCIIEVNARLSRSSALASKATGYPLAFISAKV
ALGYDLAALRNTITKKTTACFEPSLDYLVVKMPRWDLKKFTRVSNKISSSMKSVGEVMSIGRKFEEAIQKAIRMVMDGAV
EGFQAGVFPTSDEELEHPTNNRILVLASAFKDGYSIDRVHQLTKIDKWFLTKLKAIIDLENHLSTYKEPSQIPSEILKFS
KQQGFSDKQIARAVGTTELNVRDYRKKMGIIPCTKHIDTVAAEFPAQNNYLYMTYNGETNDVNINEKSYITLGSGSYRIG
SSVEFDWCAVSCIRTLRSLGLKSIMINFNPETVSTDYDECDYLYFEELSLERVLDIYERGGPNSNHGVILSVGGQIPNNL
AIPLSRCNVKVLGTHPDMIDSAENRYKFSRLLDTIGIDQPLWKELTSVSDTKDFCESVGFPCLVRPSYVLSGAAMNVVHS
SQDLETFLTEAAAVSRDHPVVISKFIQEAKEIEIDAVADNGRIVLFAISEHVENAGVHSGDATIVCPAQDLDDATILKVE
ETARKIAEALNVSGPFNIQFIAKNNEIKVIECNLRCSRSFPFVSKTLNINFIELATKIIIKHQYDLPVVNPINYVGVKVP
QFSFIRLKGADPVLGVEMASTGEVACFGNTREEAYVKGLISTGFKAPEKNVLLSIGSFKEKHEFLPSAHKLIKLGYTLFG
TQGTADFYSENGVPVTQLNWDEEDLGENVIQKKMTENTIHLFINLPSKNKYRRPSSFMSRGYSLRRVAIDFQVPLITNIK
CAKLFVDSLSYMKGPMPIENVDWRTSNKIIRLPGLVDVHVHLREPGATHKEDWDSGTATALAGGFTMVGAMPNTNPAIMD
DASFELCKSLAASKARCDYGIFIGATFTNTTTAGKFASDAMGMKMYLEETFAPLPLKDDINVWRDHIMNWPGTTPICVHA
DGRNLAAILLLGWMYDKHMHVCHVSHKEEIDIIRDAKKRGMKLSCEVSPHHLTLCDKDIPRIGAGQSEVRPKLGTEEDLN
ALWDNIDYIDMIATDHAPHTWEEKCSAKPPPGFPGLETSLPLMLTAVHNGRITIEDLVMKMHTNPIRIFNLPEQPDTYIE
VDMEQEWTIPKKPLYSRCGWTPFEGLQVRGKVVKVVLRGQIAFIDGKIIAQKGFGLNLRSKEYQVEKERLLNTTKPIYDK
IPTVQSTKNQTTNITSPSLISDSPNKAINKIKSTSTSTTPNTQEQSTQHLPLVGSNLASAVLNKKEDTLQTAFNISDNSL
AGKHIFSVKQFNRKQLHALFGIAHEMRILVKRSGGSDLLKGKVLATLFYEPSTRTQCSFTAAMQRLGGSVVTVDNVSSSV
AKGESIADTIQTLESYCDAVCMRHPAVGSVESAIQVAKKPIINAGDGVGEHPTQALLDVFTIREELGTVNGLTITVVGDL
KHGRTVHSLVRLLANYQVKINYVSPSSLSMPTEIIKELNEKGIEQKEYTNIESILPTTNVLYVTRVQKERFQSIEEYEKV
KDSFIITPHTLTKASDNMIVMHPLPRINEISPEVDSDPRAAYFRQMENGLYVRMSLLALVFGAGV
>ecocyc__ASPCARBCAT-MONOMER aspartate carbamoyltransferase catalytic subunit (Escherichia coli K-12 substr. MG1655)
MANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTSLGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSGNVPVLNAGDGSNQHPTQTLLDLFTIQETQGRLDNLHVAMVGDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPQYILDMLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEYANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQALLALVLNRDLVL
>biolip__2a0fA Structure of d236a mutant e. Coli aspartate transcarbamoylase in presence of phosphonoacetamide at 2.90 a resolution
ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTSLGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSGNVPVLNAGDGSNQHPTQTLLDLFTIQETQGRLDNLHVAMVGDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPQYILDMLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLAPSEYANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQALLALVLNRDLVL
>PDB_2hse_A Structure of d236a e. Coli aspartate transcarbamoylase in the presence of phosphonoacetamide and l-aspartate at 2.60 a resolution
ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTS
LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSGNVPVLNAGDGSNQHPTQTLLDLFTIQETQGRLDNLHVAMV
GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPQYILDMLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLAPSEY
ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQALLALVLNRDLVL
>PDB_5vmq_C Structure of the r105a mutant catalytic trimer of escherichia coli aspartate transcarbamoylase at 2.0-a resolution
ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTS
LGKKGETLADTISVISTYVDAIVMAHPQEGAARLATEFSGNVPVLNAGDGSNQHPTQTLLDLFTIQETQGRLDNLHVAMV
GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPQYILDMLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY
ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQALLALVLNRDLV
>PDB_1acm_A Arginine 54 in the active site of escherichia coli aspartate transcarbamoylase is critical for catalysis: a site-specific mutagenesis, nmr and x-ray crystallography study
ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFEASTATRLSFQTSMHRLGASVVGFSDSANTS
LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSGNVPVLNAGDGSNQHPTQTLLDLFTIQQTEGRLDNLHVAMV
GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPEYILDMLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY
ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQALLALVLNRDLVL
>CharProtDB__CH_088346 aspartate carbamoyltransferase catalytic chain; EC 2.1.3.2 (Salmonella enterica subsp. enterica serovar Typhimurium)
MANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTSLGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSGQVPVLNAGDGSNQHPTQTLLDLFTIQETQGRLDNLHIAMVGDLKYGRTVHSLTQALAKFSGNRFYFIAPDALAMPQYILDMLDEKGMAWSLHGSIEEVMADVDILYMTRVQKERLDPSEYANVKAQFVLRASDLNGARENMKVLHPLPRIDEITTDVDKTPHAWYFQQAGNGIFARQALLALVLNSELSL
>BRENDA__Q55338 aspartate carbamoyltransferase (EC 2.1.3.2) (Sulfolobus acidocaldarius)
MKHIISAYNFSRDELEDIFALTDKYSKNLNDTRKILSGKTISIAFFEPSTRTYLSFQKAIINLGGDVIGFSGEESTSVAKGENLADTIRMLNNYSDGIVMRHKYDGASRFASEISDIPVINAGDGKHEHPTQAVIDIYTINKHFNTIDGLVFALLGDLKYARTVNSLLRILTRFRPKLVYLISPQLLRARKEILDELNYPVKEVENPFEVINEVDVLYVTRIQKERFVDEMEYEKIKGSYIVSLDLANKMKKDSIILHPLPRVNEIDRKVDKTTKAKYFEQASYGVPVRMSILTKIYGE
>ENA__AAA62444.1 aspartate transcarbamoylase (Pisum sativum)
MTASSSLFSCSMHMEVLTPKISKWPKNFVSCHSKISYVETNYLKSTCYPISRFFCINNLKKTRQRDGIHCFSEGQKFQLDDVVEAQQFDRDILNAIFEVARDMEKIERNSPESQILKGYLMATLFYEPSTRTRLSFESAMRRLGGEVLTTENAREFSSAAKGETLEDTIRTVEGYSDLIVLRHFESGAARRAATIAGIPIVNAGDGPGQHPSQALLDVYTIEREIGKLDGIKVGLVGDLANGRTVRSLTYLLAKYKDVKIYFVSPEVVKMKDDIKDYLTSKGVDWEESSDLVEVASECDVVYQTRIQKERFGERLDLYEKARGKFIVNQNILNAMQRHAVIMHPLPRLDEITVDVDADPRAAYFRQAKYGLYIRMALLKLLLVGW
>ENA__AAA62443.1 aspartate carbamoyltransferase (Pisum sativum)
MTVASMLSSNSMNVGVSNPKMSSKTSACCLLNRPWPSSCSMSISSCGQFGVSEKSKLLCGAGALQVESAPLFSVGQKFQLDDVIEAQQFDRETLSAIFEVARSMENIRGNSSGSQMLKGYLMATLFYEPSTRTRLSFESAMKRLGGDVLTTENAREFSSAAKGETLEDTIRTVEGYSDIIVLRHFESGAARRAAATANIPVINAGDGPGQHPSQALLDVYTIEREIGKLDGIKVGLVGDLANGRTVRSLAYLLAKYRDVKLYFVSPNVVKMKDDIKEYLTSKGVEWEESSDLMEVASKCDVVYQTRIQKERFGEKLNLYEEARGKYIVNQDVLKVMQNHAVVMHPLPKLDEIEADVDNDPRAAYFRQAKNGLYIRMALLKVLLLGW
>SwissProt__Q91437 Multifunctional protein CAD; Carbamoyl phosphate synthetase 2-aspartate transcarbamylase-dihydroorotase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 (Squalus acanthias (Spiny dogfish))
MATLFLDDGSSFKGRLFGASSTVSGEVVFQTGMVGYPEALTDPSYLSQILVLTYPLIGNYGIPKDEEDEHGLSKWFESAKIHAAALVIGENSQNPSHWSSVRSLDQRLKEHGIPALEGIDTRSLTKKIREKGTLLGKLVIDGTDENSLPYDDPNKRHLVKEVSIKEPKVYHPSGNVKIMAVDCGMKYNQIRSLCKRGAAVTVVPWDYLFDSNEFDGLFISNGPGDPEYCQQTINNVKKAISEEKPKPLFGICLGHQILSLAIGAKTYKMKYGNRGHNQPCIHEGTQRCFYTSQNHGFAVEPCSLPRDWSVLFTNANDQSNEGIIHNSKPLFSVQFHPEHKAGPTDLVDLFDIFLECARDVKLGVNLDKTVKGRVISHYSFKNGTENSKTPPGRIQPHKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENVQSVLINPNIATVQTSKGLADKVYFLPITPEYVTQVIMNERPDGILLTFGGQTALNCGVELQKRGVLEKYHVRVLGTPVSSIEMTEDRKIFVEKMAEINEYVVPSEAAFTLEQAQGAAERLGYPVLVRAAFALGGLGSGFAQNKEELVTLVTQAFAHTSQILVDKSLKGWKEIEYEVVRDAYDNCITVCNMENVDPLGIHTGESIVVAPSQTLNDKEYNLLRTTAIKVIRHLGVVGECNIQYALSPESEQYFIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPVLRNSVTNSTTANYEPSLDYCVVKVPRWDLSKFLRLSTKIGSSMKSVGEVMAIGRNFEEAFQKALRMVDENCVGFDHTLKPASDEELETPTDKRIFVLAAALRAGYEIDRLYELTKIDKWFLHKMKNIVEYSLKLSELYMKDEVPRHDLLKVKRLGFSDKQIAMAIQSTELAVRRLRQEWKILPVVKQIDTVAAEWPAQTNYLYLTYNGEGHDLDFTKPHVMVIGSGVYRIGSSVEFDWCAVRCIQQLRKMGYKTRMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGIILSMGGQLPNNIAMDLHRQQCRILGTSPESIDTAENRFKFSRMLDTIGISQPRWKELSDTESSKQFCTKVGYPCLIRPSYVLSGVAMNVAYSDNDLEKFLSSAVAVSKEHPVVISKFIQEAKEIDVDAVACDGVVIAVAISEHVENAGVHSGDATLVTPPQDLNQKTTERIKAIVHAIGQELQATGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDMIALATKVIMGEEVEPVGLMTGTGVVGVKVPQFSFSRLAGADVVLGVEMTSTGEVACFGENRYEAYLKAMLSTGFKIPKKNILLSIGSYKNKSELLSTVQSLEQLGYNLYASLGTADFYTEHGVKIKAVDWPFEDTDNGCPLKERHRNIMDYLEENHFDLVINLSMRNSGGRRLSSFVTKGYRTRRLAVDYSVPLIIDIKCTKLFVEALRLVGDTPPVKTHIDSMSSHKLIRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTNPAITDQTSFALVQKLATAGARCDFALFLGASSDNADVLPLISNSAAGLKMYLNDTFSTLKMDNVSLWMEHFEKWPKHLPIVVHAERQTVAAILMVAQLYQRPVHICHVARKEEIQIIRAAKQKGVQVTCEVAPHHLFLNEEDLESIGHGKGQVRPMLSTKEDVNALWENLDVIDCFATDHAPHSVEEKNSDSPPPGYPGLETMLPLLLTAVSEGRLTIDDLVKRLYENPRKIFSLPVQENTYVEVDLEQEWIIPSYMQFTKSKWTPFEGKKVKGRVRRVVLRGEVAYIDGQVLVPPGYGQDVRAWPLGVPLPPPPTTVKTPEHSKPTQTETVRTRTASPRRLASSGPAVDARFHLPPRIHRCSDPGLPNAEGEYKEKPVKKFIEQDTVSQDGYIYPPPVSRLLSPQNLAAQAVPHPYSLLLHPFVGQHILSVKRFTKDQLSHLFNVAHNLRLTVQKDRSLDILKGKVMASMFYEVSTRTSSSFRAAMHRLGGSVIHFSEATSSVQKGESLLDSVQTMSCYVDVVVLRHPEPGAVELAAKHSRKPIINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLAYLLTLYRVNLRYVTPRNLRMPPNIIRFLASRGIKQEEFDSLEEALPDTDVLYMTRIQKERFASEEEYEACFGQFILTPHIMTKGKKKMVVMHPLPRVNEVSVEVDSDPRAAYFRQAENGMYVRMALLATVLGKF
>metacyc__AT3G20330-MONOMER aspartate carbamoyltransferase (EC 2.1.3.2) (Arabidopsis thaliana)
MSIASSLTSATLCGASVFPKALACSSEFPINLPSPFESSKICLTSFPASRDLKKNATLNLTRNVGPVRCHAMQAGTRELKKFELSDVIEGKQFDREMLSAIFDVAREMEKIEKSSSQSEILKGYLMATLFYEPSTRTRLSFESAMKRLGGEVLTTENAREFSSAAKGETLEDTIRTVEGYSDIIVMRHFESGAARKAAATANIPVINAGDGPGEHPTQALLDVYTIQSEIGKLDGISVALVGDLANGRTVRSLAYLLAKFKDVKIYFVSPEIVKMKDDIKDYLTSSGVEWEESSDLMEVASKCDVVYQTRIQRERFGERLDLYEAARGKYIVDKDLLGVMQKKAIIMHPLPRLDEITADVDADPRAAYFRQAKNGLFIRMALLKLLLVGW
>SwissProt_P49077 Aspartate carbamoyltransferase, chloroplastic; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Arabidopsis thaliana (Mouse-ear cress)
MSIASSLTSATLCGASVFPKALACSSEFPINLPSPFESSKICLTSFPASRDLKKNATLNLTRNVGPVRCHAMQAGTRELK
KFELSDVIEGKQFDREMLSAIFDVAREMEKIEKSSSQSEILKGYLMATLFYEPSTRTRLSFESAMKRLGGEVLTTENARE
FSSAAKGETLEDTIRTVEGYSDIIVMRHFESGAARKAAATANIPVINAGDGPGEHPTQALLDVYTIQSEIGKLDGISVAL
VGDLANGRTVRSLAYLLAKFKDVKIYFVSPEIVKMKDDIKDYLTSSGVEWEESSDLMEVASKCDVVYQTRIQRERFGERL
DLYEAARGKYIVDKDLLGVMQKKAIIMHPLPRLDEITADVDADPRAAYFRQAKNGLFIRMALLKLLLVGW
>SwissProt__P08955 Multifunctional protein CAD; Carbamoyl phosphate synthetase 2-aspartate transcarbamylase-dihydroorotase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 (Mesocricetus auratus (Golden hamster))
MAALVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDEEDEFGLSKWFESSENHVAGLVVGECCPTPSHWSATCTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQSGTEPSTLPFVDPNARPLAPEVSIKTPRVFNAGGAPRICALDCGLKYNQIRCLCQLGAEVTVVPWNHELDSQKYDGLFLSNGPGDPASYPGVVATLNRVLSEPNPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAVDADSLPAGWTPLFTNANDCSNEGIVHDSLPFFSVQFHPEHRAGPSDMELLFDVFLETVREAVAGNPGGQTVKERLVQRLCPPGLLIPGSGLPPPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVLLTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASTKEELSALVAPAFAHTSQVLIDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGESIVVAPSQTLNDREYQLLRRTAIKVTQHLGIVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPELRNSVTGGTAAFEPSLDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENCVGFDHTVKPVSDVELETPTDKRIFVVAAALWAGYSVERLYELTRIDCWFLHRMKRIVTHAQLLEQHRGQPLSQDLLHQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGNTHDLDFRTPHVLVLGSGVYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPDGVILSMGGQLPNNMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVACDGVVSAIAISEHVENAGVHSGDATLVTPPQDITPKTLERIKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRIIMGEKVEPIGLMTGSGVVGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIGSYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGECPPQRSILDQLAENHFELVINLSMRGAGGRRLSSFVTKGYRTRRLAADFSVPLIIDIKCTKLFVEALGQIGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASSENAGTLGAVAGSAAGLKLYLNETFSELRLDSVAQWMEHFETWPSHLPIVAHAERQSVAAVLMVAQLTQRPVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERLGPGRGEVRPELGSREDMEALWENMAVIDCFASDHAPHTLEEKCGPKPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPLQEDTYVEVDLEHEWTIPSHMPFSKARWTPFEGQKVKGTIRRVVLRGEVAYIDGQVLVPPGYGQDVRKWPQGAVPQPPPSAPATTEITTTPERPRRVIPGLPDGRFHLPPRIHRASDPGLPAEEPKEKPSRKVVEPELMGTPDGPCYPAPPVPRQASPQNLGSSGLLHPQTSPLLHSLVGQHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLRMPPSVWDFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSTQEYEACFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGRF
>biolip__6yvbC Arabidopsis aspartate transcarbamoylase complex with carbamoyl phosphate
HHSSGLEVLFQGPHMFELSDVIEGKQFDREMLSAIFDVAREMEKIEKSSSQSEILKGYLMATLFYEPSTRTRLSFESAMKRLGGEVLTTENAREFSSAAKGETLEDTIRTVEGYSDIIVMRHFESGAARKAAATANIPVINAGDGPGEHPTQALLDVYTIQSEIGKLDGISVALVGDLANGRTVRSLAYLLAKFKDVKIYFVSPEIVKMKDDIKDYLTSSGVEWEESSDLMEVASKCDVVYQTRIQRERFGERLDLYEAARGKFIVDKDLLGVMQKKAIIMHPLPRLDEITADVDADPRAAYFRQAKNGLFIRMALLKLLLVGW
>biolip__5g1nE Aspartate transcarbamoylase domain of human cad bound to pala
HSLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSTQEYEACFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGRF
>PDB_6ys6_B Arabidopsis aspartate transcarbamoylase complex with pala
PHMFELSDVIEGKQFDREMLSAIFDVAREMEKIEKSSSQSEILKGYLMATLFYEPSTRTRLSFESAMKRLGGEVLTTENA
REFSSAAKGETLEDTIRTVEGYSDIIVMRHFESGAARKAAATANIPVINAGDGPGEHPTQALLDVYTIQSEIGKLDGISV
ALVGDLANGRTVRSLAYLLAKFKDVKIYFVSPEIVKMKDDIKDYLTSSGVEWEESSDLMEVASKCDVVYQTRIQRERFGE
RLDLYEAARGKFIVDKDLLGVMQKKAIIMHPLPRLDEITADVDADPRAAYFRQAKNGLFIRMALLKLLLVGW
>PDB_6ypo_A Arabidopsis aspartate transcarbamoylase bound to ump
PHMFELSDVIEGKQFDREMLSAIFDVAREMEKIEKSSSQSEILKGYLMATLFYEPSTRTRLSFESAMKRLGGEVLTTENA
REFSSAAKGETLEDTIRTVEGYSDIIVMRHFESGAARKAAATANIPVINAGDGPGEHPTQALLDVYTIQSEIGKLDGISV
ALVGDLANGRTVRSLAYLLAKFKDVKIYFVSPEIVKMKDDIKDYLTSSGVEWEESSDLMEVASKCDVVYQTRIQRERFGE
RLDLYEAARGKFIVDKDLLGVMQKKAIIMHPLPRLDEITADVDADPRAAYFRQAKNGLFIRMALLKLLLVGW
>metacyc__ENSG00000084774-MONOMER CAD protein (EC 3.5.2.3; EC 6.3.5.5; EC 2.1.3.2) (Homo sapiens)
MAALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDEMDEFGLCKWFESSGIHVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQNGTEPSSLPFLDPNARPLVPEVSIKTPRVFNTGGAPRILALDCGLKYNQIRCLCQRGAEVTVVPWDHALDSQEYEGLFLSNGPGDPASYPSVVSTLSRVLSEPNPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWAPLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVKEATAGNPGGQTVRERLTERLCPPGIPTPGSGLPPPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVLLTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREELSALVAPAFAHTSQVLVDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGESIVVAPSQTLNDREYQLLRQTAIKVTQHLGIVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPELRNSVTGGTAAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENCVGFDHTVKPVSDMELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHRGQPLPPDLLQQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRTPHVLVLGSGVYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPNNMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVASDGVVAAIAISEHVENAGVHSGDATLVTPPQDITAKTLERIKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVGLMTGSGVVGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIGSYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGECPPQRSILEQLAEKNFELVINLSMRGAGGRRLSSFVTKGYRTRRLAADFSVPLIIDIKCTKLFVEALGQIGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASSENAGTLGTVAGSAAGLKLYLNETFSELRLDSVVQWMEHFETWPSHLPIVAHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPGKGEVRPELGSRQDVEALWENMAVIDCFASDHAPHTLEEKCGSRPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPGYGQDVRKWPQGAVPQLPPSAPATSEMTTTPERPRRGIPGLPDGRFHLPPRIHRASDPGLPAEEPKEKSSRKVAEPELMGTPDGTCYPPPPVPRQASPQNLGTPGLLHPQTSPLLHSLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSTQEYEACFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGRF
>ENA__CAC85728.1 aspartate carbamoyltransferase (Solanum tuberosum)
MTISATFSSHGKILMSPLRKSEWANQPVLCKSVELFKNGRNQYRMSTNSNKFQCRALEIENKSSTKFHLDDVIESQQFDRETLSAIFEVAREMEKIEKNSIGGRSEILKGYLMATLFYEPSTRTRLSFESAMKRLGGEVLTTENAREFSSAAKGETLEDTIRTVEGYSDIIVMRHFESGAARRAATTASIPIINAGDGPGQHPTQALLDVYTIEREIGKLDGINVALVGDLAYGRTVRSLAHLLAMYEDVKIYFVSPDVVKMKDDIKDYLTSMGVQWEENADLIEVASKCDVVYQTRIQRERFGERVDLYEEARGKYIVDMSVVNAMQKHAVVMHPLPRLDEITVDVDGDPRAAYFRQAKNGLYIRMALLKLLLLGW
>SwissProt__Q7S8A6 Multifunctional protein pyr-3; PyrABCN; Pyrimidine-specific carbamoyl phosphate synthase-aspartate carbamoyl transferase; CPSase-ATCase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2 (Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987))
MAATVYRPATAPIADAPCEGLVCLELEDGSAYQGYSFGAPKSIAGELVFQTGMVGYPESVTDPSYRGQILVITFPLVGNYGVPSRETVDDLLKDLPAHFESNQIHIAGLVTASYAGEDFSHFLATSSLGTWLKEQGIPAMYGVDTRALTKRIREKGSMLGRMLLQKEDLAVSAPSLGVPGDWKPHFETIEWVNPNEKNLVAEVSIKEPKLYKPDEATALKHPSGRNLRILCLDVGMKYNQLRCFIKRGVEVLVCPWDYDFSKEEYDGLFISNGPGDPKVMDTTVEHISAALQKNNTPIFGICLGHQLLARAAGAKTVKLKFGNRGHNIPCTSMVTGKCHITSQNHGYAVDATTLPTGWQELFINANDGSNEGIMHVDRPHFSVQFHPESTPGPRDTEFLFDVFIQTVAKCTTDNTLLQKGVEFPGGTTEENERLHPRVDVKKVLVLGSGGLSIGQAGEFDYSGSQAIKALKEEGIYTVLINPNIATIQTSKGLADKVYFLPVNAEFVRKVIKYEQPDAIYCTFGGQTALSVGIQLKDEFEALGVKVLGTPIDTIITTEDRELFARSMESIGEKCAKSASASSVEEALNAVKDIGYPVIVRAAYALGGLGSGFANNEAELVDLCNKALAASPQVLVERSMKGWKEIEYEVVRDAQDNCITVCNMENFDPLGIHTGDSIVVAPSQTLSDEDYNMLRTTAVNVIRHLGVVGECNIQYALNPFSREYCIIEVNARLSRSSALASKATGYPLAFIAAKLGLGIPLKEIKNTVTKVTCACFEPSLDYVVVKMPRWDLKKFTRVSTQLGSSMKSVGEVMSIGRTFEEAIQKAIRAIDFHNLGFSESKGALMSVDDELQTPSDQRLFAIANAMHAGYTVDRIWELTKIDKWFLSKLKGLSNFAKDMTKLTANDVVGRPDLLLRAKQLGFCDRQLANFWDSNELAIRRMRLEAGITPFVKQIDTVAAEFPAFTNYLYLTYNASEHDVSFEDRGVMVLGSGVYRIGSSVEFDWCSVRAIRTLRESGFKTIMVNYNPETVSTDYDEADKLYFENINLETVLDVYQMEDATGVLGAMGGQTPNNIALPLLRAGVRVLGTSPEMIDTAENRYKFSRMLDRIGVDQPTWKELTSFDEAKAFCQKVSYPVLVRPSYVLSGAAMNTVYSEADLESYLQQAADVSPEHPVVITKYIENAKEIEMDAVAKDGKVVGHFISEHVENAGVHSGDATLILPPQDLEQTTIQRIEEATRKIGAALNVTGPFNIQFIAKDNDIKVIECNVRASRSFPFVSKVMGVDLIEMATKAIMGLPFVEYPAIDRPSGGVGVKVPQFSFSRLSGADPVLGVEMASTGEVASFGVDKYEAYLKALMSTGFKVPKKNILLSIGSYKDKKEMLPSVAKLSQMGYKLFATAGTADFLQEHDIPVQFLEVLAKEDDQKSEYSLTQHLANNMIDLYINLPSNNRYRRPANYISKGYQTRRMAVDYQIPLVTNVKNAKILVEAIARYRDMEIGERDYQTSHTPLQLSGQVNFTLQDSLSRPHSFKKAHVLSVEQYTRADLHLLFTVAEEMRLSVQRGNVMDILKGRMLATLFYEPSTRTSASFEAAMKRLGGEVISIATQHSSVQKGETLQDTLRTLACYADAIVLRHPDETCVDVAKKYSPVPVVNAGNGSREHPTQAFLDLFTVREELGTVQGLTFTFVGDLRYGRPVHSLVYLLRHYSGVKVQLVSPKGLELPTDVRQQLVKAGQLLCESETLTPEILGKTDVLYCTRVQKERFPSEAEYEKVKGSYRIDNQTLKHAKSKMAIMHPLPRNEEIAEEVDFDQRAAYFRQMRYGLYCRMALLALVMSG
>biolip__8bplA Aspartate transcarbamoylase mutant (n2045c, r2238c) from chaetomium thermophilum cad-like bound to carbamoyl phosphate
SPLQEMLAAPSSFKKSHVLSVTQFTRADLHLLFQIAQEMRLGVQREGVLDILRGKVLCTLFYEPSTRTSASFDAAMQRLGGRTIPIQTSTSSVQKGETLQDTLRTLACYSDAIVLRHPDEKCVDVAKKYCPVPVINGGNGSKEHPTQAFLDLFTIREELGTMQGLTITFVGDLLYGRPVHSLVYLLRHYQVKVQLVSPKALRLPPAVRQQLVDAGQLLCESEALTPEILGRTDVLYCTRVQKERFPSLAEFEAVKDSYRIDYSTLKYAKPTTVVMHPLPRNEEVAEEVDFDQRAAYFRQMCYGLYCRMALLALVMS
>metacyc__YJL130C-MONOMER carbamoyl phosphate synthase/aspartate carbamoyltransferase (EC 2.1.3.2; EC 6.3.5.5) (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
MATIAPTAPITPPMESTGDRLVTLELKDGTVLQGYSFGAEKSVAGELVFQTGMVGYPESVTDPSYEGQILVITYPLVGNYGVPDMHLRDELVEELPRYFESNRIHIAGLVISHYTDEYSHYLAKSSLGKWLQNEGIPAVYGVDTRSLTKHLRDAGSMLGRLSLEKSGSDRTISRSSSWRSAFDVPEWVDPNVQNLVSKVSINEPKLYVPPADNKHIELQTGPDGKVLRILAIDVGMKYNQIRCFIKRGVELKVVPWNYDFTKEDYDGLFISNGPGDPSVLDDLSQRLSNVLEAKKTPVFGICLGHQLIARAAGASTLKLKFGNRGHNIPCTSTISGRCYITSQNHGFAVDVDTLTSGWKPLFVNANDDSNEGIYHSELPYFSVQFHPESTPGPRDTEFLFDVFIQAVKEFKYTQVLKPIAFPGGLLEDNVKAHPRIEAKKVLVLGSGGLSIGQAGEFDYSGSQAIKALKEEGIYTILINPNIATIQTSKGLADKVYFVPVTAEFVRKVILHERPDAIYVTFGGQTALSVGIAMKDEFEALGVKVLGTPIDTIITTEDRELFSNAIDEINEKCAKSQAANSVDEALAAVKEIGFPVIVRAAYALGGLGSGFANNEKELVDLCNVAFSSSPQVLVEKSMKGWKEVEYEVVRDAFDNCITVCNMENFDPLGIHTGDSIVVAPSQTLSDEDYNMLRTTAVNVIRHLGVVGECNIQYALNPVSKDYCIIEVNARLSRSSALASKATGYPLAYTAAKLGLNIPLNEVKNSVTKSTCACFEPSLDYCVVKMPRWDLKKFTRVSTELSSSMKSVGEVMSIGRTFEEAIQKAIRSTEYANLGFNETDLDIDIDYELNNPTDMRVFAIANAFAKKGYSVDKVWEMTRIDKWFLNKLHDLVQFAEKISSFGTKEELPSLVLRQAKQLGFDDRQIARFLDSNEVAIRRLRKEYGITPFVKQIDTVAAEFPAYTNYLYMTYNADSHDLSFDDHGVMVLGSGVYRIGSSVEFDWCAVTAVRTLRANNIKTIMVNYNPETVSTDYDEADRLYFETINLERVLDIYEIENSSGVVVSMGGQTSNNIAMTLHRENVKILGTSPDMIDSAENRYKFSRMLDQIGVDQPAWKELTSMDEAESFAEKVGYPVLVRPSYVLSGAAMNTVYSKNDLESYLNQAVEVSRDYPVVITKYIENAKEIEMDAVARNGELVMHVVSEHVENAGVHSGDATLIVPPQDLAPETVDRIVVATAKIGKALKITGPYNIQFIAKDNEIKVIECNVRASRSFPFISKVVGVNLIELATKAIMGLPLTPYPVEKLPDDYVAVKVPQFSFPRLAGADPVLGVEMASTGEVATFGHSKYEAYLKSLLATGFKLPKKNILLSIGSYKEKQELLSSVQKLYNMGYKLFATSGTADFLSEHGIAVQYLEVLNKDDDDQKSEYSLTQHLANNEIDLYINLPSANRFRRPASYVSKGYKTRRLAVDYSVPLVTNVKCAKLLIEAISRNITLDVSERDAQTSHRTITLPGLINIATYVPNASHVIKGPAELKETTRLFLESGFTYCQLMPRSISGPVITDVASLKAANSVSQDSSYTDFSFTIAGTAHNAHSVTQSASKVTALFLPLRELKNKITAVAELLNQWPTEKQVIAEAKTADLASVLLLTSLQNRSIHITGVSNKEDLALIMTVKAKDPRVTCDVNIYSLFIAQDDYPEAVFLPTKEDQEFFWNNLDSIDAFSVGALPVALANVTGNKVDVGMGIKDSLPLLLAAVEEGKLTIDDIVLRLHDNPAKIFNIPTQDSVVEIDLDYSFRRNKRWSPFNKDMNGGIERVVYNGETLVLSGELVSPGAKGKCIVNPSPASITASAELQSTSAKRRFSITEEAIADNLDAAEDAIPEQPLEQKLMSSRPPRELVAPGAIQNLIRSNNPFRGRHILSIKQFKRSDFHVLFAVAQELRAAVAREGVLDLMKGHVITTIFFEPSTRTCSSFIAAMERLGGRIVNVNPLVSSVKKGETLQDTIRTLACYSDAIVMRHSEEMSVHIAAKYSPVPIINGGNGSREHPTQAFLDLFTIREEIGTVNGITVTFMGDLKHGRTVHSLCRLLMHYQVRINLVSPPELRLPEGLREELRKAGLLGVESIELTPHIISKTDVLYCTRVQEERFNSPEEYARLKDTYIVDNKILAHAKENMAIMHPLPRVNEIKEEVDYDHRAAYFRQMKYGLFVRMALLAMVMGVDM
>PDB_5g1p_A Aspartate transcarbamoylase domain of human cad bound to carbamoyl phosphate
VGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSV
QKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDL
KHGRTVHSLACLLTQYRVSLRYVAPPSLRMPPTVRAFVASGTKQEEFESIEEALPDTDVLYMTRIQKERFQFILTPHIMT
RAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGRF
>SwissProt__Q09794 Multifunctional protein ura1; Pyrimidine-specific carbamoyl phosphate synthase-aspartate carbamoyl transferase; CPSase-ATCase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2 (Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast))
MSGLLPSLSSSFPLVQSEALGMPRTHGPKPSENDPKEPTCSPSPAFYSVNGEMKDYKLMALELEDKSVLQGYSFGADHSVSGELVFQTGMVGYPESLTDPSYRGQILVFTFPTVGNYGVPDRRILDEISGLPKYFESNQIHVAAIIISSYSQNYSHFLAHSSLGEWLKEQGIPGIFGIDTRALTKKIRDQGSMLGRLLIQKDESPINPSSITGLGKDWSTAFEDIPWKNPNTENLTSQVSIKEPKLYEPHPTTAIKKADGKIIRILVIDVGMKYNQIRCFLNRGVELLVVPWDYDFTKETYDGLFISNGPGDPSLMDLVVDRVKRVLESKTVPVFGICFGHQIMARAAGASTTKMKFGNRGHNIPCTCMISGRCYITSQNHGYAVDASSLSNGWKELFVNANDGSNEGIYNTEYPFFSVQFHPESTPGPRDTEFLFDVFIDVVKRSADAKSLQPFKLPGGTIEENRSRHPLVDAKRVLILGSGGLSIGQAGEFDYSGSQAIKALREEGIYTILINPNIATIQTSKGLADKVYFLPVNADFVRKVIKQERPDSIYVTFGGQTALNVGIELKDEFEQLGVKVLGTPIDTIITTEDRELFARAMDEINEKCAKSASASSIEEAIKVSKDISFPVIVRAAYALGGLGSGFADNEAELIDLCTLAFATSPQVLIERSMKGWKEIEYEVVRDAFDNCITVCNMENFDPLGIHTGDSIVVAPSQTLTDEDYNMLRTTAVNVIRHLGVVGECNIQYALNPFTKEYCIIEVNARLSRSSALASKATGYPLAFTAAKLGLNIPLNEVKNSVTKVTCACFEPSLDYVVVKIPRWDLKKFTRVSTQLSSAMKSVGEVMSIGRTFEEAIQKAIRAIDYSNTGFNVKDALMSIDTELQTPSDQRLFAIANAMASGYSVDRIWELTRIDKWFLEKLMGLIRTSQLISKHDISSLPISLLKTAKQLGFADVQIAAFMNSTELAVRRIRTEAGIRPFVKQIDTVAAEFPAFTNYLYTTYNAVEHDIHFNDKGVMVLGSGVYRIGSSVEFDWCAVRAVRTLRDRGVKTIMVNYNPETVSTDYDEADRLYFENIGLETVLDIYEQESSSGIIIAMGGQTANNIALPLHRENVKILGTSPEMIDGAENRFKFSRMLDDIGVDQPKWKELTSFDEADKFCDTVGYPVLVRPSYVLSGAAMNTVYSQSDLHSYLQQAVAINKDHPVVISKYIENAKEIELDAVAREGKMVMHVISEHVENAGVHSGDATLVLPPQDLAPTTIERIVDAAAKIGEALNITGPYNIQFIAKDNEIKVIECNVRASRSFPFVSKVIGVDMISMATDVIMGNPIQPYPDVDLPRDYVAVKVPQFSFSRLSGADPVLGVEMASTGEVACFGHNKFEAYLKAMISTGFRLPKKNILISIGSYKEKAELLPYVKKLYENNYNIFATAGTSDYFMESGVPCKYLADLPAEEANNEYSLSAHLANNMIDMYINLPSNNRYRRPANYISSGYKSRRLAIDYSVPLVTNVKCAKLMIEAICRNLDFSLSTVDFQSSFQTANLPGLINISAFLPEFTSEAVSDYTKECIASGFTMARFLPFSTSSTLADKDSLSAVKKLALDHAHCDYNFSVIASSTNEVTISELTSESGCLFFHFEKDDSGIDHVTAVASHFNVWPDTQTVMTDAKSTTLASLLLLASLHNRRIHITNVSSKDDLNLIVLAKQRSLPVTFDVSVYSLFLNQNDYPGATFLPTADDQVEIWNKLSYIDCFSIGSIPSRLAKFVGNTAFTGFGVREAIPLLLTAVNEGRLTLKDVVDRFYSNPKAIFRLHDQDDSGVQLEVDRSVSWSSKDWTPFNGKKLYGSIQSVQFDGHDVFFDGELNFEHTYGRDYSSASLADKSKATRKVSALMSPGLPHAAPSLAEAFGQAPENKAHPDISLNMTPNFKPSHELVQLINSSPFYRKHIISVHQVTRSDLHVLFAIAHQMRIIVERQGVIDLCYGKLLCTMFFEPSTRTSSSFDAAMQRLGGKVVAVTASASSVNKGESLADTIRTLGCYGDAIVLRHPSIESARIAANFSPVPIINGGNGSKEHPTQAFLDLYTIREELGSVNGLTITFIGDLKYGRTVHSLARLLAFWHVELHLVSPEQLALPDDVKDDIRANGLNFIEHRELTKEVVAQSDVLYCTRVQKERFASVDEYEKLKDSFIVDNSVLASAKSHCIVMHPLPRNREISEEVDFDQRRAAYFRQMRYGLYIRMALLACVMGATEVAN
>BRENDA__Q8EHC7 nitrite reductase (cytochrome; ammonia-forming) (EC 1.7.2.2) (Shewanella oneidensis)
MNQFEGSHILSVNQLDLDSIQTIFNVAHRMMPYALREKRTKVLEGAILGNLFFEPSTRTRVSFGCAFNLLGGHVRETTGMASSSLSKGESLYDTARVLSTYSDVIAMRHPDSYSVKEFAEGSRVPVINGGDGSNEHPTQALLDLFTIQKELGHASRGIDGMHIAMVGDLKFGRTVHSLSRLLCMYKNISFTLISPTELAMPDYVISDIENAGHSIKITDQLEGHLDKADILYLTRIQEERFPSQEEANKYRGKFRLNRSIYTQHCKSNTVIMHPLPRDSRAQANELDNDLNSHPNLAIFRQADNGLLIRMALFALTLGVDSQLEKYECPVNWYSRKADR
>SwissProt__P05990 Multifunctional protein r; Protein rudimentary; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 (Drosophila melanogaster (Fruit fly))
MASTDCYLALEDGTVLPGYSFGYVPSENESKVGFGGEVVFQTGMVGYTEALTDRSYSGQILVLTYPLIGNYGVPAPDEDEHGLPLHFEWMKGVVQATALVVGEVAEEAFHWRKWKTLPDWLKQHKVPGIQDIDTRALTKKLREQGSMLGKIVYEKPPVEGLPKSSFVDPNVRNLAKECSVKERQVYGNPNGKGPRIAILDCGLKLNQLRCLLQRGASVTLLPWSARLEDEQFDALFLSNGPGNPESCDQIVQQVRKVIEEGQKPVFGICLGHQLLAKAIGCSTYKMKYGNRGHNLPCLHRATGRCLMTSQNHGYAVDLEQLPDGWSELFVNANDGTNEGIVHASKPYFSVQFHPEHHAGPQDTEFLFDVFMESIQQKDLTIPQLIEQRLRPTTPAIDSAPVMPRKVLILGSGGLSIGQAGEFDYSGSQAIKAMRESNIQTVLINPNIATVQTSKGMADKCYFLPLTPHYVEQVIKSERPNGVLLTFGGQTALNCGVQLERAGVFSKYNVRILGTPIQSIIETEDRKLFAERVNEIGEQVAPSEAVYSVAQALDAASRLGYPVMARAAFSLGGLGSGFANNEEELQSLAQQALAHSSQLIVDKSLKGWKEVEYEVVRDAYNNCITVCNMENFDPLGIHTGESIVVAPSQTLSDREYQMLRSTALKVIRHFGVVGECNIQYALCPHSEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGLPLPDIKNSVTGNTTACFEPSLDYCVVKIPRWDLAKFVRVSKHIGSSMKSVGEVMAIGRNFEEAFQKALRMVDSDVLGFDPDVVPLNKEQLAEQLSEPTDRRPFVIAAALQLGMSLRELHQLTNIDYWFLEKLERIILLQSLLTRNGSRTDAALLLKAKRFGFSDKQIAKYIKSTELAVRHQRQEFGIRPHVKQIDTVAGEWPASTNYLYHTYNGSEHDVDFPGGHTIVVGSGVYRIGSSVEFDWCAVGCLRELRKLQRPTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYEMENSEGIILSMGGQLPNNIAMDLHRQQAKVLGTSPESIDCAENRFKFSRMLDRKGILQPRWKELTNLQSAIEFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASEVSREHPVVISKFLTEAKEIDVDAVASDGRILCMAVSEHVENAGVHSGDATLVTPPQDLNAETLEAIKRITCDLASVLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLDHDFVATATRAIVGLDVEPLDVLHGVGKVGVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMMSTGFQIPKNAVLLSIGSFKHKMELLPSIRDLAKMGYKLYASMGTGDFYAEHGVNVESVQWTFDKTTPDDINGELRHLAEFLANKQFDLVINLPMSGGGARRVSSFMTHGYRTRRLAVDYSIPLVTDVKCTKLLVESMRMNGGKPPMKTHTDCMTSRRIVKLPGFIDVHVHLREPGATHKEDFASGTAAALAGGVTLVCAMPNTNPSIVDRETFTQFQELAKAGARCDYALYVGASDDNWAQVNELASHACGLKMYLNDTFGTLKLSDMTSWQRHLSHWPKRSPIVCHAERQSTAAVIMLAHLLDRSVHICHVARKEEIQLIRSAKEKGVKVTCEVCPHHLFLSTKDVERLGHGMSEVRPLLCSPEDQEALWENIDYIDVFATDHAPHTLAEKRSERPPPGFPGVETILPLLLQAVHEGRLTMEDIKRKFHRNPKIIFNLPDQAQTYVEVDLDEEWTITGNEMKSKSGWTPFEGTKVKGRVHRVVLRGEVAFVDGQVLVQPGFGQNVRPKQSPLASEASQDLLPSDNDANDTFTRLLTSEGPGGGVHGISTKVHFVDGANFLRPNSPSPRIRLDSASNTTLREYLQRTTNSNPVAHSLMGKHILAVDMFNKDHLNDIFNLAQLLKLRGTKDRPVDELLPGKIMASVFYEVSTRTQCSFAAAMLRLGGRVISMDNITSSVKKGESLEDSIKVVSSYADVVVLRHPSPGAVARAATFSRKPLINAGDGVGEHPTQALLDIFTIREEFGTVNGLTITMVGDLKNGRTVHSLARLLTLYNVNLQYVAPNSLQMPDEVVQFVHQRGVKQLFARDLKNVLPDTDVLYMTRIQRERFDNVEDYEKCCGHLVLTPEHMMRAKKRSIVLHPLPRLNEISREIDSDPRAAYFRQAEYGMYIRMALLAMVVGGRNTAL
>SwissProt__Q18990 Multifunctional protein pyr-1; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 (Caenorhabditis elegans)
MRATLHLEDGSTFVGSIYGATKSVVGEIVFQTGMVGYVESLTDPSYAKQLLTLTYPLIGNYGVPSAEILDQFKLPAEFESDRIWPAALIVEKICVDGEHSHWQAVQSLSEWLRKADVPCLSGIDVRQLVKKIRETGTMKAKLVIESDNAQNFDYVDVNAENLVDFVSRKEPVVYGSGDQTILAVDCGLKNNQIRCLAKRGFRVKVVPWNHPIDTESDYDGLFLSNGPGDPEICAPLVDRLAKVIARGDKPIFGICLGHQILSRAIGAKTYKLKYGNRGHNQPCTHYATGRCYITSQNHGYAVDPDSLPADWKALFTNENDKTNEGIVHSSKPFFSVQFHPEHTAGPTDCEFLFDVFADSVRQAKSGTFMNVDQELTRLMTFTPIYHAKEQRKVLVLGSGGLTIGQAGEFDYSGAQALKALREEGIRTVLINPNIATVQTSKGFADFTYFLPITKEYVTDVIKKERPTGILCTFGGQTALNCAIDLYKDGIFEQYDVQVLGTQINTIMKTEDRDLFNQEISAIGEKVAPSKAATTMEGAIEAAEELGYPVLVRAAYALGGLGSGFADNREELIAIAQQALAHSNQVLVDKSLKGWKEVEYEVVRDAYDNCITVCNMENVDPLGIHTGESVVVAPSQTLSDREYNALRTCAIKVIRHLGIIGECNIQYALDPYSLTYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGQHLPVIRNSVTGTTTACFEPSLDYCVVKIPRWDLGKFARVSTQIGSSMKSVGEVMGIGRCFEEALQKALRMVSDHADGFSPYTFSRPTTADDLSKPTDKRMFALARGMYYGDFDVEKAHELTRIDRWFLFRMQNIVDIYHRLEKTDVNTVSAELLLEAKQAGFSDRQIAKKIGSNEYTVREARFVKGITPCVKQIDTVAGEWPAQTNYLYTTFNGIENDVSFNMKNAVMVLGSGVYRIGSSVEFDSSCVGCIRELKALGYSTITVNCNPETVSTDYDICDRLYFEEISFETVLDVYHLEKPKGVILAFGGQAPNNIAMSLSRAQVKIFGTSPNDIDNAEDRFKFSRKLESLKISQPQWKKSENMEDAKNFCAQVGYPCLIRPSYVLSGAAMNVAHNAEDLEVFLKQAAVVAKEHPVVVSKFINEAKELDVDAVALDGKLVVMAVSEHIENAGVHSGDATLVTPAQDMNKLTLDRIKDITFRIAEAFNVNGPFNMQLIAKNNELKVIECNLRVSRSFPFVSKTLDYDFVALATRAMMASDSPAIRATIKPTATLLKGKGRVGVKVPQFSFSRLAGADVMLGVEMASTGEVACFGTSRCDAYLKALLSTGFVVPKQNIFISIGGYHAKAEMLKSVEALLKLGYELYGSKGTADYFQSNKINVKPVDWPFEEGSSDEKTASGTRSVVEFLENKEFHLVINLPIRGSGAYRVSAFRTHGYKTRRMAIDNGIPLITDIKCAKTFIQALEMVGKRPTMNSLVDCVTSKSLKRLPGMVDIHVHVREPGATHKEDWATCSKAALAGGVTTILAMPNTSPVLVDTDSFYQTEQLASAKSVVDYALYIGATPNNSKFAAEFADKAAGLKMYLNETFSTLKMDNISDWAKHLSAFPANRPIVCHAEKQTLAAILCMAQMANRAVHIAHVATADEINLVKEAKQRGWNVTCEVCPHHLFLIEEDLPDGIREVRPRLVKPEDRQALWDNMEYIDCFATDHAPHTWAEKTGKDGKIPPGFPGVEYMLPLLLTAVHDGKLTMKELTDRMSTNPRRIFNLPPQDDTYIEVDLNEEWTIPENGGQSKAGWTPFAGRKVFGKVHNVIIRGEEAVIDGRIVAIPGFGKNVRLYPHSGTAHRGDSDFDQILEPIPQQMIESSSDEQSPLHTPPRAHTPIAFPGELLAKNCISVKHLDKGQINRIFELADRYKHDVEKGHPLTHILNGKVLVNLFYEVSTRTSCSFSAAMQRLGGSVISVDSQSSSVQKGETLEDTVQVLGSYGDILVLRSNENGAADRAARVCDQPVINGGDGTGEHPTQALLDVYTIRQEMGTVNGLTIALVGDLKNGRTVHSLAKLLCLYKDITLHYVAPSTELEMPQEVLDYVSSKSNFVQKKFTSLAEGINHVDVVYVTRIQKERFSSPDEYNKVKGSYVINAKLLNEAARDVEEPSSLLVPARSLPIVMHPLPRVDEIAVELDHDERAAYFRQAKNGVFVRMSILSLLLGRGHL
>BRENDA__O15804 aspartate carbamoyltransferase (EC 2.1.3.2) (Plasmodium falciparum)
MIEIFCTAIVVITILIVGVFVYMIIRTKKKKLKLDNMFYINSKYKIDLDKIMTKMKNKSVINIDDVDDEELLAILYTSKQFEKILKNNEDSKYLENKVFCSVFLEPSTRTRCSFDAAILKLGSKVLNITDMNSTSFYKGETVEDAFKILSTYVDGIIYRDPSKKNVDIAVSSSSKPIINAGNGTGEHPTQSLLDFYTIHNYFPFILDRNINKKLNIAFVGDLKNGRTVHSLSKLLSRYNVSFNFVSCKSLNIPKDIVNTITYNLKKNNFYSDDSIKYFDNLEEGLEDVHIIYMTRIQKERFTDVDEYNQYKNAFILSNKTLENTRDDTKILHPLPRVNEIKVEVDSNPKSVYFTQAENGLYVRMALLYLIFSSTS
>biolip__7zeaB Crystal structure of truncated aspartate transcarbamoylase from plasmodium falciparum with bound inhibitor o-benzylhydroxylamine
FYINSKYKIDLDKIMTKMKNKSVINIDDVDDEELLAILYTSKQFEKILKNNEDSKYLENKVFCSVFLEPSTRTRCSFDAAILKLGSKVLNITDMNSTSFYKGETVEDAFKILSTYVDGIIYRDPSKKNVDIAVSSSSKPIINAGNGTGEHPTQSLLDFYTIHNYFPFILDRNINKKLNIAFVGDLKNGRTVHSLSKLLSRYNVSFNFVSCKSLNIPKDIVNTITYNLKKNNFYSDDSIKYFDNLEEGLEDVHIIYMTRIQKERFTDVDEYNQYKNAFILSNKTLENTRDDTKILHPLPRVNEIKVEVDSNPKSVYFTQAENGLYVRMALLYLIFSSTSSAWSHPQF
>PDB_7zid_B Crystal structure of truncated aspartate transcarbamoylase from plasmodium falciparum in complex with bda-14
DLDKIMTKMKNKSVINIDDVDDEELLAILYTSKQFEKILKNNEDSKYLENKVFCSVFLEPSTRTRCSFDAAILKLGSKVL
NITDMNSTSFYKGETVEDAFKILSTYVDGIIYRDPSKKNVDIAVSSSSKPIINAGNGTGEHPTQSLLDFYTIHNYFPFIL
DRNINKKLNIAFVGDLKNGRTVHSLSKLLSRYNVSFNFVSCKSLNIPKDIVNTITYNLKKNNFYSDDSIKYFDNLEEGLE
DVHIIYMTRIQKERFTDVDEYNQYKNAFILSNKTLENTRDDTKILHPLPRVNEIKVEVDSNPKSVYFTQAENGLYVRMAL
LYLIFSSTSSA
>BRENDA__Q6F4D1 dihydroorotate dehydrogenase (fumarate) (EC 1.3.98.1) (Neobodo saliens)
MQGTLQALRGAHIAGASQYNRTILEDLTALALHLKQLNAAGHVFDELRGKVMSPLFFENSSRTYASFVAAMQKLGGSVVALPIEASSVSKGETVSDTVRTMDAYSDVIVLRHPSVDAMADASRVSRAPVLNAGNGSGEHPTQALLDVVTMLAELGRIDGKTVVLVGDLKHGRTVHSLARVLANFNVAALHFVAPAGLEMPDSVASELLAAGVATETHAALTPELVAEADVVYLTRTQKERFASAEAYEAVKGTYRMDAALLAHAKSDMVVMHPLPRNEELSTDVDGDRRAAYMRQMNYGLYARMALLLVVLGRADEHARVASAAMAPREAARAVDLSVSVLGHTFANPLMNAAGVCCSTTEELDSLLASASGTLITKSCTAQQRDGNPAPRFKPLPLGSINSMGLPNEGYEYYAEYVSHRAKGGAAAKPIFFSISGMTMQDSADMAAKLAAHPQGANVLLELNLSCPNVPGKPQIGYDMQDMRRYLEAVTAVYPRPFGVKLPPYFDMAHFDQAAEVLNAFPSVAFLTCINSVGNGLVIDDTCDTVAIKPKNGFGGIGGEYVLPTALANVNAFRTRCPEKVIIGCGGVLCGRDAYQHLLAGASLVQVGTQLWKEGPDAFRRIRDELQAHLARKGYGADRDAIGKLKVIE
>CharProtDB__CH_122562 protein pyrABCN [Includes glutamine-dependent carbamoyl-phosphate; Aspartate carbamoyltransferase]; EC 2.1.3.2; EC 6.3.5.5 (Emericella nidulans)
MPETVGHEEPALPSSPQAGGAVAYNAISKELQPLPPTETANGGIIPPASSRIEGSTGRLCALELEDGTVYQGYNFGAEKSVAGELVFQTGMVGYPESITDPSYRGQILVITFPLVGNYGVPSRETMDELLKTLPKHFESTEIHIAALVVATYAGENYSHFLAESSLGQWLKEQGVPAIHGVDTRALTKRIRQKGSMLGRLLLHKADVAETDAALAQDTWKSSFEQIDWVDPNTKNLVSEVSIREPKLFSPPENVALKHPSSRPIRVLCLDVGLKFNQLRCLVARGVEVLVVPWDYDFPTLAGKDYDGLFVSNGPGDPATMTTTVNNLAKTMQEARTPIFGICLGHQLIARSVGAQTLKMKFGNRGHNIPCTSLVTGKCHITSQNHGYAVDSSTLPSDWQELFVNANDGSNEGIRHVSRPYFSVQFHPESTPGPRDTEYLFDVFINAIKDTIASPEALQKPVNFPGGAVAENIKASPRVSVKKVLILGSGGLSIGQAGEFDYSGSQAIKALKEEGIYTILINPNIATIQTSKGLADKVYFLPVNADFVRKVIKHERPDAIYVTFGGQTALQVGIQLKDEFESLGVKVLGTPIDTIITTEDRELFARSMDSIGEKCAKSASASSLEEALQVVESIGFPVIVRAAYALGGLGSGFADNLDELKDLCAKAFAASPQVLIERSMKGWKEIEYEVVRDARDNCITVCNMENFDPLGIHTGDSIVVAPSQTLSDEDYNMLRTTAVNVIRHLGVVGECNIQYALNPYSKEYCIIEVNARLSRSSALASKATGYPLAFIAAKLGLNIPLNEIKNSVTKVTCACFEPSLDYCVVKIPRWDLKKFTRVSTQLGSSMKSVGEVMAIGRTFEEAIQKAIRSVDFHNLGFNETNALMSIKTELQTPSDQRLFAIANAMAAGYSVDDIWKLTNIDKWFLTRLKGLSDFGKLMTNYNASTVTAPLLRQAKQLGFSDRQLAKFLSSNELAIRRLRVEAGIIPIVKQIDTVAAEFPSVTNYLYLTYNASEHDVRFDDNGIMVLGSGVYRIGSSVEFDWCSVRTIRTLREQGHKTVMVNYNPETVSTDYDEADRLYFENINLETVLDIYQLESSSGVIMSMGGQTPNNIALPLHRLNVRILGTSPEMIDGAENRYKFSRMLDRIGVDQPAWKELTSIEEAREFCDKVGYPVLVRPSYVLSGAAMNTVYSEHDLASYLNQAADVSREHPVVITKYIENAKEIEMDAVARNGVMVGHFISEHVENAGVHSGDATLILPPQDLDPETVRRIEEATRKIGNALNVTGPFNIQFIAKDNDIKVIECNVRASRSFPFVSKVMGVDLIEMATKAMIGAPFAEYPPVTIPKDYVGVKVPQFSFSRLAGADPVLGVEMASTGEVASFGRDKYEAYLKALLSTGFKLPKRNILLSIGSYKEKMEMLPSIIKLRDVGFELFATSGTADFLKENGVPVKYLEILPGEDEDIKSEYSLTQHLANNLIDLYINLPSSNRFRRPANYMSKGYRTRRMAVDYQTPLVTNVKNAKILIEAIARHYALNVQTIDYQTSHRSIILPGLINVGAFVPGLGSADSKDFEAVTKASIAAGFSMIRVMPVGVDSSITDARTLKLVQQNAGKASFCDYNFSVVATSSNSAEVGQLTGEVGSLFIPFNHLSGNISKVAAVTSHFGAWPSSKPIITDAKSTDLASVLLLASLHSRNIHVMSVTSKEDIGLIALSKEKGLKVTCDVSIYCLFLSRDDYPEAAFLPTAEDQKALWEHLSTIDIFSIGSIPYQLAGEKGSPAAGIAEALPLLFTAVSEGRLTVEDIIARLYENPKKIFELHDQSDSSVEVEIDRPYLFQSAQAWSPFSGKSVKGLVQRVIFQGKTSCLDSEITPDAPKGSDMSGHRIVPASPSLKAMSPRVDGALDRRQSISIAGTPARLGRKPVDHFPAATGAELGPPLYTPVPRASSPLLQMLSRSPFKQKHVLSVNQFNRADLHLLFTVAQEMRLGVQREGVLDILKGRLLCTLFYEPSTRTSASFDAAMQRLGGRTIAISTEHSSTKKGETLQDTLRTLGCYGDAVVLRHPEPSSTEVAAKFSPVPVINGGNGSVEHPTQAFLDLFTIREELGTVGGLTITFTGDLKYGRPVHSLIKLLQFYDVRVQLVAPKDLSLPADIRQQLLATGQLLTESEELTPEIVARSDVLYSTRVQKERFADLEQYERLKNSFIIDNALLKHAKSHMVVMHPLPRNAEVSEEVDFDQRAAYFRQVSLQSRGPSSEFDMLMWMQMRYGLYCRMALLALIMAP
>PDB_6hl7_A Crystal structure of truncated aspartate transcarbamoylase from plasmodium falciparum with mutated active site (r109a/k138a) and n- carbamoyl-l-phosphate bound
INSKYKIDLDKIMTKMKNKSVINIDDVDDEELLAILYTSKQFEKILKNNEDSKYLENKVFCSVFLEPSTATRCSFDAAIL
KLGSKVLNITDMNSTSFYAGETVEDAFKILSTYVDGIIYRDPSKKNVDIAVSSSSKPIINAGNGTGEHPTQSLLDFYTIH
NYFPFILDRNINKKLNIAFVGDLKNGRTVHSLSKLLSRYNVSFNFVSCKSLNIPKDIVNTITYNLKKNNFYSDDSIKYFD
NLEEGLEDVHIIYMTRIQKERFTDVDEYNQYKNAFILSNKTLENTRDDTKILHPLPRVNEIKVEVDSNPKSVYFTQAENG
LYVRMALLYLIFSST
>PDB_7zst_B Crystal structure of truncated aspartate transcarbamoylase from plasmodium falciparum in complex with fla-01
IDLDKIMTKMKNKSVINIDDVDDEELLAILYTSKQFEKILKNNEDSKYLENKVFCSVFLEPSTRTRCSFDAAILKLGSKV
LNITDMNSTSFYKGETVEDAFKILSTYVDGIIYRDPSKKNVDIAVSSSSKPIINAGNGTGEHPTQSLLDFYTIHNYFPFI
LDRNINKKLNIAFVGDLKNGRTVHSLSKLLSRYNVSFNFVSCKSLNIPKDIVNTITYNLKKNNFYSDDSIKYFDNLEEGL
EDVHIIYMTRIQKERFTDVDEYNNAFILSNKTLENTRDDTKILHPLPRVNEIKVEVDSNPKSVYFTQAENGLYVRMALLY
LIFSSTSSA
>PDB_6fba_A Crystal structure of truncated aspartate transcarbamoylase from plasmodium falciparum with bound inhibitor 2,3-naphthalenediol
DLDKIMTKMKNKSVINIDDVDDEELLAILYTSKQFEKILKNNEDSKYLENKVFCSVFLEPSTRTRCSFDAAILKLGSKVL
NITDMNSTSFYKGETVEDAFKILSTYVDGIIYRDPSKKNVDIAVSSSSKPIINAGNGTGEHPTQSLLDFYTIHNYFPFIL
DRNINKKLNIAFVGDLKNGRTVHSLSKLLSRYNVSFNFVSCKSLNIPKDIVNTITYNLKKNNFYSDDSIKYFDNLEEGLE
DVHIIYMTRIQKERYNQYKNAFILSNKTLENTRDDTKILHPLPRVNEIKVEVDSNPKSVYFTQAENGLYVRMALLYLIFS
S
>PDB_6jkt_A Crystal structure of aspartate transcarbamoylase from trypanosoma cruzi in complex with n-(phosphonacetyl)-l-aspartic acid (pala).
GSMLELPPVASLKGKSITSAEQFSRADIYALIHLASAMQRKIDAGEVLNLLQGRIMTPLFFEDSSRTFSSFCAAMIRLGG
SVVNFKVEASSINKGETLADTIRTLDSYSDVLVMRHPRQDAIEEALSVAQHPILNAGNGAGEHPTQALLDTLTIHSELGS
VDGITIALIGDLKMGRTVHSLLKLLVRNFSIKCVFLVAPDALQMPQDVLEPLQHEIATKGVIIHRTHALTDEVMQKSDVL
YTTRLQKERFDITIDAARMRLAKEKMIVMHPLPRNDELSTTVDADPRAAYFRQMRYGMFMRMAILWSVLA
>biolip__6jksD Crystal structure of aspartate transcarbamoylase from trypanosoma cruzi in complex with carbamoyl phosphate (cp) and aspartate (asp)
GSMLELPPVASLKGKSITSAEQFSRADIYALIHLASAMQRKIDAGEVLNLLQGRIMTPLFFEDSSRTFSSFCAAMIRLGGSVVNFKVEASSINKGETLADTIRTLDSYSDVLVMRHPRQDAIEEALSVAQHPILNAGNGAGEHPTQALLDTLTIHSELGSVDGITIALIGDLKMGRTVHSLLKLLVRNFSIKCVFLVAPDALQMPQDVLEPLQHEIATKGVIIHRTHALTDEVMQKSDVLYTTRLQKERFMASTSDDAAALQSFAAKADITIDAARMRLAKEKMIVMHPLPRNDELSTTVDADPRAAYFRQMRYGMFMRMAILWSVLA
>PDB_6jkt_F Crystal structure of aspartate transcarbamoylase from trypanosoma cruzi in complex with n-(phosphonacetyl)-l-aspartic acid (pala).
ELPPVASLKGKSITSAEQFSRADIYALIHLASAMQRKIDAGEVLNLLQGRIMTPLFFEDSSRTFSSFCAAMIRLGGSVVN
FKVETLADTIRTLDSYSDVLVMRHPRQDAIEEALSVAQHPILNAGNGAGEHPTQALLDTLTIHSELGSVDGITIALIGDL
KMGRTVHSLLKLLVRNFSIKCVFLVAPDALQMPQDVLEPLQHEIATKGVIIHRTHALTDEVMQKSDVLYTTRLQKERFDI
TIDAARMRLAKEKMIVMHPLPRNDELSTTVDADPRAAYFRQMRYGMFMRMAILWSVLA
>PDB_7zp2_A Crystal structure of truncated aspartate transcarbamoylase from plasmodium falciparum in complex with bda-04
YINSKYKIDLDKIMTKMKNKSVINIDDVDDEELLAILYTSKQFEKILKNNEDSKYLENKVFCSVFLEPSTRTRCSFDAAI
LKLGSKVLNITDMNSTSFYKGETVEDAFKILSTYVDGIIYRDPSKKNVDIAVSSSSKPIINAGNGTGEHPTQSLLDFYTI
HNYFPFILDRNINKKLNIAFVGDLKNGRTVHSLSKLLSRYNVSFNFVSCKSLNIPKDIVNTITYNLKKNNFYSDDSIKYF
DNLEEGLEDVHIIYMTRIQKNAFILSNKTLENTRDDTKILHPLPRVNEIKVEVDSNPKSVYFTQAENGLYVRMALLYLIF
SSTSHPQF
>PDB_7zhi_A Crystal structure of truncated aspartate transcarbamoylase from plasmodium falciparum with bound inhibitor indole
YINSKYKIDLDKIMTKMKNKSVINIDDVDDEELLAILYTSKQFEKILKNNEDSKYLENKVFCSVFLEPSTRTRCSFDAAI
LKLGSKVLNITDMNSTSFYKGETVEDAFKILSTYVDGIIYRDPSKKNVDIAVSSSSKPIINAGNGTGEHPTQSLLDFYTI
HNYFPFILDRNINKKLNIAFVGDLKNGRTVHSLSKLLSRYNVSFNFVSCKSLNIPKDIVNTITYNLKKNNFYSDDSIKYF
DNLEEGLEDVHIIYMTRIQKNAFILSNKTLENTRDDTKILHPLPRVNEIKVEVDSNPKSVYFTQAENGLYVRMALLYLIF
SSTSHPQF
>PDB_7zcz_A Crystal structure of truncated aspartate transcarbamoylase from plasmodium falciparum with bound inhibitor 1-(4-chlorophenyl) methanamine
YINSKYKIDLDKIMTKMKNKSVINIDDVDDEELLAILYTSKQFEKILKNNEDSKYLENKVFCSVFLEPSTRTRCSFDAAI
LKLGSKVLNITDMNSTSFYKGETVEDAFKILSTYVDGIIYRDPSKKNVDIAVSSSSKPIINAGNGTGEHPTQSLLDFYTI
HNYFPFILDRNINKKLNIAFVGDLKNGRTVHSLSKLLSRYNVSFNFVSCKSLNIPKDIVNTITYNLKKNNFYSDDSIKYF
DNLEEGLEDVHIIYMTRIQKNAFILSNKTLENTRDDTKILHPLPRVNEIKVEVDSNPKSVYFTQAENGLYVRMALLYLIF
SSTSHPQF
>biolip__6jkrE Crystal structure of aspartate transcarbamoylase from trypanosoma cruzi in complex with carbamoyl phosphate (cp)
GSMLELPPVASLKGKSITSAEQFSRADIYALIHLASAMQRKIDAGEVLNLLQGRIMTPLFFEDSSRTFSSFCAAMIRLGGSVVNFKVEASSINKGETLADTIRTLDSYSDVLVMRHPRQDAIEEALSVAQHPILNAGNGAGEHPTQALLDTLTIHSELGSVDGITIALIGDLKMGRTVHSLLKLLVRNFSIKCVFLVAPDALQMPQDVLEPLQHEIATKGVIIHRTHALTDEVMQKSDVLYTTRLQKADITIDAARMRLAKEKMIVMHPLPRNDELSTTVDADPRAAYFRQMRYGMFMRMAILWSVLA
>PDB_6jks_B Crystal structure of aspartate transcarbamoylase from trypanosoma cruzi in complex with carbamoyl phosphate (cp) and aspartate (asp)
SMLELPPVASLKGKSITSAEQFSRADIYALIHLASAMQRKIDAGEVLNLLQGRIMTPLFFEDSSRTFSSFCAAMIRLGGS
VVNFKVEASSINKGETLADTIRTLDSYSDVLVMRHPRQDAIEEALSVAQHPILNAGNGAGEHPTQALLDTLTIHSELGSV
DGITIALIGDLKMGRTVHSLLKLLVRNFSIKCVFLVAPDALQMPQDVLEPLQHEIATKGVIIHRTHALTDEVMQKSDVLY
TTRLQADITIDAARMRLAKEKMIVMHPLPRNDELSTTVDADPRAAYFRQMRYGMFMRMAILWSVLA
>PDB_6jl4_A Crystal structure of aspartate transcarbamoylase from trypanosoma cruzi in complex with carbamoyl aspartate (ca) and phosphate (pi)
MLELPPVASLKGKSITSAEQFSRADIYALIHLASAMQRKIDAGEVLNLLQGRIMTPLFFEDSSRTFSSFCAAMIRLGGSV
VNFKVEASSINKGETLADTIRTLDSYSDVLVMRHPRQDAIEEALSVAQHPILNAGNGAGEHPTQALLDTLTIHSELGSVD
GITIALIGDLKMGRTVHSLLKLLVRNFSIKCVFLVAPDALQMPQDVLEPLQHEIATKGVIIHRTHALTDEVMQKSDVLYT
TRLQAKADITIDAARMRLAKEKMIVMHPLPRNDELSTTVDADPRAAYFRQMRYGMFMRMAILWSVLA
>PDB_7zgs_A Crystal structure of truncated aspartate transcarbamoylase from plasmodium falciparum with bound inhibitor 2-phenylethan-1-amine
YINSKYKIDLDKIMTKMKNKSVINIDDVDDEELLAILYTSKQFEKILKNNEDSKYLENKVFCSVFLEPSTRTRCSFDAAI
LKLGSKVLNITDMNSTSFYKGETVEDAFKILSTYVDGIIYRDPSKKNVDIAVSSSSKPIINAGNGTGEHPTQSLLDFYTI
HNYFPFILDRNINKKLNIAFVGDLKNGRTVHSLSKLLSRYNVSFNFVSCKSLNIPKDIVNTITYNLKKNNFYSDDSIKYF
DNLEEGLEDVHIIYMTNAFILSNKTLENTRDDTKILHPLPRVNEIKVEVDSNPKSVYFTQAENGLYVRMALLYLIFSSTS
HPQF
>biolip__6hl7C Crystal structure of truncated aspartate transcarbamoylase from plasmodium falciparum with mutated active site (r109a/k138a) and n- carbamoyl-l-phosphate bound
MFYINSKYKIDLDKIMTKMKNKSVINIDDVDDEELLAILYTSKQFEKILKNNEDSKYLENKVFCSVFLEPSTATRCSFDAAILKLGSKVLNITDGETVEDAFKILSTYVDGIIYRDPSKKNVDIAVSSSSKPIINAGNGTGEHPTQSLLDFYTIHNYFPFILDRNINKKLNIAFVGDLKNGRTVHSLSKLLSRYNVSFNFVSCKSLNIPKDIVNTITYNLKKNNFYSDDSIKYFDNLEEGLEDVHIIYMTRINAFILSNKTLENTRDDTKILHPLPRVNEIKVEVDSNPKSVYFTQAENGLYVRMALLYLIFSSTWSHPQFE
>metacyc__MONOMER-21723 ureidoglycine carbamoyltransferase monomer (EC 2.1.3.16) (Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1))
MQKEAVRDAANLPSIRSLVRAVGFEGRSLHSINDLTNDQIYALFELARALEPFHRSSVDLLRGSVMVTLFFQPSTRTRMSFETAMHRLGGAVVTEANPLVSSSAAKEESLADTMRTISKYANVIVLRHPDDVAAREGASYSESPVINGGWGDWEHPTQALLDLYTLWRTHGGVEGAKVVVATPDMVHARTGHSMAYGLARLGAEVTLASRSDYRAPEEVIEGLRRVEGAKVREVFDLDQDGFNDLVSEMDLVYLPGCSAPKGEAAEEFKKMMDEYYVRLETLEKVRESEGRIIRVTHTLPRRPGEMDLRIDDTPHQQYFEAIAYSVAIRMALVAAIVGA
>metacyc__BSU15490-MONOMER aspartate carbamoyltransferase (EC 2.1.3.2) (Bacillus subtilis (strain 168))
MKHLTTMSELSTEEIKDLLQTAQELKSGKTDNQLTGKFAANLFFEPSTRTRFSFEVAEKKLGMNVLNLDGTSTSVQKGETLYDTIRTLESIGVDVCVIRHSEDEYYEELVSQVNIPILNAGDGCGQHPTQSLLDLMTIYEEFNTFKGLTVSIHGDIKHSRVARSNAEVLTRLGARVLFSGPSEWQDEENTFGTYVSMDEAVESSDVVMLLRIQNERHQSAVSQEGYLNKYGLTVERAERMKRHAIIMHPAPVNRGVEIDDSLVESEKSRIFKQMKNGVFIRMAVIQRALQTNVKRGEAAYVISH
>biolip__3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis
MKHLTTMSELSTEEIKDLLQTAQELKSGKTDNQLTGKFAANLFFEPSTRTRFSFEVAEKKLGMNVLNLDGTSTSVQKGETLYDTIRTLESIGVDVCVIRHSEDEYYEELVSQVNIPILNAGDGCGQHPTQSLLDLMTIYEEFNTFKGLTVSIHGDIKHSRVARSNAEVLTRLGARVLFSGPSEWQDEENTFGTYVSMDEAVESSDVVMLLRIQNERHQSAVSQEGYLNKYGLTVERAERMKRHAIIMHPAPVNRGVEIDDSLVESEKSRIFKQMKNGVFIRMAVIQRALQT
>SwissProt_P05654 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Bacillus subtilis (strain 168)
MKHLTTMSELSTEEIKDLLQTAQELKSGKTDNQLTGKFAANLFFEPSTRTRFSFEVAEKKLGMNVLNLDGTSTSVQKGET
LYDTIRTLESIGVDVCVIRHSEDEYYEELVSQVNIPILNAGDGCGQHPTQSLLDLMTIYEEFNTFKGLTVSIHGDIKHSR
VARSNAEVLTRLGARVLFSGPSEWQDEENTFGTYVSMDEAVESSDVVMLLRIQNERHQSAVSQEGYLNKYGLTVERAERM
KRHAIIMHPAPVNRGVEIDDSLVESEKSRIFKQMKNGVFIRMAVIQRALQTNVKRGEAAYVISH
>PDB_3r7l_A Crystal structure of pala-bound aspartate transcarbamoylase from bacillus subtilis
MKHLTTMSELSTEEIKDLLQTAQELKSGKTDNQLTGKFAANLFFEPSTRTRFSFEVAEKKLGMNVLNLDGTSTSVQKGET
LYDTIRTLESIGVDVCVIRHSEDEYYEELVSQVNIPILNAGDGCGQHPTQSLLDLMTIYEEFNTFKGLTVSIHGDIKHSR
VARSNAEVLTRLGARVLFSGPSEWQDEENTFGTYVSMDEAVESSDVVMLLRIQNERHQSAVSQEGYLNKYGLTVERAERM
KRHAIIMHPAPVNRGVEIDDSLVESEKSRIFKQMKNGVFIRMAVIQRALQ
>PDB_3r7f_A Crystal structure of cp-bound aspartate transcarbamoylase from bacillus subtilis
MKHLTTMSELSTEEIKDLLQTAQELKSGKTDNQLTGKFAANLFFEPSTRTRFSFEVAEKKLGMNVLNLDGTSTSVQKGET
LYDTIRTLESIGVDVCVIRHSEDEYYEELVSQVNIPILNAGDGCGQHPTQSLLDLMTIYEEFNTFKGLTVSIHGDIKHSR
VARSNAEVLTRLGARVLFSGPSEWQDEENTFGTYVSMDEAVESSDVVMLLRIQNERHQSAVSQEGYLNKYGLTVERAERM
KRHAIIMHPAPVNRGVEIDDSLVESEKSRIFKQMKNGVFIRMAVIQRALQT
>biolip__6pnzA The structure of the aspartate transcarbamoylase trimer from staphylococcus aureus complexed with pala at 2.27 resolution.
MNHLLSMEHLSTDQIYKLIQKASQFKSGERQLPNFEGKYVANLFFENSTRTKCSFEMAELKLGLKTISFETSTSSVSKGESLYDTCKTLESIGCDLLVIRHPFNNYYEKLANINIPIANAGDGSGQHPTQSLLDLMTIYEEYGYFEGLNVLICGDIKNSRVARSNYHSLKALGANVMFNSPNAWIDDSLEAPYVNIDDVIETVDIVMLLRIQHERHGLAEETRFAADDYHQKHGLNEVRYNKLQEHAIVMHPAPVNRGVEIQSDLVEASKSRIFKQMENGVYLRMAVIDELLK
>BRENDA__Q5SK66 aspartate carbamoyltransferase (EC 2.1.3.2) (Thermus thermophilus)
MRHLLDFQGWSRTEVESLLDTARVMREVLERPIKKVPALQGFTVATVFFEPSTRTRISFELAARRMSADVVSFAAQTSSLQKGESYKDTLLTLEAMGVDAYVIRADSAGVPHQATRWVKGAVINGGDGRRAHPTQALLDAYTLLEALGTLEGKKVAIVGDILHSRVARSGAELLSLLGAQVFCAGPPSLLPQSLPGAHLTPRLEEALEEADAVMVLRLQKERMEAGLVHLEDYVARYQVTEKRLALAKPQAPLLHPGPMNRDVELEGTLADSARSLVNRQVQNGVAVRMAVLYHLLVGREKA
>metacyc__ARGFBACSU-MONOMER ArgF (EC 2.1.3.3) (Bacillus subtilis (strain 168))
MHTVTQTSLYGKDLLTLKDLSEEDINALLAEAGELKQNKIQPIFHGKTLAMIFEKSSTRTRVSFEAGMAQLGGSALFLSQKDLQLGRGETVADTAKVLSGYVDAIMIRTFEHEKVEELAKEADIPVINGLTDKYHPCQALADLLTIKEIKGKLKGVKVAYIGDGNNVAHSLMIGCAKMGCDISIASPKGYEVLDEAAEAAKTYALQSGSSVTLTDDPIEAVKDADVIYSDVFTSMGQEAEEQERLAVFAPYQVNAALVSHAKPDYTFLHCLPAHREEEVTAEIIDGPNSAVFQQAENRLHVQKALLKAILYKGESSKNC
>ENA__CAA71345.1 aspartate carbamoyltransferase with fused catalytic and regulatory chains (Thermotoga maritima)
MKRDFLGRTLAVIEDLSVEEQMFLYEKTRELKQRWYSGEDVSDFRIKKRNVGIYIVFVEPSTRTKESFINAAKFHSGPNVKVNVFDSEHSSFNKQESYTDTFSMLTGYSDYSIFVVRTRLEGVCRLLERRISEFASRNGIEVPSFINAGDGKHEHPTQELLDEYTFLEQNGFDNSFIHVALVGDLLHGRTVHSKVNGLKIFKNVKVDLVAPEELMMPEHYVEKMKKNGFEVRIFSSIREYLDQKDVAKIWYFTRLQLERMGEDILEKVHVLREAVTFKKEYLDALPEGVKFYHPLPRHKVYPTIPNFLDTLPLNGWETQARNGYWVRIVLLSMFGGALEAPFDTSKKEEKPEEDFIIPAPITHGSKGVQKEGKRGIKPIENGTVIDHIAKGKTPEEIYSTILKIRKILRLYDVDSADGIFRSSDGSFKGYISLPDRYLSKKEIKKLSAISPNTTVNIIKNSTVVEKYRIKLPPTIYGFEELRCKNENCITNPAHGENASPSFVRNEKGQFICEYCETPHSFEEIT
>metacyc__MONOMER-503 PyrBI (EC 2.1.3.2) (Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8))
MKRDFLGRTLAVIEDLSVEEQMFLYEKTRELKQRWYSGEDVSDFRIKKRNVGIYIVFVEPSTRTKESFINAAKFHSGPNVKVNVFDSEHSSFNKQESYTDTFSMLTGYSDYSIFVVRTRLEGVCRLLERRISEFASRNGIEVPSFINAGDGKHEHPTQELLDEYTFLEQNGFDNSFIHVALVGDLLHGRTVHSKVNGLKIFKNVKVDLVAPEELMMPEHYVEKMKKNGFEVRIFSSIREYLDQKDVAKIWYFTRLQLERMGEDILEKVHVLREAVTFKKEYLDALPEGVKFYHPLPRHKVYPTIPNFLDTLPLNGWETQARNGYWVRIVLLSMFGGALEAPFDTSKKEEKPEEDFIIPAPITHGSKGVQKEGKRGIKPIENGTVIDHIAKGKTPEEIYSTILKIRKILRLYDVDSADGIFRSSDGSFKGYISLPDRYLSKKEIKKLSAISPNTTVNIIKNSTVVEKYRIKLPPTIYGFEELRCKNENCITNPAHGENASPSFVRNEKGQFICEYCETPHSFEEIWSI
>BRENDA__O66726 aspartate carbamoyltransferase (EC 2.1.3.2) (Aquifex aeolicus)
MRSLISSLDLTREEVEEILKYAKEFKEGKEETIKASAVLFFSEPSTRTRLSFEKAARELGIETYLVSGSESSTVKGESFFDTLKTFEGLGFDYVVFRVPFVFFPYKEIVKSLNLRLVNAGDGTHQHPSQGLIDFFTIKEHFGEVKDLRVLYVGDIKHSRVFRSGAPLLNMFGAKIGVCGPKTLIPRDVEVFKVDVFDDVDKGIDWADVVIWLRLQKERQKENYIPSESSYFKQFGLTKERFEKVKLYMHPGPVNRNVDIDHELVYTEKSLIQEQVKNGIPVRKAIYKFLWT
>PDB_3d6n_B Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase
MRSLISSLDLTREEVEEILKYAKEFKEGKEETIKASAVLFFSEPSTRTRLSFEKAARELGIETYLVSGSESSTVKGESFF
DTLKTFEGLGFDYVVFRVPFVFFPYKEIVKSLNLRLVNAGDGTHQHPSQGLIDFFTIKEHFGEVKDLRVLYVGDIKHSRV
FRSGAPLLNMFGAKIGVCGPKTLIPRDVEVFKVDVFDDVDKGIDWADVVIWLRLQKERQKENYIPSESSYFKQFGLTKER
FEKVKLYMHPGPVNRNVDIDHELVYTEKSLIQEQVKNGIPVRKAIYKFLWT
>metacyc__MONOMER-662 ArcB (EC 2.1.3.3) (Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1))
MEHLVDINDVESEEIEQLLDLAASMKENPGEFSGVMDNKSLVMLFAKPSTRTRLSFETGMTQLGGHGIFFEMGSSQLSRGEPISDVSQVMSRYEDAIMARLFEHDEMMELAENADVPVVNGLTDFLHPCQALTDMFTMQEKDRLDTLAFVGDGNNVAHSLMQASAKMGVDCRIATPEGMEPDEEIQDRVSDANVTVTNDPYEAVDGATAVYGDVFVSMGEEEQREEKLAEFDGFQIDQDLMDAARDDAIFMHCLPAHRGEEVTAEVADGPQSVIFDQAENRMHVQKAIVHTLVNQ
>BRENDA__O93656 ornithine carbamoyltransferase (EC 2.1.3.3) (Pyrococcus abyssi)
MVVSLKGRDLLCLQDYTPEEIWTILETAKMLKIWQKIGKPHRLLEGKTLAMIFQKPSTRTRVSFEVAMAHLGGHALYLNAQDLQLRRGETIADTARVLSRYVDAIMARVYDHKDVEDLAKYASVPVINGLSDFSHPCQALADYMTIWEKKGTIKGVKVVYVGDGNNVAHSLMIAGTKLGADVVVATPEGYEPDEKVIKWAEQNAAESGGSFELLHDPVKAVKDADVIYTDVWASMGQEAEAEERRKIFRPFQVNKDLVKHAKPDYMFMHCLPAHRGEEVTDDVIDSPNSVVWDEAENRLHAQKAVLALLLGGVKTGF
>SwissProt__Q51742 Ornithine carbamoyltransferase, anabolic; OTCase; EC 2.1.3.3 (Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1))
MVVSLAGRDLLCLQDYTAEEIWTILETAKMFKIWQKIGKPHRLLEGKTLAMIFQKPSTRTRVSFEVAMAHLGGHALYLNAQDLQLRRGETIADTARVLSRYVDAIMARVYDHKDVEDLAKYATVPVINGLSDFSHPCQALADYMTIWEKKGTIKGVKVVYVGDGNNVAHSLMIAGTKLGADVVVATPEGYEPDEKVIKWAEQNAAESGGSFELLHDPVKAVKDADVIYTDVWASMGQEAEAEERRKIFRPFQVNKDLVKHAKPDYMFMHCLPAHRGEEVTDDVIDSPNSVVWDQAENRLHAQKAVLALVMGGIKF
>biolip__4nf2A Crystal structure of anabolic ornithine carbamoyltransferase from bacillus anthracis in complex with carbamoyl phosphate and l- norvaline
QVPKLNTKDLLTLEELTQEEIISLIEFAIYLKKNKQEPLLQGKILGLIFDKHSTRTRVSFEAGMVQLGGHGMFLNGKEMQMQRGETVSDTAKVLSHYIDGIMIRTFSHADVEELAKESSIPVINGLTDDHHPCQALADLMTIYEETNTFKGIKLAYVGDGNNVCHSLLLASAKVGMHMTVATPVGYRPNEEIVKKALAIAKETGAEIEILHNPELAVNEADFIYTDVWMSMGQEGEEEKYTLFQPYQINKELVKHAKQTYHFLHCLPAHREEEVTGEIIDGPQSIVFEQAGNRLHAQKALLVSLFKN
>SwissProt_Q81M99 Ornithine carbamoyltransferase; OTCase; EC 2.1.3.3 from Bacillus anthracis
MSTVQVPKLNTKDLLTLEELTQEEIISLIEFAIYLKKNKQEPLLQGKILGLIFDKHSTRTRVSFEAGMVQLGGHGMFLNG
KEMQMGRGETVSDTAKVLSHYIDGIMIRTFSHADVEELAKESSIPVINGLTDDHHPCQALADLMTIYEETNTFKGIKLAY
VGDGNNVCHSLLLASAKVGMHMTVATPVGYKPNEEIVKKALAIAKETGAEIEILHNPELAVNEADFIYTDVWMSMGQEGE
EEKYTLFQPYQINKELVKHAKQTYHFLHCLPAHREEEVTGEIIDGPQSIVFEQAGNRLHAQKALLVSLFKNVEELS