ids
stringlengths 6
10
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stringlengths 11
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stringlengths 108
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P38025 | MAQCVRSTLNPVRTPQSFTRKAYVKSPAFASVSFLRAVPEFNKYPKPCSLVMSCQGKAQNQQEERPQLSLDDLVTSNRKGEVLGTIKDSLSNCLSETNLLATVPGLKSRIKGKVRDIYDAGDYLVLITTDRLSAFDRNLASIPFKGQVLNETSLWWFNNTQHITPNAIVSSPDRNVVIAKKCSVFPIEFVVRGYVTGSTDTSLWTVYNKGVRNYCGNELSDGLVKNQKLPANILTPTTKAADHDVPISPNEIVEGGFMTQAEFDEASMKALSLFEFGQGVAKKHGLILVDTKYEFGRSSDGSILLIDEIHTPDSSRYWLAGSYEERFQKGLEPENVDKEFLRLWFKENCNPYEDEVLPAAPAELVTELAWRYIFLYETITGSRIDIIPTQEPIHDRISRNTSQALSSLRQL | Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 46063
Sequence Length: 411
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
Subcellular Location: Plastid
EC: 6.3.2.6
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O28996 | MGSVKDLVVLKEPAEKPGLGRFIFSNRYSVFDYGEMPDKIEDKGRALCMVTAYFFEKLEEAGIATHYLGLVEGGKVRRFDEVENAVNEMEVKLVRVIKPKNGDYSIFKTLKGNFLVPLEIIYRNSIPEGSSLLRRIERGEAKPEDFGLTKIEAGMRLERPIVDFSTKLEDVDRYLSHSEAKEISGLSDEEFEALKELVVKVDEIITREVSKAGLINEDGKIEVALDDERNLMVVDAVGTPDECRFSFDGFEVSKELLREYYRKTEWYDKVRQLKGQEGWREAVGLPPPLPDEVREGVSNLYRAFCNEVTGRKFFDAPKLKEVVSQLKEVLE | Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 37780
Sequence Length: 331
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
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Q5P7J7 | MAQPLFESTIKSLPLLGRGKVRDIYAVDADKLLIVTSDRLSAFDVILPDPIPDKGRVLTAMAAFWFARLGHIVPNQLTGIDPESVVASDERDQVRGRSLVVKRLKPLPIEAVVRGYVIGSGWKDYQDTGAICGIRLPAGLAQAAKLPSPIFTPASKADVGDHDENISFAAAQTRCAAELTGLLAGSGTNGARLATEARDAAITLYVEAANYAAGRGIIIADTKFEFGIDSAGTLHLIDEALTPDSSRFWPADSYREGISPPSYDKQYVRDYLETLTWGKKAPGPHLPADVIAKTAAKYREAFERLTGQSLA | Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 33436
Sequence Length: 311
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
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Q8REV1 | MEKGKFIYEGKAKQLYETDDKDLVIVHYKDDATAGNGAKKGTIHNKGIMNNEITALIFNMLEEHGIKTHFVKKLNDRDQLCQRVKIFPLEVIVRNIIAGSMAKRVGIKEGTKISNTIFEICYKNDEYGDPLINDHHAVAMGLATYDELKEIYDITGKINNLLKEKFDNIGITLVDFKIEFGKNSKGEILLADEITPDTCRLWDKKTGEKLDKDRFRRDLGNIEEAYIEVVKRLTEKK | Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 27141
Sequence Length: 237
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
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Q74BF0 | MAELVLKTDFPDLKLAGRGKVRDIYDLGDALLIVTTDRISAFDVIMNEAIPDKGYVLTQISSFWFRQMEDIIPNHIISTDVKDFPAECQKYAAQLEGRSMLVKKAKPLPVECIVRGYISGSGWKDYKATGAICGITLPAGLVESDKLEEPIFTPSTKAELGEHDENISFDKCVELIGRELAEKIRDVTIAIYKRARDIADTKGIIIADTKFEYGIYNGELIIIDECMTPDSSRFWPKDSYKPGGAQPSFDKQFLRDYLETLDWGKTAPAPPLPEEIVRKTGEKYMEALVRLTGKGK | Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 33138
Sequence Length: 296
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
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Q7NJB6 | MILQPGAWAVADILYEGKAKIIYPTPDPAIVLAVFKDDATAFNAQKRGTISGKGAVNATVSAKLFLLLERSGVPTHYIDQPAANQLLFRRLKMIPLEVVVRNIVAGSLAKRTGLASGTVLGEAIVEFYYKNDALGDPLLNDEHILKVLTTVDALQLAELRRSALQVNAILSAFYRECGIRLVDFKLEYGYDGAGQLQLGDELSPDNCRLWTLEEDRILDKDRFRFDMGEVEGAYQEVLARVIAKAGP | Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 27165
Sequence Length: 247
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
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P43851 | MTQQLPILSLKKIYSGKVRDLYEIDDKRMLMVTSDRLSAFDVILDDPIPRKGEILTQISNFWFNKLAHIMPNHFTGDSVYDVLPKEEADLIRDRAVVCKRLNPIKIESIVRGYLTGSGLKDYKQTGTICGLKLPEGLVEASKLPEAIFTPSSKEEVGNHDINISYAECEKLIGADLAAQVKEKAIALYTVAAEYALTKGIIICDTKFEFGLDENGTLTLMDEVLTPDSSRFWSVDTYQAGTNPPSFDKQFVRDWLENSGWNKQAPAPKVPENIIQKTVDKYQEALDLLTK | Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 32581
Sequence Length: 290
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
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Q82FV6 | MSGFVEKPEPLQVPGLVHLHTGKVRDLYQNEAGDLVMVASDRLSAFDWVLPTEIPDKGRVLTQLSLWWFDRLVDLAPNHVLSTELPPGAPADWQGRTLICKSLKMEPVECVARGYLTGSGLVEYNETRTVCGLALPEGLVDGSELPGPIFTPATKAAVGEHDENVSYEEVARQVGAETAAKLRQTTLAVYARARDIARRRGIILADTKFEFGFDGDTLVLADEVLTPDSSRFWPADQWEPGRAQPSFDKQFVRDWLTSPESGWDRKSEQPPPPLPQHVVDATRAKYVEAYERLTGANWS | Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 33180
Sequence Length: 299
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
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Q9RKL1 | MSGFVEKPEPIQVPGLVHLHTGKVRELYRNEAGDLVMVASDRISAYDWVLPTEIPDKGRVLTQLSLWWFDQLADLAPNHVLSTELPPGAPADWEGRALVCKSLRMVPVECVARGYLTGSGLAEYDETRTVCGLALPEGLVDGSELPAPIFTPATKAEVGEHDENVSYEEVARQVGADTAAALRQATLAVYSRARDIARERGIVLADTKFEFGFDGDDLVLADEVLTPDSSRFWPADRWQPGRAQPSYDKQFVRDWLTSAESGWDRKSEQPPPPLPQQVVDATRAKYVEAYELLTGQSWS | Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 33065
Sequence Length: 299
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
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O67775 | MRAIISVYRKEGIDKLAKALQELGYEIVSTGGTAKYLREKGISVKEVSEITGFPEILEGRVKTLHPVVHGGILFRDWVEKDKEEIEKHGIKPIDVVVVNLYPFEEKLKEGLTDKDLMEFIDIGGPTLIRAAAKNFFRVVILVDPEDYDWVIEKLKKGNLTLQDRAYLAWKAFSHTAYYDGVISQAFKKLYSIDTFGKEEALPLKRMQKLRYGENPHQRGFLYENPLEDIGITKAQVLQGKEMSFNNYLDADSAVRLVAEFPNQTVCAIIKHNNPCGVALGSSVKEAFLRAKEADPVSAFGGIVAFNDKVDGETAKELTSMFLEVVIAPDYDEEALRELSRKKNLRVIRFFGFQHAFDVKKVSGGYLLQDEDTVLYEKLQVVTKREPTAEEMEDLLFAWKVVKHTKSNAVVIAKNGQTLGIGSGNVSRVDSLKCAINKAKEFGFDLKGAVVASEAFFPFRDSIDIMAKEGITAVIQPGGSIRDQEVIDACNEHGIAMIFTGLRHFKH | Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 56677
Sequence Length: 506
Domain: The IMP cyclohydrolase activity resides in the N-terminal region.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.
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Q81IP9 | MKKRALVSVSDKTGVVEFVKGLLEQGIEVISTGGTKKLLEENGLQVIGISEVTGFPEIMDGRVKTLHPNIHGGLLAVRDNETHVTQMNELGMEPIDFVVVNLYPFKETIAKPDVTFADAIENIDIGGPTMIRSAAKNHKFVSVIVDPVDYDIVLAELKENGEVAEETKRKLAAKVFRHTAAYDALISNYLTEQMGEESPETLTVTFEKKQDLRYGENPHQKATFYKAPFAATSSVAYAEQLHGKELSYNNINDADAALSIVKEFTEPAVVAVKHMNPCGVGVGTDIHEAYTRAYEADPVSIFGGIIAANREIDKATAEKLHEIFLEIVIAPSFSQEALEVLQSKKNLRLLTINIEKATSASKKLTSVQGGLLVQEEDTLSLDESTISIPTKREPSEQEWKDLKLAWKVVKHVKSNAIVLAKDDMTIGVGAGQMNRVGSAKIAITQAGEKAQGSALASDAFFPMPDTLEEAAKAGITAIIQPGGSIRDEDSIKVADTYGIAMVFTGVRHFKH | Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 55574
Sequence Length: 511
Domain: The IMP cyclohydrolase activity resides in the N-terminal region.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.
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Q8X611 | MQQRRPVRRALLSVSDKAGIVEFAQALSARGVELLSTGGTARLLAEKGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRRGQDDAIMEEHQIQPIDMVVVNLYPFAQTVAREGCSLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYDAIIKEMDDNEGSLTLATRFDLAIKAFEHTAAYDSMIANYFGSMVPAYHGESKEAAGRFPRTLNLNFIKKQDMRYGENSHQQAAFYIEENVKEASVATATQVQGKALSYNNIADTDAALECVKEFAEPACVIVKHANPCGVAIGNSILDAYDRAYKTDPTSAFGGIIAFNRELDAETAQAIISRQFVEVIIAPSASEEALKITAAKQNVRVLTCGQWGERVPGLDFKRVNGGLLVQDRDLGMVGAEELRVVTKRQPTEQELRDALFCWKVAKFVKSNAIVYAKNNMTIGIGAGQMSRVYSAKIAGIKAADEGLEVKGSSMASDAFFPFRDGIDAAAAAGVTCVIQPGGSIRDDEVIAAADEHGIAMLFTDMRHFRH | Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 57358
Sequence Length: 529
Domain: The IMP cyclohydrolase activity resides in the N-terminal region.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.
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B2KCF7 | MTQERKIKRALISVSDKTGLEVFAKGLHKLGVELVSTSGTAKFLKAAGLPVRDLSDLTGFPEILDGRVKTLHPRVHGAILYKRDDDAHCKVIKDMGIEDIDMLVVNLYPFRETAAKAKHSFDAEVIENIDIGGPSMLRSAAKNFAHVAVLCRPKDYEVVLSEMAASQGALSYATRQRLCVEAFTHTAEYDAAISEEFKKGLNHEFPESKIVVLHKTQDLRYGENPHQKAVLYSQKKDFSFEQLHGKELSYNNILDAFGTWDAVCDFDLPACVIFKHVTPCGIGTGKVLTEAFNNAWACDPKSAFGGIIALNKPMQRDIAEAISKVFIEAVCAPDYDLESLEILKQKKNIRILKRNSPLSAAYQLKSVGDEVLLQQPDRTLLLDNKWDCVTKRKPTEEEDKALKFAWASVKHVKSNAVILTSESASVGIGAGQMSRVDSVKMAGMKFEEYLQENKKPKVLVIGSDAFFPFRDGVDAAAKLGVSAIVQPGGSVRDEEAIAAADEHGIAMIFTGLRHFRH | Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 57049
Sequence Length: 517
Domain: The IMP cyclohydrolase activity resides in the N-terminal region.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.
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O74928 | MYALLSVYDKTGLLELAKALTSKGVKLLGSGGTAKMIRESGMEVADVSSITNAPEILGGRVKTLHPAVHGGILARDIPSDEKDLVEQSIEKIDIVVCNLYPFRETIAKPNVTIPEAVEEIDIGGVTLLRAAAKNHARVTILSDPADYATFTDKFLSDKLTQDDRNTYALKAFASTASYDAAITDYFRKQYAAGVDQLTLRYGANPHQSPAQAFMEQGPLPFKVLCGSPGYINLMDALNSWPLVKELRENIGIPAAASFKHVSPAGAAVGLPLSDVEKKVYFVSDITEFTPLACAYARARGADRMSSFGDFIALSDTVDVCTARIISREVSDGVIAPGYEPEALELLKKKKGGKYCVLQMDPKYVPAEIETRQVYGISLQQHRNHAKIDFSLFEKVVSKNKDLPKSALIDLVIATTALKYTQSNSVCYAKNGMVVGLGAGQQSRIHCNRLAGDKADNWWLRHHPKVLGMQFKKSAKRPEKSNAIDLYVLDAVPAEGSEREQWESAFETIPEPLTKKEREEFLATCKDVVCASDAFFPFPDNIYRLAQSGVKYVAAPGGSVMDQAVRDTANEFNMVFSEIPLRLFHH | Function: Bifunctional enzyme that catalyzes the last two steps of purine biosynthesis. Acts as a transformylase that incorporates a formyl group to the AMP analog AICAR (5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) to produce the intermediate formyl-AICAR (FAICAR). Also catalyzes the cyclization of FAICAR to IMP.
Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 64123
Sequence Length: 585
Domain: The IMP cyclohydrolase activity resides in the N-terminal region.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.
Subcellular Location: Cytoplasm
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Q8EJM1 | MTVANHARPIRRALLSVSDKTGILEFAKALHAQGVELLSTGGTARLLADNGVPVIEVSDYTGHPEIMDGRVKTLHPKVHGGILARRGLDENVMAANNINAIDLVAVNLYPFADTVAKAGCTLEDAIENIDIGGPTMVRAAAKNHKDVTIVVNAADYNRVLAEMAVNNGSTTHATRFDLAIAAFEHTAGYDGMIANYFGTMVPMHRVPAHSTDECFQDSLSVEGSKFPRTFNTQLVKKQDLRYGENSHQAAAFYVDTKIDEASVATAVQLQGKALSYNNIADTDAALECVKEFSEPACVIVKHANPCGVALGKDLLDAYNRAYQTDPTSAFGGIIAFNGELDAATASAIVERQFVEVIIAPVVSQGARDVVAKKTNVRLLECGQWNTKTQTLDYKRVNGGLLVQDRDQGMVGLDDIKVVTKRQPTESELKDLMFCWKVAKFVKSNAIVYAKDGMTIGVGAGQMSRVYSAKIAGIKAADEGLEVVNSVMASDAFFPFRDGIDAAAAAGISCIIQPGGSMRDAEIIAAADEHGMAMVMTGMRHFRH | Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 58221
Sequence Length: 543
Domain: The IMP cyclohydrolase activity resides in the N-terminal region.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.
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Q3IIQ6 | MPSIVVVGANWGDEGKGRIVDFLAENASASIRFQGGNNAGHTVVNDFGTFKLHQLPSGIFNPDCIAVLGPGMVISPSALSEEIAEVKAAGVNVKLCISDRATLCLPLHALEDTLEELRLGDAAYGSTRQGISPAYGDRVMKKGILVGWLNQPDVLLERIQFMLDWKMPQLKALYPSCDFSQTAEEMTQWLLDVTAPWRAFICNVTEPLKALQKQNANLLFEAQLGAGRDLVYGEYPYTTSSNVTAAYAGIGSGLPALRPERVVAVAKSFSSSVGTGTLVTAMEEQDNFRESANEYGAVTGRPRDMGYFDAVATRNGVELQAATEIALTKIDCLSGMKDLKICVAYDGDHSENPIWPQTAALSPVYENMQPWDEDITGCRTFDSLPIAAQQYVERIEALMGVPITMVSVGPEREQMIIR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 45407
Sequence Length: 418
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
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A3DK09 | MATRVVVGTQWGDEGKGKYIDMLAKDSDMVVRFSGGNNAGHTIVANGVKYALHLIPSGILNEGKTCIIGNGVVVDPAVLLKEIKELNEKGISTDRLLISDRAHVIMPYHKLLDELQEKFRGENSIGTTKRGIGPCYSDKTERSGIRMCDLVDEDEFVRKVRENLKVKNLIIEKVYGGQKLDEEQVISEYLEYGRKLKEYVADVNSIIFEAIEQGKNILFEGAQATFLDLDFGTYPYVTSSNPVAGGVCTGAGVGPVFINEVYGVLKAYTSRVGAGPFPTEQNNEIGDRIRELGWEYGTTTGRPRRCGWLDLVMIKYAARVNGLTALAINHVDTIGKLPKIKLCVAYKKNGQETRNFPCSLKELAQCEPVYEEFDGWDEDISNVKSFDDLPDNAKKYLSRIEEIVGVKIKLIGVGKEREQTIVVN | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 47041
Sequence Length: 424
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
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Q6AN65 | MSSVVVVGAQWGDEGKGKIVDLLTKYSDYIVRFQGGNNAGHTLVVDGKKFVFHIIPSGILYEEKTCMIGNGVILDPGVLLEEMASLKERGLEVKPNRLMISDNAHLIMPYHSQLDQAKESALSASNKIGTTGRGIGPCYMDKVGRVGIKAGDLLDEDLFREKLRCAIEEKNFILTKKFGAPAVDFDSVYRQFMDFAEQLSPYFGNVSVTLDEARRADKNILFEGAQGTQLDIDHGTYPFVTSSNTVAGNACAGSGFGPSHIDAVVGIVKAYTTRVGSGPFPTELFDEKGEELQNKGSEFGATTGRRRRCGWFDGVVANDAVRLNGLTGWALTKLDVLSGQKSIKMASSYDLNGKKLHAMPNNIKDAEALKPVYEEVPGWADEVDGICNYDDLPTEAKDYVRRIEDFTGVPANIVSVGPDRAQTMMLSNPFETKKCCK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 47678
Sequence Length: 437
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
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A4J9P7 | MSTVVIIGAQWGDEGKGKITDFLAEKAEIIVRYQGGNNAGHTVVVDDAEFKLHLIPSGILHPEKLCVIGNGVVIDPQVLKQELDSLAERGVKTGRLCVSQRSHIIMPYHRKMDAVEEEQKGEGKIGTTKRGIGPTYTDKASRVGIRVVDLIDKEEFPKLLKNNIECKNEIFEKLYNTKGFEYEEVLKEYQGYAEMLEPMTEDVSVLVHNAIKEGKNVLFEGAQGTLLDLDHGTYPYVTSSHPTAAAACLGSGVGPTKINRALGIVKAYTTRVGEGPFPTELNDGLGEEIRKNGNEYGTTTGRPRRCGWFDAVIVRYAARISGLDSLAITKLDVLSGLPVIKLCSGYRYKGEIIREFPASLKELAKCEPVYEDFPGWSEDISNVTRYEDLPENAKRYLERIVELTEVKISLISVGVKRSQTIILEDLFN | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 47424
Sequence Length: 428
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
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A1V9U1 | MSNVVVMGAQWGDEGKGKIVDLLTRESDVIVRFQGGNNAGHTVLVGEKQYILHLIPSGILHEGKKCLIGNGVVLDPEVFCREIDSLRAQGVDMSPARLMISRKTHLIMPYHKVLDQAREAHKCKDAKIGTTGRGIGPCYEDKSARIGVRAADLAMPELLRSKIEAALVEKNALFTGLYGQQPLDADAVFEEVMAHGAKLVPYLADVSSEIHDAWAEGRSVLFEGAQGTHLDIDHGTYPFVTSSNTVSGNAAAGSGVPPTKLDRIIAIVKAYTTRVGAGPFPTELDDATGEYLQQKGHEFGATTGRKRRCGWLDAVVLRESVRLNGPTDIALTKLDVLSGLKEISICTAYTYRGEQVAYPPQEQNGMAHVTPVYETMPGWDDDITGCTTWESLPAPVKAYVLRIEEITGVRISLVSVGPERDQTIRR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 46287
Sequence Length: 426
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
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P21900 | MASIIIGSQWGDEGKGKLVDILSQQFDVVARCQGGANAGHTIVVDGKKIALHLIPSGILNEKASCILGNGMVIHLPTFFKEVQGLQDKGINYKGRLFVSDRAHLVFDLHQMIDAMKEAELSNGTSNDSIGTTKRGIGPCYSSKASRGGLRVCDLYSPEHFRKTFTRLVENKHKRFGSFEYDVEAELKRYQEFAEMLKPFVIDSVYYLNQAFKDGKKVLIEGAQSTMLDLDFGCYPYVTSSASSVGGACTGLGISPNKVVTQIGVVKAYTTKVGSGPFPTEQNDHVGDSLRKAGSEFGTTTGRPRRIGWLDAVVLRYTSMINDFTRLNLTKLDVLSDFEEIKIGVDYKYKGETIKSFPASLETLAQCEVVYESFPGWKCDLSHVTEYDQLPIQAKNYIKRIEELVGVPIVYIGVGVERKNLIERKELI | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 47285
Sequence Length: 427
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
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Q9Y0Y2 | MSASATNGTHYEQLHQGRTKMYKSKVDVVLGAQWGDEGKGKVVDMLASDVDIVCRCQGGNNAGHTVVANGTEFDFHLLPSGVVNEKCVSVIGNGVVIHLPSLFDEVLKNEAKGLQHLENRLIISDRAHLVFDFHQHVDGMQEAEKGGKSLGTTKKGIGPAYSSKATRNGIRVGELLGDFNLFSEKFKSIVATHVRLFPSINVDVEAELARYKDYADKVRPYVKDTICFLHTALRNGKTILVEGANAAMLDIDFGTYPYVTSSNCSIGGVLTGLGLPPQTIGEVIGVVKAYTTRVGDGPFPTEQLNDIGDLLQTRGFEVGVTTKRKRRCGWLDIPLLKYTSLVNGYTCICLTKLDILDTLPEIKVAVAYKKPNGEKLDHFPGTIAELGNIEVEYAVLPGWQTSTEEVRNFKELPENAQSYVRLLESELSVPVRWVGVGKGRESIINVH | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity). Plays a role in the regulation of adult life span.
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 48901
Sequence Length: 447
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
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Q6F243 | MREINSLVVVGSQWGDEGKGKMTDYFAQKADVVVRFAGGDNAGHVINFNGQKHKVTIIPSGIFNSEVTSVIGNGCAVNLINLVKELETIKNSGVKLGKLLISDRAQLILPYHILIDGAQEESRGARKIGTTKRGIGPTYQDKAARLGIRVADIEEEDFKETFKEIFEYQMMFLDRMFNVESIDFEETYANLINAYNVIKDCVTDTGIFVEQAIKNGKKVLFEGAQGALLDIDHGTYPYVTSSNTSANNASTGTGISHKLINNTLGVVKAYSTRVGAGAFPTELLNEVGDGIRERGHEYGSNTKRPRRVGWLDLVALKHAIRTSGIDYLFITLLDVLSGVEELLICDKYILNGEEINYIPATSSKHEKCKANYISMPGWKEDITKVKHFEELPLNAKNYLNKIAEICEVEISGFSVGPDRLQTVITKEIM | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 47438
Sequence Length: 429
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
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Q9U8D3 | MNIFDHQIKNVDKGNVVAILGAQWGDEGKGKIIDMLSEYSDITCRFNGGANAGHTISVNDKKYALHLLPCGVLYDNNISVLGNGMVIHVKSLMEEIESVGGKLLDRLYLSNKAHILFDIHQIIDSIQETKKLKEGKQIGTTKRGIGPCYSTKASRIGIRLGTLKNFENFKNMYSKLIDHLMDLYNITEYDKEKELNLFYNYHIKLRDRIVDVISFMNTNLENNKKVLIEGANAAMLDIDFGTYPYVTSSCTTVGGVFSGLGIHHKKLNLVVGVVKSYLTRVGCGPFLTELNNDVGQYLREKGHEYGTTTKRPRRCGWLDIPMLLYVKCINSIDMINLTKLDVLSGLEEILLCVNFKNKKTGELLEKGCYPVEEEISEEYEPVYEKFSGWKEDISTCNEFDELPENAKKYILAIEKYLKTPIVWIGVGPNRKNMIVKKNFNLN | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the salvage pathway for purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 50065
Sequence Length: 442
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
|
B2AWF0 | MPTTIILGSQWGDEGKGKLSDILCQKAQICARAAGGHNAGHSVVANGVSYDFHLLPSGLINPNCENLIGSGVVVNVEAFFKELNALEEKGLKHVREKILISDRAHVNLTLHAAVDRAEEAQLEGNKKIGTTGRGIGPSYATKASRKGIRVHEIFKEAVFEKKLRTLAEGYKKQFGELFEYDVEEEIARFREYRKLLPNFVCDGPNFIDQAQKSGRDLLIEGANALMLDIDYGTYPYVTSSNTGFGGAVTGLALDYKQIKEVIGVVKAYTTRVGGGPFKTEDLGDAGTKLQEIGREWGVSTGRRRRCGWLDLVVLKYSQLINNYTSWNLTKLDILDTFPTIKVAVAYKDKETGEVIEHFPADLDYLDTLEVVYKEFEGWQTPITSVKTFDALPAQAQAYVKFIEEFTGIPVKWIGTGPARDDMIYL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 47085
Sequence Length: 425
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
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B9IJ21 | MNLSSLRLESNPRWSYHAAHFPAHHGLNPSFRRNFVSCSSIKPSASSSLSVAESFTRDSASRIESLSQVSGVLGSQWGDEGKGKLVDILAEHFDIVARCQGGANAGHTIYNSEGKKFALHLVPSGILNEDTLCVIGNGVVVHLPGLFKEIDGLEANGVSCTGRILVSDRAHLLFDFHQEVDGLREAELAKSFIGTTRRGIGPCYSSKVIRNGIRVCDLRHMDTFPQKLDALLSDVASRFESFKYGPEMLKEEVERYKRFAERLEPFITDTVHFMNESIAKKKKILVEGGQATMLDIDFGTYPFVTSSSPSAGGICTGLGIAPRVVGDLIGVVKAYTSRVGSGPFPTEILGQGGDLLRFAGQEFGTTTGRPRRCGWLDVVALKYVCQINGFSSLNLTKLDVLSEFSEIQIGVSYKQIDGTPVESFPGDLCLLEQLKVDYEVLPGWKSDISSIRKYADLPKAAQQYVERIEELVGVPIHYIGIGPGRDALIYK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 53698
Sequence Length: 491
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Plastid
EC: 6.3.4.4
|
Q7MWW8 | MEKVDVLLGLQWGDEGKGKIVDVLTPHYDIVARFQGGPNAGHTLEFNGEKYVLRSIPSGIFQGEKTNVIGNGVVLDPLLFKEEAEALARSGHDLTKRLVISRKAHLIMPTHRLLDAANEMAKGSGKIGTTGKGIGPTYTDKVSRNGLRVGDLEHGFEEAYSVAKERHLRILNSLNYPTDKLADLEERWMEATKYLRKFEFVDSEFLINGALLSGKKVLAEGAQGSLLDIDFGSYPFVTSSNTICAGCCTGLGVAPRNVGDVYGIFKAYCTRVGAGPFPTELFDETGDKLCELGREFGSVTGRKRRCGWIDLVALRYTIMLNGVTKLIMMKSDVMDLFPTIKACVAYEIDGKETRNFPFHLTEGVTPVYKELPGWQQSMTNVVSEADFPKEFSDYIAFLEKELGVGIAIVSVGPDREQTIIRQA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 46574
Sequence Length: 423
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
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Q386E7 | MAAAPSATAPKHNYTLGTNASQLELYKYLKTVPPIPELRQAVTIKKYEEASVDDTLYPLIDEHQIIMVVGAFFGDEGKGKTVDAVARHPACTCVARVNSGENAGHTVFDDIGRKYVFNLAPSSLLTPNTRNYVSSECVMDPISFMEREIGQFIKSNMPYKDKLFVGNVFVVTPYHKLLDLLGSAPNSSTLKGMSPIHASKVTKRGIRLDHIFNDEGVLRARLAKDMDTYYGLLKVKGLTDKDVVRRCQEENADGVERVPGYVVDFARAENKIDYLVKLYTERVKNNKDFPRRCDVTHELRAALARGEKLLLEGPQSYWLSNAREKFWESTTSADTTAGGLLASAQFNFQRYKVLVINVHKAPGSSRVGIGANPSSFVPQDYYSAQDIKTLEALPKGGCVDFDKIQNFFYTKAFNTESKTFNGIYEPLEYEDATGKYNIGVAMSIASARHHGECGAVTKKPRVCGFFDCVLHFEVNAVQGPYLSISAVDRGDDYDRIGITIAYVYYDVGNKMVDANGRVYKNGDIIKAGDPVPCEMALYHCYPIVKVINGWKGAPIAASKRRPNEPLPKGVCEFIANVEFFTGAKVISIGNGPRGSDIIYLKQ | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the salvage pathway for purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 66675
Sequence Length: 602
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
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Q4P7R2 | MAAMPKPSDSKTGGKATVLLGSQWGDEGKGKLADVLSGQMDVCARCAGGNNAGHTIVADVNGVKTKFDFHLLPSGLVNPRCAGFIGSGVVVHVPSFFAELDTIQKKGLNCDGRLFISDRAHLVFDFHQVVDGLKEVELGGSSIGTTKKGIGPAYSSKASRSGLRVHHLYDPELFATKFRKLVEGRFKRYGHFEYDTEGEIARYRAFAERLRPHIVDGVTFIHTALAQNRKVLVEGANALFLDIDFGTYPFVTSSSTSIGGVLTGLGIPPTAIGDVIGVMKAYTTRVGMGPFPTELHEEIGHHLQEVGAEYGVTTGRRRRCGWLDLVMMRYSCLINGYTSLNLTKLDVLDQLKEIKICVGYVVDGKELPSFPADLEVLAKVEVQYKTLPGWQQDISKTTTWEELPENCRNYVDFIEQFLGVKIEWIGVGPARESMIHRAG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 48040
Sequence Length: 439
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
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A7TID0 | MVNVVLGSQWGDEGKGKLVDLLVGKYDIVARCAGGNNAGHTIVVNGIKYDFHMLPSGLVNPNCSNLLGNGVVIHVPSLFSELNNLSEKGLKDCDKRLFISSRAHIVFDFHQHTDKLRELELKGISKDGKNIGTTGKGIGPTYSTKASRSGLRVHHLVNDQPGAWEEFEAKYRRLLKTRRERYGDFEYDPEEELNRYKKYKELLKPMVVDSVFFINNAIANGKKILVEGANALMLDIDFGTYPFVTSSSTGIGGVITGLGVSPRHINEVYGVVKAYTTRVGEGPFPTEQLNEQGEKLQTIGAEFGVTTGRKRRCGWLDLVVLKYSAMINGYTSLNITKLDVLDTFKEIPVGVSYSINGKKLDSFPEDLINLGNVDVEYVTLPGWDQDITKITEFDQLPENAKKYLKFIEDFVGIPIEWVGTGPARESMLHRDV | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 48009
Sequence Length: 432
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
|
P40607 | MGNNVVVLGTQWGDEGKGKIVDLLTEDAKYVVRYQGGHNAGHTLVIDGEKTVLHLIPSGILRDNVKCVIGNGVVLSPEALLKEMKPLEERGIPVRERLFISEACPLILPYHVAMDQAREIARGKKAIGTTGRGIGPAYEDKVARRGLRVGDLFDMEAFAEKLKEVMEYHNFQLVNFYKAEPVSYEAVLEEAKGYAELLTSMVIDVTDELDAARKRGDKIMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVAAGSGFGPRHIGYILGIAKAYCTRVGAGPFPTELYDGLEKQDPVGKHLGTVGHEFGATTGRLRRTGWFDAVAMRRAIQINSVSGFCLTKLDVLDGLEELKICTGYKMEDGSVLEVSPMAAEAFEKATPIYETMPGWSENTFGAKSLDALPQAALNYIKRIEELTGVPVDIISTGPDRNETIIKVHPFEA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 47694
Sequence Length: 438
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
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O24396 | AAAAAGRGRSFSPAAPAPSSVRLPGRQAPAPAAASALAVEADPAADRVSSLSQVSGVLGSQWGDEGKGKLVDVLAPRFDIVARCQGGANAGHTIYNSEGKKFALHLVPSGILHEGTLCVVGNGAVIHVPGFFGEIDGLQSNGVSCDGRILVSDRAHLLFDLHQTVDGLREAELANSFIGTTKRGIGPCYSSKVTRNGLRVCDLRHMDTFGDKLDVLFEDAAARFEGFKYSKGMLKEEVERYKRFAERLEPFIADTVHVLNESIRQKKKILVEGGQATMLDIDFGTYPFVTSSSPSAGGICTGLGIAPRVIGDLIGVVKAYTTRVGSGPFPTELLGEEGDVLRKAGMEFGTTTGRPRRCGWLDIVALKYCCDINGFSSLNLTKLDVLSGLPEIKLGVSYNQMDGEKLQSFPGDLDTLEQVQVNYEVLPGWDSDISSVRSYSELPQAARRYVERIEELAGVPVHYIGVGPGRDALIYK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 50918
Sequence Length: 476
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Plastid
EC: 6.3.4.4
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Q8D322 | MKKNIIVLGAQWGDEGKGKVIDFLSKNINYVVRCQGGNNAGHTVVIKEEKTVLHLLPSSILNKNTINIISSGVVISPIDLVKEINMIEKKGISIKNRILISELCPLVLKYHVSMDVAREKNRKKKEIDSIGTTHRGIGPAYEDKIARRALRIHHLINKDKFKKKLKNIVEYYNFQLINYYKEQPVNHEKIFNELINKSKLLNNISIDIPSYLNSINKKNKSIIFEGAQGALLDIDYGTYPYVTSSNTTVGGIISSTGISPFSIKYILGIIKAYSTRVGNGPFPTEIFDETKNIILEKGKEFGSTTGRKRRIGWFDAVAVKRVIQINSFSGFCLTKIDVLDNIKEIKICTSYILPNGKILDNISNIDDWNKAKPIYKSMPGWLSKTKGVKNFKNLPILAKNYIKKLQSIIKIPIEIISTGSDRNDIIVLNKKLVE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 48918
Sequence Length: 434
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
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Q2J4M9 | MTGNPAAPAATSVSPPAEQPYQELGLTDDEYARIIATLGRRPSDAELAMYSVMWSEHCSYKSSKVHLRQFRDTPLTDRLLVGMGENAGVVDVGEGLAVTFKIESHNHPSFVEPYQGAATGVGGIVRDILTMGARPIGVLDPLRFGEADAADTARVLPGVVAGIGGYGNCLGLPTIGGEVVFDPTYAGNPLVNALCVGVMPVDRVQTSAATGVGNAVVLLGAKTGRDGIGGVSILASATFDEGGGPARRPSVQVGDPFTEKILIETCLELFDRKLVTGIQDLGGAGLTCALTETTAAGIATGQPGGMEVDLDLVPLREASMAAHEVLASESQERMLAIVTPEALPEVLALAERWGVLATRIGTVTNSGRLTVRWHGEVVVDVPPGSLADDGPVYERPLRRPVDFDLVRADAPTPARLARPRTGPELRETLLRLVASPNLCSRAWVTDQYDRYVQAGTVLAQPEDAGVLRLSAATGLGIALATDGNGRYARLDPFAGTQLALAEACRNVAAAGSVPIAVTNCLNFGSPEDPEVMWQFAQACAGLAEGCRRLGLPVTGGNVSFYNQTGSTPIHPTPVIGVLGLFDDVTRRTPIGFAEEGDVLILLGETADEFGGSEWAWVTHRHLGGEPPAVDFAREKLLGEILVAGSRDGMLTAAHDLSDGGLAQALVESCLRGGHGARIILPAGSDPFVELFSESAGRAVVAVPRAEELRFTDMCEVRGLPWRRVGVVDGDTLDVQDAFTVGLDELRAAHEGTLPALFGRLT | Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 79825
Sequence Length: 761
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.5.3
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Q7NIR9 | MTAPTESSPFSPADLARHRLSPQEYRRITELIGRHPNLNELGMFSVMWSEHCCYKNSRPLLKGFPTTGPRVLVGPGENAGVIDIGDGLRVAFKIESHNHPSAVEPFQGAATGVGGILRDIFTMGARPIASLNSLRFGPLEDARNRALFRGVVHGIGHYGNCVGVPTVGGEVYFDPTYSGNPLVNAMAIGVLETPEIVRSGAAGIGNPVLYVGSTTGRDGMGGASFASAELSDASQKDRPAVQVGDPFTEKSLIEACLEAFRTGAVVAAQDMGAAGLTCSSSEMAAKGGVGIEMDLDLVPVRETGMVPYEFLLSESQERMLFVAEKGREGELIALFERWGLHAVVVGRVIGEPLVRIFHSGKVVAELPARALTDDAPVYPRAVLPEPPAAILKLRAFDWHSLAEPTDYAEALLTLLDSPTIGSKSWVYRQYDHQVQNNTVIVPGAADAAVIRVRPQSFGPGEVEAVPFTERGIAATVDCNSRYVYLDPYRGAMLAVAEAARNLSCVGATPLAVTDNLNFGSPEKPEGYWQLAMACRGIADACLELMTPVTGGNVSLYNETQSDGRTTAIYPTPTIGMVGLVEDIHRTCSQNFKSPGDLVYLLGGGEPTLGGSEYLACLHGVAAGEPPVLDMALEIQVQSVCRLGIERGLFKSAHDVAEGGLAVALAECCITGNLGLDAVLGANHPRADVVCFGEMAAAIIVTIDPCDQVACELWLECSLAERWKLLGTVAAQSFDLRVENRDCRISTSCERLKTTFEQAIPRRMEHIPVTEAPQR | Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 82656
Sequence Length: 774
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.5.3
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A8ABX6 | MPLTEEELKLIEETLGRKPNQVELAMFEAQWSEHCSYKSSRKHLRKLKMDSPWVVKGGDAAVVDFGSVYVAFRIESHNHPSAVDPYNGAATGVGGIIRDILSSGAKPIALLDDLIFGDLDENLVKWHVKGVVKGISDYGNRVGVPTVGGETWFDPDFTRNPMVSVACVGVCPKDKLINGTPRPGDLIVIAGNYTGKDGLLGSSFASKNLEEGVEEEYAAIQVPDPLMEKLLIDSILEMRDERLLVFVKDLGGGGLATALSEVAASFGLGVEARLDALHLREPMEAWEIVVSESQERMMLVIRPEDLERAKKVLEKYDVPYSVIGKFTDTGRVVLYYNGEKVADLPAKFLAEGPELDRPYERPKWHLELELLPPLPEVDLGDAIRKVLSSPNVASKRWIYEQYDHEVQIRTVVKPGEGDAAVLRLLEDPPKGIAVATDSNPRYTFLDPLWGAADVFLEAYRNVVASGARPLAAVDQVDAGSPERPDRFWFFVRMIDGLAWVEREVDVPIVGGKVSFYNEDDVTGKQIKPTVMITMIGKVENVYNAKRARAEEGDLLVLVGETFPELGGSEFLWSVHKLVRGKPPVPRPSTEARVAERILKAIKVSGVTGVHDVSVGGLAAAVAELAKGFGATLELDKVKGPWKRPEEALFSESGARYLLAVKPEAAEEVLKVTGGTVVGKVGGGPLRVLLNGKEVASVDDFEDLLENGMTSRLV | Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 77918
Sequence Length: 713
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.5.3
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O51423 | MKTIEHELYYEFRIADDVKMIYTKKPFNLKLKELSNDNFNFVPRSKKIKYLKQLHTDIIYKVEDDFINFQEGDGLISSSLDVALVAYFADCLPIYFYDSVKKIIGLIHSGYKGSFNLIILKMLFMFEKMGSALKDLKIVFGPYNRSCCYEVSEIFLKEVSNKFSKDLLNASFVTRDGKIYFDNASFNLNLLSSFNLNIYNSKLCTYCLKNLYSYRRLRESQSYALIWRI | Function: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine. Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase activity.
Catalytic Activity: adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate
Sequence Mass (Da): 26948
Sequence Length: 229
EC: 2.4.2.1
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Q9PN78 | MGRSRKNFLSLLENDKVGIFCAFDKDYNVFRAKIHNENLFSHLGFKDIEKCVFMDQIHSHKVIIYDENLKNLSCDGLISKEKNIALCVLSADCLPLILYHESGIIAALHSGRKGSFENILKECVDQITMQNSHLDKNKFHLFILPGICAKNYEIDGEILEFAKKEFKEFVQDDKLDLKALVKFQAQNLGIENIKDCGICSFDDESFFSYRRDKTTKRFVSVVYLKD | Function: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine. Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase activity.
Catalytic Activity: adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate
Sequence Mass (Da): 26064
Sequence Length: 226
EC: 2.4.2.1
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P33664 | MNIKKVDKYSFLEFKDDKFSLYFSTAENGLNFNINTEEGNDNIRNLKDWFNVKDVGYLKQTHSDIILNYDSDKELLEGDALITDKDNTLVGVFTADCVPVLLYDKSKNVMAAVHSGWKGTSDMIVKKTIIKMKQEFLSTASDITVYIGPHNKACCYEFGEEALSEFEGSGIYDISEIYKDGKLDLEKCIVKQCKSENVNNIKCLNICTNCSKEYKMFSYRRDGKSAGRMFSFIIKK | Function: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine. Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase activity.
Catalytic Activity: adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate
Sequence Mass (Da): 26945
Sequence Length: 236
EC: 2.4.2.1
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P94338 | MDSLDPRNRPVRKVFTTRAGGVSQSPYASFNLGDHVGDDPQAVASNRNRLADIIGLSPDKVVYMEQIHSNTVTVIDEAPADGQAVEATDALVTTQRGLALAVLVADCVPVLLSDTDAGVIAAVHAGRMGARNGIVAKTIAKMEELGAKPSRIHALMGAAASGANYEVPEAMARDVEAKLPGSIARTTKGTTGLDIRAGLLRQMLSLGVQMIDSDPRCTIEDEDLFSYRREGTTGRQAGVVWLPKEA | Function: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine. Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase activity.
Catalytic Activity: adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate
Sequence Mass (Da): 26004
Sequence Length: 246
EC: 2.4.2.1
|
Q9RT03 | MTAPGLPLLRAPNLAVPHAFTTRAGGVSAGPYAGLNLDDRSDDPRPVAENRARLAAALGFAADDFARLNQVHGVQVVHAQAPGFWEGDALVTATPGVLLAIGTADCYPLLLADPEAGVIGAAHAGWKGTVGRIGQRTVEQMVNLGARPERIHAAVGPGICGEQYEVGEDVAAQFRAAGLGEWVLEREGRTHLDLAGANRALLEGAGVGDLWVSGRCSTEADFYSYRRDAGQTGRMWAVIGLPRREGQTGEARA | Function: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine. Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase activity.
Catalytic Activity: adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate
Sequence Mass (Da): 26492
Sequence Length: 253
EC: 2.4.2.1
|
P33644 | MSKLIVPQWPQPKGVAACSSTRIGGVSLPPYDSLNLGAHCGDNPDHVEENRKRLFAAGNLPSKPVWLEQVHGKDVLKLTGEPYASKRADASYSNTPGTVCAVMTADCLPVLFCNRAGTEVAAAHAGWRGLCAGVLEETVSCFADNPENILAWLGPAIGPRAFEVGGEVREAFMAVDAKASAAFIQHGDKYLADIYQLARQRLANVGVEQIFGGDRCTYTENETFFSYRRDKTTGRMASFIWLI | Function: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine . Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate . Also has adenosine deaminase activity . May also act as a polyphenol oxidase: able to oxidize syringaldazine and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) in vitro .
Catalytic Activity: adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate
Sequence Mass (Da): 26339
Sequence Length: 243
EC: 2.4.2.1
|
P84138 | MPDIFQQEARGWLRCGAPPFAGAVAGLTTKHGGESKGPFASLNMGLHVGDDRTDVVNNRRRLAEWLAFPLERWVCCEQVHGADIQKVTKSDRGNGAQDFATAVPGVDGLYTDEAGVLLALCFADCVPIYFVAPSAGLVGLAHAGWRGTAGGIAGHMVWLWQTREHIAPSDIYVAIGPAIGPCCYTVDDRVVDSLRPTLPPESPLPWRETSPGQYALDLKEANRLQLLAAGVPNSHIYVSERCTSCEEALFFSHRRDRGTTGRMLAFIGRREEWT | Cofactor: Binds 2 zinc ions . One zinc is catalytic and mediates binding to the substrate, while the second is probably structural .
Function: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine . Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate . Also has adenosine deaminase activity .
Catalytic Activity: adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate
Sequence Mass (Da): 29844
Sequence Length: 274
EC: 2.4.2.1
|
P44552 | MQAINPNWNVPKNIHAFTTTREGGVSLAPYLSFNLGDHVGDNKSAVKTNRTLLVEKFGLPQTPIFLTQTHSTRVIQLPYSGQNLEADAVYTNVPNQVCVVMTADCLPVLFTTTSGNEVAATHAGWRGLCDGVLEETVKYFQAKPEDIIAWFGPAIGPKAFQVGIDVVEKFVVVDEKAKLAFQPDAIEEGKYLSNLYQIATQRLNNLGITQIYGGNHCTFNEKEKFFSYRRDNQTGRMASVIWFE | Function: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine. Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase activity.
Catalytic Activity: adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate
Sequence Mass (Da): 27138
Sequence Length: 244
EC: 2.4.2.1
|
P67257 | MLASTRHIARGDTGNVSVRIRRVTTTRAGGVSAPPFDTFNLGDHVGDDPAAVAANRARLAAAIGLPGNRVVWMNQVHGDRVELVDQPRNTALDDTDGLVTATPRLALAVVTADCVPVLMADARAGIAAAVHAGRAGAQRGVVVRALEVMLSLGAQVRDISALLGPAVSGRNYEVPAAMADEVEAALPGSRTTTAAGTPGVDLRAGIACQLRDLGVESIDVDPRCTVADPTLFSHRRDAPTGRFASLVWME | Function: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine. Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase activity.
Catalytic Activity: adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate
Sequence Mass (Da): 25965
Sequence Length: 250
EC: 2.4.2.1
|
Q9CCE3 | MGGFADTGQVSVRIRWVITMRAGGVLVSPFDFLDLGDHVGDDPDCGGHLSRAWLVAAIGLGVDRVVWMSQVHGDRVKVVHEPCDAVVDNTDALVTRTSQPALPVVTIHCVPVLLSDARPGVTAAVHVGEGRGSARCASPCDGYDAGPGCVRWRRDIAVLLGPAVSGRNYEVPVVIADGVEAASPDSCTTTRISAGTPGLDLRTGIACQFRDLGVMSIEDDPRRTVADRALFSHLQTVSTGRLASLVWME | Function: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine. Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase activity.
Catalytic Activity: adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate
Sequence Mass (Da): 26305
Sequence Length: 249
EC: 2.4.2.1
|
P33663 | MNAWLTPDWPAPARVRACVTTRSGGVSQAPFDSLNLGAHVDDDPRAVEENRRRLTERLECRPSWLDQVHGVTVVEADPSRVLRADASWSAMPGVACTIMTADCLPALFCDRSGTRVAAAHAGWRGLAAGVLEATVDSLGVPGDELLVWLGPAIGPRAFEVGGEVRDAFVAAHAEARSAFVPSANPGRFMADIYRLARIRLGAHGVTAVHGGGFCTFSDTARFYSYRRSSRTGRFASLVWLQD | Function: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine. Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase activity.
Catalytic Activity: adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate
Sequence Mass (Da): 26047
Sequence Length: 242
EC: 2.4.2.1
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Q9ZD53 | MEVLIHKSVYYKIFDKTFNNSSHRYIQENHSINEAEILANIESITNYFKAQDILILNQVHSNQIVNADEHIVTIPEADGSITTKKNLVLTVQSADCVPVLLASDDGKIIGVAHAGWQGSINNIISNIVTKMIEKGAKNLIAVIGPAIAQSSYEVDDKYYKTFLSKDINNKRFFINSIKENHYMFDLPAFVELKLNESGVKDIKNITEDTYTNPSKYPSKRRSYHMQVPYNEKILSAIVIK | Function: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine. Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase activity.
Catalytic Activity: adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate
Sequence Mass (Da): 27182
Sequence Length: 240
EC: 2.4.2.1
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Q82FW3 | MTARIGVVTFPGSLDDRDTQRAIKLAGAEPVALWHKDKDLKQVDAVVLPGGFSYGDYLRAGAISRFSPVMETVIEQAKSGMPVLGICNGFQILTEAHLLPGAMLGNNHLHFICRDQKLRVENADTAWTSDYEAGQEIHIPLKNMDGRYVADERTLDMLEAEGRVAFRYVVGGAAADGYGNPNGSLRDIAGITNEAGNVVGLMPHPEHAVEPLIGTGRTDGLPFFTSILKKLVNA | Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 25255
Sequence Length: 234
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.5.3
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Q31Q18 | MNVGVIVFPGSNCDRDVQWVTAGLLGQSTRMIWHEERDLSGLDLIVVPGGFSYGDYLRCGAIARFSPAMQATVAFAEAGGLVLGICNGFQILTEVGLLPGALVRNRDLHFRCETTPLRVERSDRPWSRTYQQGQILNLPIAHGEGRYHADPATLAALEANGQVLFRYLDNPNGSCNDIAGITNVAGNVLGMMPHPERAAEAIAGSVDGLGLFAGLLEPVAA | Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 23601
Sequence Length: 221
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.5.3
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Q55843 | MTSFGIIVFPGSNCDRDIATVTAGLLDQPTRFIWHQETDLHGVDVVVLPGGFSYGDYLRCGAIARFSPIMTAIIDHANAGKRVLGICNGFQVLTEVGLLPGALIRNRDLHFICDRVTVRVESNQTVWTKGYQSQQVITLPIAHGEGRYFADGDTLKALEDNEQILFRYSNAQGELTTDSNPNGSLHNIAGITNVQGNVLGMMPHPERAADRLLKATDGLAMFIS | Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 24429
Sequence Length: 224
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.5.3
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Q9HIM1 | MKPPKVGILLMEGTNNETEVFFSVRRSGGDPDYVHVSDIAAGRKAISDYDALIVPGGFSAGDYIRAGVIFAARLLAVAGKEIRDFVDSGRPLIGICNGFQVIMEMGLIGKRDELTLTNNESGRFECRYTYITMTSDNPIFRDAFKGKGSFQVPVAHAEGRIAVSGVSVLKRLYENDQVLFKYSDTHGVTDEYPWNPNGSVDSIASLTNEHGNVIGLMPHPERIYYSYQAMYDDARKDQATGKLFYDSLISYLSGVHG | Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 28314
Sequence Length: 257
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.5.3
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Q0W4L8 | MGITARKVLGTPYANGAKLMFLGAGELGKETMIEAQRMGIEIVAVDRYANSPGMQVAHRSYVTNMKSERALLAIVEKEKPDAIIPEIEAINTDTLFKLEKEGFFVAPCANAVWTAMHRERLREAIASTGARTSKYEYATDLESFKAACKKIGFPCVSKPIMSSSGKGSYVLKSSKDVEKAFKEAAKARGSSDKIIVEEFIDFDVEITALSVRYLNGKGKPESKFVRPLGHYQIEGDYHASWHPWTDATDKKIDKLEKEIYDYAGRIMDKLGGYGLFAHEMFVDTKNGKVYANETACRPHDTGLVTIASMPFGYSEFALHAKAVLGIPIACEGKVIQPRSTAASHVILSHTEGWYPQFKVDGAYAPDTNVLIFGKPEAYEERRLGVVLATAGTVEDAKKKAQKAAHTVKVSANDKWAGQEITEKHYR | Function: Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate.
Catalytic Activity: ATP + formate + N(1)-(5-phospho-beta-D-ribosyl)glycinamide = ADP + H(+) + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Mass (Da): 46993
Sequence Length: 426
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (formate route): step 1/1.
EC: 6.3.1.21
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Q59S63 | MGDKFSVPTNQSKERQPIVKKKKKKKRTNIYSYILIISFPVIDQFQMSESLNIQELTDNSSIIPIPTESTDVQDVTSVSNKDTTTTTTTTTTTTESTTRVRKSSPSPSANENDKKRLKKEFQPRQKIEYTPLVDENGQPIPKAPRKPKRKVAVMLGYCGTGYNGMQVQNDPNVKTIEKDIYDAMATAGAISAENAVDLKKSGFQRAARTDKGVHAAGNVISLKMIIEDPEIINKINDLLPKQIRIWGIQRTTKGFDCRKCCSSRIYEYLLPTFSLLPPKPKSVLSELVKEKKLENPDLFEDDQEGIDWWENVKSKILASGITQEQIDSITSSYDEQQQQQQQQQQQQADEEERDISELSFTKLIKQIKTIENQSRRSYRISSSRLQHFREVMKQYEGTHNFHNFTVGKPFKDTSANRFMIKTIVSDPFVIEGTEWISIKIHGQSFMLHQIRKMIAMAALVVRLSLPCGIINNFFQSTKINIPKAPALGLLLENPVFDGYNIKLTKSDYEPIDFTKFDKEMNEFKMKYIYDKIYAEESKENIFYGFFGYIDAYRGNKNEDGEPIQNGASIFDFLFNYTERVENTKNKDAKNTSKTEESKPEESKPEESKSEQS | Cofactor: Binds 1 zinc ion per subunit.
Function: Formation of pseudouridine at positions 27 and 28 in the anticodon stem and loop of transfer RNAs; at positions 34 and 36 of intron-containing precursor tRNA(Ile) and at position 35 in the intron-containing tRNA(Tyr). Catalyzes pseudouridylation at position 44 in U2 snRNA. Also catalyzes pseudouridylation of mRNAs.
Catalytic Activity: a uridine in tRNA = a pseudouridine in tRNA
Sequence Mass (Da): 70099
Sequence Length: 612
Subcellular Location: Nucleus
EC: 5.4.99.-
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Q9Y606 | MGLQLRALLGAFGRWTLRLGPRPSCSPRMAGNAEPPPAGAACPQDRRSCSGRAGGDRVWEDGEHPAKKLKSGGDEERREKPPKRKIVLLMAYSGKGYHGMQRNVGSSQFKTIEDDLVSALVRSGCIPENHGEDMRKMSFQRCARTDKGVSAAGQVVSLKVWLIDDILEKINSHLPSHIRILGLKRVTGGFNSKNRCDARTYCYLLPTFAFAHKDRDVQDETYRLSAETLQQVNRLLACYKGTHNFHNFTSQKGPQDPSACRYILEMYCEEPFVREGLEFAVIRVKGQSFMMHQIRKMVGLVVAIVKGYAPESVLERSWGTEKVDVPKAPGLGLVLERVHFEKYNQRFGNDGLHEPLDWAQEEGKVAAFKEEHIYPTIIGTERDERSMAQWLSTLPIHNFSATALTAGGTGAKVPSPLEGSEGDGDTD | Function: Pseudouridylate synthase that catalyzes pseudouridylation of tRNAs and mRNAs . Acts on positions 27/28 in the anticodon stem and also positions 34 and 36 in the anticodon of an intron containing tRNA . Also catalyzes pseudouridylation of mRNAs: mediates pseudouridylation of mRNAs with the consensus sequence 5'-UGUAG-3' . Acts as a regulator of pre-mRNA splicing by mediating pseudouridylation of pre-mRNAs at locations associated with alternatively spliced regions . Pseudouridylation of pre-mRNAs near splice sites directly regulates mRNA splicing and mRNA 3'-end processing . Involved in regulation of nuclear receptor activity through pseudouridylation of SRA1 mRNA .
Catalytic Activity: a uridine in tRNA = a pseudouridine in tRNA
Sequence Mass (Da): 47470
Sequence Length: 427
Subcellular Location: Mitochondrion
EC: 5.4.99.-
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Q9WU56 | MGFPRLWAALLRNWGRWTARPGPRVPGLPPMAGNKVPPALASHQPDRKGRGGWVWEETEHPAKRVKGGEDEEPPRKLPKRKIVLLMAYSGKGYHGMQRNLGSSQFRTIEDDLVSALVQAGCIPENHGTDMRKMSFQRCARTDKGVSAAGQVVSLKVWLIDDILDKINSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPTFAFAHKDRDVQDESYRLSAETLQQVNRLLACYKGTHNFHNFTSQKGPREPSARRYILEMYCEEPFVREGLEFAVIKVKGQSFMMHQIRKMVGLVVAIVKGYAPESVLERSWGEEKVDVPKAPGLGLVLERVHFEKYNQRFGGDGLHEPLDWTQEEGKVTAFKEQYIYPTIVSTERDERSMAQWLNTLPIHNFSGTALGAADTGAKVPSSLEGSEGDGDTD | Function: Pseudouridylate synthase that catalyzes pseudouridylation of tRNAs and mRNAs . Acts on positions 27/28 in the anticodon stem and also positions 34 and 36 in the anticodon of an intron containing tRNA . Also catalyzes pseudouridylation of mRNAs: mediates pseudouridylation of mRNAs with the consensus sequence 5'-UGUAG-3' (By similarity). Acts as a regulator of pre-mRNA splicing by mediating pseudouridylation of pre-mRNAs at locations associated with alternatively spliced regions (By similarity). Pseudouridylation of pre-mRNAs near splice sites directly regulates mRNA splicing and mRNA 3'-end processing (By similarity). Involved in regulation of nuclear receptor activity through pseudouridylation of SRA1 mRNA .
Catalytic Activity: a uridine in tRNA = a pseudouridine in tRNA
Sequence Mass (Da): 47502
Sequence Length: 423
Subcellular Location: Nucleus
EC: 5.4.99.-
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Q4KM92 | MGFPRLWAALLRAWGRWTARPGPRVPGLPPMAGNKVPPALPSHQPDRKGRGGWVWEETEHPAKRVKGGEDEEPPRKLPKRKIVLLMAYSGKGYHGMQRNLGSSQFRTIEDDLVSALVQAGCIPENHGTDMRKMSFQRCARTDKGVSAAGQVVSLKVWLIDDILDKINSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPTFAFAHKDRDVQDESYRLSAETLQQVNRLLGCYKGTHNFHNFTSQKGPREPSARRYILEMYCEEPFVREGLEFAVIKVKGQSFMMHQIRKMVGLVVAIVKGYAPESVLERSWGEEKVDVPKAPGLGLVLERVHFEKYNQRFGSDGLHEPLDWAQEEGKVTAFKEQYIYPTIVSTERDERSMAQWLNTLPIHNFSGTALGADDTGAKVPSSLEGSEGDGDTD | Function: Pseudouridylate synthase that catalyzes pseudouridylation of tRNAs and mRNAs. Acts on positions 27/28 in the anticodon stem and also positions 34 and 36 in the anticodon of an intron containing tRNA. Also catalyzes pseudouridylation of mRNAs: mediates pseudouridylation of mRNAs with the consensus sequence 5'-UGUAG-3'. Acts as a regulator of pre-mRNA splicing by mediating pseudouridylation of pre-mRNAs at locations associated with alternatively spliced regions. Pseudouridylation of pre-mRNAs near splice sites directly regulates mRNA splicing and mRNA 3'-end processing. Involved in regulation of nuclear receptor activity through pseudouridylation of SRA1 mRNA.
Catalytic Activity: a uridine in tRNA = a pseudouridine in tRNA
Sequence Mass (Da): 47515
Sequence Length: 423
Subcellular Location: Nucleus
EC: 5.4.99.-
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O94396 | MGRGGKRTWYNGDRREAKRNRPNSIYNGEGRPENLVVGEKKPKRKVACLVGYCGSGYHGMQLNPPSKTIEGDLFDAFVKAGAVSSYNADDPKKVALARAARTDKGVHAAGNVISLKLIMEDEKLIEKVNEHLPPSIRLWDVIRTINSFNPRTYCESRIYEYMVPTYAFVPPKPSSILGNCIMKNSPMPAEPINKENINQLSRSLFYEEGKEFWDDYDIAAKEILSLYEQDPEGFVNPYSKRGAAALANSENNKGSEAGVSAKTNPDMDSDSSAIVNEFLKPDSVEDESAGSKIDPSYRLERALKHIEVLKLKNYRISADRLSVIRETLNQYVGVHNFHNFTVGQAFHQKNSNRVIRSFTASDPFMIGDTEWISCKVHGQSFMLHQIRKMIALAILVVRTGCPVERIQDAFKKTKINIPKGPGFGLLLESPFFKGYNEHKAPENNRDPIDFTKYEQKITAFKHAHIYDKIFLEEARKQVFHCFLSFIDSYNEEDFSYLSDIGITEKTQEVSSKLPDVLSSDEEEDSAENKDDLEG | Cofactor: Binds 1 zinc ion per subunit.
Function: Formation of pseudouridine at positions 27 and 28 in the anticodon stem and loop of transfer RNAs; at positions 34 and 36 of intron-containing precursor tRNA(Ile) and at position 35 in the intron-containing tRNA(Tyr) . Catalyzes pseudouridylation at position 44 in U2 snRNA (By similarity). Also catalyzes pseudouridylation of mRNAs (By similarity).
Catalytic Activity: a uridine in tRNA = a pseudouridine in tRNA
Sequence Mass (Da): 60324
Sequence Length: 534
Subcellular Location: Nucleus
EC: 5.4.99.-
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Q6CC39 | MSEPTTTPVVGNSASGDSAEQHDLGQKRGKGGNWNRPRGDHQAKKQKMDRRGDRQREQEKQGEGRDTRRKTDGPLVADEVRQPKRKVACMIGYCGTGYHGMQLNPPQKTIEGDIFQAFVKAGAISQNNADDPKKSAFMRAARTDKGVHAAGNVISLKMIIEDENIVEKINSHLPEQLRVWGVSRTNKAFECRKLCSSRVYEYLMPTYSFLNPRPGTVMSEKLLKDGTSPDEEGKKYWESVAADLESQGVSYDEWMKRACIDEIKGEETKEVAESEVKTDSKTDAATLEKIKAVERRHREEFRISGERLAKIREILKIYEGTHNFHNFTLGKAFKDPSAMRTMKSLTCSDPFLIDGTEWVSIKIHGQSFMLHQIRKMISMVALSVRCNADPQKLIPQTFEKARINIPKAPALGLLLERPVYDSYNKKLQGEFGREGVHFDNWNDQIEAFKHKFIYDKIYAEEKGQHVFHAFFSFVDVFTGDASFDFLLKQGITKECTTDYMNKKAKEEGKEIKKLEEDDDEVANEQNEG | Cofactor: Binds 1 zinc ion per subunit.
Function: Formation of pseudouridine at positions 27 and 28 in the anticodon stem and loop of transfer RNAs; at positions 34 and 36 of intron-containing precursor tRNA(Ile) and at position 35 in the intron-containing tRNA(Tyr). Catalyzes pseudouridylation at position 44 in U2 snRNA. Also catalyzes pseudouridylation of mRNAs.
Catalytic Activity: a uridine in tRNA = a pseudouridine in tRNA
Sequence Mass (Da): 60051
Sequence Length: 528
Subcellular Location: Nucleus
EC: 5.4.99.-
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Q12211 | MSEENLRPAYDDQVNEDVYKRGAQSKLTKARKADFDDEKDKKKDNDKHIDKRPKSGPRLDENGNPLPKEPRLPKRKVAVMVGYCGTGYHGMQYNPPNPTIESALFKAFVEAGAISKDNSNDLKKNGFMRAARTDKGVHAGGNLISLKMIIEDPDIKQKINEKLPEGIRVWDIERVNKAFDCRKMCSSRWYEYLLPTYSLIGPKPGSILYRDIEESKTELPGVLDEDLESKEFWEEFKKDANEKFSTEEIEAILAYVPPARDEFDINEELYQKVKKYKQLENAHRRRYRISAAKLAKFRASTSQYLGAHNFHNFTLGKDFKEPSAIRFMKDIKVSDPFVIGDAQTEWISIKIHGQSFMLHQIRKMVSMATLITRCGCPVERISQAYGQQKINIPKAPALGLLLEAPVFEGYNKRLEQFGYKAIDFSKYQDEVDKFKMKHIYDKIYKEEVDENVFNAFFSYIDSFNKVTGAQGEETADKSGPAVQKSIFEFLTAKGIPGLTDAPESNKKIKQRKRMEEEEAASKKAEISSTTQSNEPEVQPEAAAN | Cofactor: Binds 1 zinc ion per subunit.
Function: Formation of pseudouridine at positions 27 and 28 in the anticodon stem and loop of transfer RNAs; at positions 34 and 36 of intron-containing precursor tRNA(Ile) and at position 35 in the intron-containing tRNA(Tyr) . Catalyzes pseudouridylation at position 44 in U2 snRNA . Also catalyzes pseudouridylation of mRNAs .
Catalytic Activity: a uridine in tRNA = a pseudouridine in tRNA
Sequence Mass (Da): 62143
Sequence Length: 544
Subcellular Location: Nucleus
EC: 5.4.99.-
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Q3ECD0 | MLSISQLPSFSLTTAKSLRYPSSPSSSLSIFFSFFPKVSNFVRASSGIPNLVACSPTEIIIPRVNNAGLRIEEIVDAAKGKIRLDSWISSRINGVSRARVQSSIRLGLVTVNGRVVDKVSHNVKSGDEVNCTISELQPLKAEAEDIPLDIVYEDKHVLVVNKPAHMVVHPAPGNPTGTLVNGILHHCSLPCVDYSNSEEDDDSDEETFSDDEEMTTSPSSYAASVRPGIVHRLDKGTTGLLVVAKDEHSHAHLAEQFKLHTIERVYVSLTTGVPSPPQGRIEIPIGRDSSNRIRMAAIPGGVRGGRARHAASRYKVIETFAGGGSALVEWRLETGRTHQIRAHAKYMGVPLLGDEVYGGTKSMALSLLQKRVSRSDQEEIIELISRMDRPCLHAIVLGFTHPCTGEIVKFSCPPPSDLAEIVGLLRRSGL | Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Mass (Da): 46715
Sequence Length: 430
Subcellular Location: Plastid
EC: 5.4.99.-
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Q5Z8P2 | MATTAAASPPAIATALSALLRRQRRRSSRCVGASHARCLAADANAEAVAPSRRGGHGGTRLEEAVPAGEGRSRIDAWISARLGGGGVSRARIQASIRAGLVVVNGRPVSKVSHMVKGGDIVSCTVLELQPLRAEPEDIPLDIVYEDDHLLVVNKPAHMVVHPAPGNANGTLVNAILHHCKISTFTCLARNSIDDECPDSSDDDIDVFDIDQFTTGEVSSEVREALVRPGIVHRLDKGTSGLLVVAKDEHSHAQLAEQFKLHTIRRVYISLTCGAPNPNSGRIEVPIARDPNNRIRMIATPGSGHRYARHAASRYKVREVFAGGGSALVEWRLETGRTHQIRAHAKYLGIPLLGDETYGGTKSMALSLLRPRTPSRYHCDLSNMISKIDRPCLHAALLGFKHPHSGKILEFSCPPPDDFTEVLNELHQVTLASNGNSGGGVARICD | Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Mass (Da): 47839
Sequence Length: 445
Subcellular Location: Plastid
EC: 5.4.99.-
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O94295 | MTSISKRKNQQEHIPAEDLETPKLPKREKIEGTKESNKVRIIILLGYSGYGYHGIQINNPLKTIEGDVVAVLKKLGYLKTNNIDAEHLCIARAARTDKGVHTLRNLISLNLFVDKPLDISLLKTELNEALCSQIRVWSVFPAPKYFNPRISCESRTYEYLIPSFALLPPKPSCPLFKKMQKNLSRKLDNELERNLVYSMNDLISFWNTVKLKQKEIQEMFDTNKDAFTNPFKGMFYEKPIPAGIVIPPQAKLKKALKQAEYYCYMNYRIKEDRLKVLQQLLKKYEGRHNFHNFTVTDDSTSPSNYRFIESVTCGTPFVYENWEWIPVTIKGNSFMLNQIRKMMAHVLMIIRSCAPTGLIDKAFDPNITMNISKSPGHVLLLKDIKFSSYNDSVTDGLEKIQFDCFEEDILSLKIKTIYPDIIKLEQKEKLFFSFLSYIDQHTGHQFDYLFG | Cofactor: Binds 1 zinc ion per subunit.
Function: Formation of pseudouridine at positions 27 and 28 in the anticodon stem and loop of transfer RNAs; at positions 34 and 36 of intron-containing precursor tRNA(Ile) and at position 35 in the intron-containing tRNA(Tyr).
Catalytic Activity: a uridine in tRNA = a pseudouridine in tRNA
Sequence Mass (Da): 52272
Sequence Length: 451
Subcellular Location: Nucleus
EC: 5.4.99.-
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P53167 | MLLGYCGSGYYGMQYNPPHKTIEGEILTKLFDVGAISEENSLAPKKNSFMAAARTDKGVHAMLNLLSLKITLREDTVAKLNAALPPEIRVWGIQPVNKKFNARSACDSRWYQYLIPEFILIGPPRSSLLHRNVGGCYREDGSQEVWDTFLEQTRGRFSGDELCRLQDTAQKLSESDPLVQDYVGLLSGTLSGYCLSPSKLDAFEAAMQEYVGTHNFHNFTTGKLWGDPSAQRHIKKVVVSQASPGWICVRIHGQSFMLHQIRRMVALAVLAARCQLPPNIVRNYFNAGPRKYIPRAPAQGLLLEGPVFDGYNTKLRNLLYCEIRPDDITLERMCRFRERQICTAIAHEETQRHVFCHFVRQMNRLATPLI | Function: Mitochondrial-specific pseudouridine synthase catalyzing the formation of pseudouridine at positions 27 and 28 in the anticodon stem and loop of mitochondrial transfer RNAs.
Catalytic Activity: uridine(27/28) in mitochondrial tRNA = pseudouridine(27/28) in mitochondrial tRNA
Sequence Mass (Da): 41891
Sequence Length: 370
Subcellular Location: Mitochondrion
EC: 5.4.99.44
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Q5XET6 | MWKAKTCFRQIYLTVLIRRYSRVAPPPSSVIRVTNNVAHLGPPKQGPLPRQLISLPPFPGHPLPGKNAGADGDDGDSGGHVTAISWVKYYFEEIYDKAIQTHFTKGLVQMEFRGRRDASREKEDGAIPMRKIKHNEVMQIGDKIWLPVSIAEMRISKRYDTIPSGTLYPNADEIAYLQRLVRFKDSAIIVLNKPPKLPVKGNVPIHNSMDALAAAALSFGNDEGPRLVHRLDRETSGLLVMGRTKESIDYLHSVFSDYKGRNSSCKAWNKACEAMYQQYWALVIGSPKEKEGLISAPLSKVLLDDGKTDRVVLAQGSGFEASQDAITEYKVLGPKINGCSWVELRPITSRKHQLRVHCAEALGTPIVGDYKYGWFVHKRWKQMPQVDIEPTTGKPYKLRRPEGLDVQKGSVLSKVPLLHLHCREMVLPNIAKFLHVMNQQETEPLHTGIIDKPDLLRFVASMPSHMKISWNLMSSYLV | Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Mass (Da): 53801
Sequence Length: 478
Subcellular Location: Mitochondrion
EC: 5.4.99.-
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Q9BZE2 | MAYNDTDRNQTEKLLKRVRELEQEVQRLKKEQAKNKEDSNIRENSAGAGKTKRAFDFSAHGRRHVALRIAYMGWGYQGFASQENTNNTIEEKLFEALTKTRLVESRQTSNYHRCGRTDKGVSAFGQVISLDLRSQFPRGRDSEDFNVKEEANAAAEEIRYTHILNRVLPPDIRILAWAPVEPSFSARFSCLERTYRYFFPRADLDIVTMDYAAQKYVGTHDFRNLCKMDVANGVINFQRTILSAQVQLVGQSPGEGRWQEPFQLCQFEVTGQAFLYHQVRCMMAILFLIGQGMEKPEIIDELLNIEKNPQKPQYSMAVEFPLVLYDCKFENVKWIYDQEAQEFNITHLQQLWANHAVKTHMLYSMLQGLDTVPVPCGIGPKMDGMTEWGNVKPSVIKQTSAFVEGVKMRTYKPLMDRPKCQGLESRIQHFVRRGRIEHPHLFHEEETKAKRDCNDTLEEENTNLETPTKRVCVDTEIKSII | Function: Formation of pseudouridine at position 39 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39) in tRNA = pseudouridine(38/39) in tRNA
Sequence Mass (Da): 55647
Sequence Length: 481
Subcellular Location: Nucleus
EC: 5.4.99.45
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Q9JI38 | MAENTDRNQIEKLLNRVKELEQEVERLKKKKEQANNIKDSSIRENSLGSGKAKRAFDFSAHGRRHVALKIAYLGWGYQGFASQENTSNTIEEKLFEALTKTRLVESRQTSNYHRCGRTDKGVSAFGQVISLDLRSQFPTSRDSEDSNLKHEADDLAKEIRYTHILNRVLPADIRVLAWAPVEPSFSARFSCLERTYRYFFPRADLDIATMNYAAQKYVGTHDFRNLCKMDVANGVINFQRTILCAQVQLVAQSPGEERRQEPFQLCQFEVIGQAFLYHQVRCMMAILFLIGQGMEKPEIIDELLNIQKNPQKPQYSMAVEFPLVLYDCKFENTKWIYDHEVQEFNVTHLQQLWANHAVKTHMLYSMLQGLDSVMVTCAAGTKMDEATEWRNIQPPVIKHTSAFVEGVKMRTYKPLMDRPKCQGLESRIRHFVSRGRIEHPHLLHKEEIKARRDCADKEENTVVENPSKRVCIIDAEINSIA | Function: Formation of pseudouridine at position 39 in the anticodon stem and loop of transfer RNAs. Also acts on position 38, but much less efficiently.
Catalytic Activity: uridine(38/39) in tRNA = pseudouridine(38/39) in tRNA
Sequence Mass (Da): 55546
Sequence Length: 481
Subcellular Location: Nucleus
EC: 5.4.99.45
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Q0J4D4 | MLCRRRRVGAAVRWLSRLAPPAPAEADPVVVRVDGSNVARLGKPKPGPRPRQLLSLPPFPGGGDGDPLPGRKAAAPRRVTAVSWVKHYLADVPQEVVQAHFNKRLVYSECSDHEVSVETIKSQKHHLKKIKHNDVMEPGMRIHLPVSVAEGEIKKRYETIPTATLHPNKDEIEYLRRLVIHKDSAILVLNKPPKVPMKGNLPVHNSMDVLAAAALSYGNEEGPKLVHRLDRESSGLLLFGRTKESFTRLHWLFTSVNLAKTNSQVWNAACEAYMQRYWALVIGTPKEREGIISAPLSKVLLDDGKAERVILAHPSGIDGAQEAVTAYRVMGPTIHGCSWIELRPLTGRKHQLRVHCAEALGTPIVGDYKYGWFVHQRWKQNPQPDFEPFTGEPYKLRRPEGLEIQKGSVLSKVPLLHLHCREMVIPNIAKFLSSNGEWHENGAPWSKEKPNLLRFIAPMPAHMKISWNIMSSYLV | Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Mass (Da): 53324
Sequence Length: 475
Subcellular Location: Mitochondrion
EC: 5.4.99.-
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Q9DC11 | MARFRRADLAAAGVMLLCHFLTDRFQFAHGEPGHHTNDWIYEVTNAFPWNEEGVEVDSQAYNHRWKRNVDPFKAVDTNRASMGQASPESKGFTDLLLDDGQDNNTQIEEDTDHNYYISRIYGPADSASRDLWVNIDQMEKDKVKIHGILSNTHRQAARVNLSFDFPFYGHFLNEVTVATGGFIYTGEVVHRMLTATQYIAPLMANFDPSVSRNSTVRYFDNGTALVVQWDHVHLQDNYNLGSFTFQATLLMDGRIIFGYKEIPVLVTQISSTNHPVKVGLSDAFVVVHRIQQIPNVRRRTIYEYHRVELQMSKITNISAVEMTPLPTCLQFNGCGPCVSSQIGFNCSWCSKLQRCSSGFDRHRQDWVDSGCPEEVQSKEKMCEKTEPGETSQTTTTSHTTTMQFRVLTTTRRAVTSQMPTSLPTEDDTKIALHLKDSGASTDDSAAEKKGGTLHAGLIVGILILVLIIAAAILVTVYMYHHPTSAASIFFIERRPSRWPAMKFRRGSGHPAYAEVEPVGEKEGFIVSEQC | Function: May play a role in tumor angiogenesis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 59616
Sequence Length: 530
Subcellular Location: Membrane
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O81270 | MGSKTEMMERDAMATVAPYAPVTYHRRARVDLDDRLPKPYMPRALQAPDREHPYGTPGHKNYGLSVLQQHVSFFDIDDNGIIYPWETYSGLRMLGFNIIGSLIIAAVINLTLSYATLPGWLPSPFFPIYIHNIHKSKHGSDSKTYDNEGRFMPVNLELIFSKYAKTLPDKLSLGELWEMTEGNRDAWDIFGWIAGKIEWGLLYLLARDEEGFLSKEAIRRCFDGSLFEYCAKIYAGISEDKTAYY | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group.
Function: Calcium-binding peroxygenase involved in the degradation of storage lipid in oil bodies. May be involved in the interaction between oil bodies and vacuoles during seed germination and in the oxylipin signaling pathways and plant defense responses. Can catalyze sulfoxidation of thiobenzamide, hydroxylation of aniline, epoxidation of oleic acid or intramolecular oxygen transfer.
PTM: Phosphorylated. Partially phosphorylated at Ser-225, but not phosphorylated at Ser-72, Tyr-145, Thr-166 or Ser-172. Phosphorylation is not required for catalytic activity.
Catalytic Activity: RH + ROOH = ROH + ROH.
Sequence Mass (Da): 28038
Sequence Length: 245
Domain: The proline-knot motif (118-127) may be involved in targeting to lipid bodies.
Subcellular Location: Microsome membrane
EC: 1.11.2.3
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G1JSL4 | MAEDAVVSDAVVVSDAMSSVAKGAPVTAQRPVRDDLEKHIPKPYLARALVAVDVNNPEGTKGGRHEHGQKSVLQQHVSFFDQNGDGIIYPWETFRGLRRLGFNLIVSFIVAIGIHTGLSYPTLPTWRPSLLFPVYIDRIHKAKHGSDTATFDTEGRFMPVNFENIFSKNARSQPDKLTLREIWMMTNDHRLAYDPFGWVANKGEWILLYMLAKDDEGYLPKEAIRGVYDGSLFEFLAEQRTKKAHGKQH | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group.
Function: Calcium-binding peroxygenase involved in cutin monomers biosynthesis. Can catalyze epoxidation of fatty acid and sulfoxidation reactions that can proceede competitively, although in favor of the sulfoxidation. Can only use unsaturated fatty acids with double bonds in the cis configuration as substrates. The preferred substrate is oleic acid and is inactive toward ricinoleic acid. Free fatty acid and fatty acid methyl esters are effective substrate forms, but not phospholipids and acyl-CoA. Hydroperoxy-trienoic (HPOT) acids are preferred over Hydroperoxy-dienoic (HPODT) acids as oxygen donors.
Catalytic Activity: RH + ROOH = ROH + ROH.
Sequence Mass (Da): 28107
Sequence Length: 249
Domain: Transmembrane regions are predicted by sequence analysis tools, but these regions probably constitute hydrophobic domains associated to phospholipids.
Subcellular Location: Microsome membrane
EC: 1.11.2.3
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Q9FLN9 | MTSMERMERDAMETVAPYARVTYHRRVRGDLDDTLPKPYLPRALQAPDMEHPQGTPDHRHNGLSVLQQHVAFFDLDNNGIIYPFETFSGFRLLGFNLLASLILAAGINIALSYATLPGWLPSPFFPIYIHNIHKAKHGSDSKTYDNEGRYTPANLELMFSKYARTIPDKLSLGELWDMTEGNRDAFDFFGWLASKVEWGVLYALASDEEGFLSKEAIRRCFDGSLFEYCAKNYAEIKEYKTYY | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group.
Function: Calcium-binding peroxygenase involved in the degradation of storage lipid in oil bodies. May be involved in the interaction between oil bodies and vacuoles during seed germination and in the oxylipin signaling pathways and plant defense responses. Can catalyze sulfoxidation of thiobenzamide, hydroxylation of aniline and epoxidation of oleic acid.
Catalytic Activity: RH + ROOH = ROH + ROH.
Sequence Mass (Da): 27876
Sequence Length: 243
Domain: Transmembrane regions are predicted by sequence analysis tools, but these regions probably constitute hydrophobic domains associated to phospholipids.
Subcellular Location: Lipid droplet
EC: 1.11.2.3
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O22788 | MAGEAEALATTAPLAPVTSQRKVRNDLEETLPKPYMARALAAPDTEHPNGTEGHDSKGMSVMQQHVAFFDQNDDGIVYPWETYKGFRDLGFNPISSIFWTLLINLAFSYVTLPSWVPSPLLPVYIDNIHKAKHGSDSSTYDTEGRYVPVNLENIFSKYALTVKDKLSFKEVWNVTEGNRMAIDPFGWLSNKVEWILLYILAKDEDGFLSKEAVRGCFDGSLFEQIAKERANSRKQD | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group.
Function: Probable calcium-binding peroxygenase. May be involved in the degradation of storage lipid in oil bodies, in abiotic stress-related signaling pathway and in drought tolerance through stomatal control under water deficit conditions.
PTM: Phosphorylated. Increased phosphorylation upon stress.
Catalytic Activity: RH + ROOH = ROH + ROH.
Sequence Mass (Da): 26600
Sequence Length: 236
Domain: Transmembrane regions are predicted by sequence analysis tools, but these regions probably constitute hydrophobic domains associated to phospholipids.
Subcellular Location: Microsome membrane
EC: 1.11.2.3
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Q9CAB7 | MASSISTGVKFVPEEDNFLQRHVAFFDRNKDGIVYPSETFQGFRAIGCGYLLSAVASVFINIGLSSKTRPGKGFSIWFPIEVKNIHLAKHGSDSGVYDKDGRFVASKFEEIFTKHAHTHRDALTNEELKQLLKANKEPNDRKGWLAGYTEWKVLHYLCKDKNGLLHKDTVRAAYDGSLFEKLEKQRSSKTSKKHP | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group.
Function: Calcium-binding peroxygenase involved in the degradation of storage lipid in oil bodies. May be involved in the interaction between oil bodies and vacuoles during seed germination (By similarity). Acts as a negative regulator of abscisic acid responses in non-seed tissues.
Catalytic Activity: RH + ROOH = ROH + ROH.
Sequence Mass (Da): 22092
Sequence Length: 195
Domain: Transmembrane regions are predicted by sequence analysis tools, but these regions probably constitute hydrophobic domains associated to phospholipids.
Subcellular Location: Lipid droplet
EC: 1.11.2.3
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Q9CAB8 | MASSISAAEVKVVPEEYNFLQKHVAFFDRNKDGIVYPSETFQGFRAIGCGYLLSTFAAVFINISLSSKTRPGKGFSFSFPIEVKNVRLGIHSSDSGVYDKDGRFVASKFEEIFAKHAHTHRDALTSKELKELLKANREPNDCKGGILAFGEWKVLYNLCKDKSGLLHKEIVRAVYDGSLFEQLEKQRSSKTP | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group.
Function: Calcium-binding peroxygenase involved in the degradation of storage lipid in oil bodies. May be involved in the interaction between oil bodies and vacuoles during seed germination (By similarity).
Catalytic Activity: RH + ROOH = ROH + ROH.
Sequence Mass (Da): 21519
Sequence Length: 192
Domain: Transmembrane regions are predicted by sequence analysis tools, but these regions probably constitute hydrophobic domains associated to phospholipids.
Subcellular Location: Lipid droplet
EC: 1.11.2.3
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A8B479 | MGSTSDPSPSIITVAAEAPVTAERKQNLHLQEQLAKPYVARALAAVDPAHPNGTEGHEHHNMSVLQQRAAFFDRNNDGIVYPWETYQGFRAVGFGVLTSILGGFLINLGLSYRSQPSWIPSPVLSIHIKNIHRCKHGSDTESYDTEGRFEPSKFDAIFSKYALTQPDALTSEEISTMLQVNRNLLDFIGWVASIAEWRLLYQIGKDEDGLLHKETIRGAFDGSLFERLEKDRASRTKIV | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group.
Function: Calcium-binding peroxygenase involved in the degradation of storage lipid in oil bodies.
Catalytic Activity: RH + ROOH = ROH + ROH.
Sequence Mass (Da): 26696
Sequence Length: 239
Domain: Transmembrane regions are predicted by sequence analysis tools, but these regions probably constitute hydrophobic domains associated to phospholipids.
Subcellular Location: Lipid droplet
EC: 1.11.2.3
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D7A0Y0 | MDEPVRLSLAEVHVLCRDTLVAAGLGEEHAQAIARSITRAEADECHSHGLYRLIGYVASVRSGKAERHALPALARATPAVLRVDAKHGFAPLAVETGVPALIAAAKEIGIAALAIHDCYHFSALWADIEPAVEAGLAAWCFTVGQCCVAPAGGTTPLLGTNPFAFGWPGPSGRPFIFDFATSAAARGEIELKRRGGEKIPPGWAVGPDGAPTTDPAAALAGALLPFGGHKGSALSMMVELIAGPLIGDLTSRQSKAVENGDGGPPLGGELFIAIDPAVFGTGNLSSRLADADELFALAKAQPGVRLPSERRYQARERSRTNGIAVPAALFAELQALGPRGS | Function: Catalyzes the reduction of Delta(1)-pyrroline-2-carboxylate (Pyr2C) to L-proline, using NADPH as the electron donor. Is likely involved in a degradation pathway that converts cis- and trans-3-hydroxy-L-proline (c3LHyp and t3LHyp) to L-proline, which would allow S.novella to grow on c3LHyp or t3LHyp as a sole carbon source.
Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-2-carboxylate + H(+) + NADH
Sequence Mass (Da): 35221
Sequence Length: 341
EC: 1.5.1.49
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P80558 | MSRLFKITALVPSLSRTRTQRELQNTYFTKLVPYENWFREQQRIQKAGGKIIKVELATGKQGTNAGLQ | Function: Rod linker protein, associated with allophycocyanin. Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 7840
Sequence Length: 68
Subcellular Location: Cellular thylakoid membrane
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O30019 | MFSKILVANRGEIAVRVMRACRELGIKTVGVYSSADKRAFHRVYADECYYIGKADPRDSYLNIDRIIEVAKKSGAEAIHPGYGFLAENAEFAERCEEEGIVFIGPSPEVIRIAGSKVRSRESMQRAGVPVIPGSPKIDTVDEAKEWAEKIGYPVAVKASGGGGGIGIVVVNSQEELEEAFRKSKKLGESYFKDSTVYLEKYLARPRHIEVQILADQHGNVIHLGERECSIQRRHQKLIEEAPSPALNEEMREELGKLAVKGAREIGYTNAGTFEFLYENGNFYFLEINSRLQVEHTITEVVTGIDIVKYQIRIAYGEELRHGQEDVAIRGHAIECRINAEDPVNFYPRSGRILHYRSPGGIGIRVDSGIHMGYRIPEEYDSMISKLIAYGETREEAIARMKRALYEYIIEGVETNIPFHFAVLNDEEFVRGNIHTKFVEERNIAEKVKEYLRIFRPIKARLDEIFMESEFTWEEISAIVTAIDAYEQELERGIEERIWQAIFSLGA | Function: Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.
Catalytic Activity: ATP + hydrogencarbonate + pyruvate = ADP + H(+) + oxaloacetate + phosphate
Sequence Mass (Da): 57438
Sequence Length: 506
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 6.4.1.1
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Q58626 | MFNKVLIANRGEIAIRIIRACWELGIKTVAVYSEADKRSLHATLADEAYCIGPAPAAKSYLNIDAILNVAEKAKVDAIHPGYGFLAENAEFARAVKKAGFEFIGPNPDAIEAMGSKINAKKIMKKAGVPLIPGSEGAIEDIDEAIEIAEAIGFPVVVKASAGGGGMGMSVAYSKEELKEVIESARNIAKSAFGDPTVFIEKYLENPRHIEIQLLGDKHGNIIHLGDRECSIQRRHQKLIEEAPSPIMTEELRERMGEAAIKAGKAINYDSAGTVEFLYENGNFYFLEMNTRIQVEHTVTEQVTGIDLVKAMIKIAAGEELTLKQEDVKIRGHAIECRINAEDPLNDFVPCPGKIKLYRSPGGPGVRIDSGVYGGAEIPPYYDSMIAKLITYGNSREEAIARMKRALREYVIIGVKTNIPFHRAVLEEENFLKGNISTHYVEQNMHKLREKMVKYALESRDLYSVVSEKVFEKNKKIAAAVGGLTMYISQIMKENEVNNKEW | Function: Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.
Catalytic Activity: ATP + hydrogencarbonate + pyruvate = ADP + H(+) + oxaloacetate + phosphate
Sequence Mass (Da): 55403
Sequence Length: 501
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 6.4.1.1
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Q58628 | MVKIVDTTFRDAQQSLIATRMRTEDMLPIAEKMDEVGFYSMEVWGGATFDACIRYLNEDPWERLRALKKRIQNTPLQMLLRGQNLVGYRHYPDDIVEKFVIKAHENGIDIFRIFDALNDVRNMETAIKTAKKVGAEVQGAICYTISPVHTIDQYVELAKKLEEMGCDSICIKDMAGLLTPYEGYELVKRLKEEISLPIDVHSHCTSGLAPMTYLKVIEAGADMVDCAISPFAMGTSQPPTESIVVALKGTKYDTGLDLKLLNEIRDYFMKVREKYKMLFSPISQIVDARVLVYQVPGGMLSNLVSQLKEQGALDKFEEVLQEIPRVRKDLGYPPLVTPTSQIVGTQAVLNVLTEERYKIITNEVVNYVKGFYGKPPAPINPELLKRVLDEGEKPITCRPADLLPPEWEKVKKEAEEKGIVKKEEDILTYALYPQIAVKFLRGELKAEPIPKEKDIGKILEIPTEYIVEVDGEKFEVKIEPKIGTELKRKKEVITAEMEGAVTSPFRGMVTKIKVKEGDKVKKGDVIVVLEAMKMEHPIESPVEGTVERILIDEGDAVNVGDVIMIIK | Function: Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.
Catalytic Activity: ATP + hydrogencarbonate + pyruvate = ADP + H(+) + oxaloacetate + phosphate
Sequence Mass (Da): 63908
Sequence Length: 567
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 6.4.1.1
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O27179 | MKGIKVVETAFRDAHQSLLATRLRTRDMTPIAEEMDRVGFFSLEAWGGATFDTCIRYLNEDPWERLRELKEHVKRTPIQMLLRGQNLVGYKHYPDDIVRKFIEKSYENGVDVFRIFDALNDIRNMEYAIKVAREQEAHVQGVICYTISPYHTLESYVDFARELEALECDSVAIKDMAGLISPHDAYELVRALKEETDLMVNLHCHCTSGMTPMSYYAACEAGVDILDTAISPLSWGASQPPTESIVAALRDTPYDTGLDLEILKNIKKYFEEIRKKYSSILDPIAEQIDTDVLIYQIPGGMLSNLVAQLKEQNALDRYEEVLEEMPRVRKDMGYPPLVTPTSQIVGIQAVMNVLSGERYSMVTNEVKDYFRGLYGRPPAPLNEEVARKVIGDEKPIDCRPADILKPQYDECRRKGEEMGIIEKEEDILTLALYPAIAPKFLRGEIEEEPLEPPAEEMAPTGEVPTVFHVEVDGDEFEVKVVPTGYMTIEEAEPEPVDVEGAVKSTMQGMVVKLKVSEGDQVNAGDVVAVVEAMKMENDIQTPHGGVVEKIYTAEGEKVETGDIIMVIK | Function: Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.
Catalytic Activity: ATP + hydrogencarbonate + pyruvate = ADP + H(+) + oxaloacetate + phosphate
Sequence Mass (Da): 63955
Sequence Length: 568
EC: 6.4.1.1
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P0DV24 | MSFKDVTAKNFKGLKNVSLKKSMAMEGHTLVGTEARLGDAFELCESFSTSPSNIIEYEYQEEIRPFFQKAGLNKHSIGTHPELTGLGVGMIYNQYTVTMFVDIRKSSRLSLLLPLEQVYVVKNRILQACIDIVRALDGYPHRLMGDALMAFFGRSDVSKEDAIADAINAASTLRLILMDYIFPSLNEDIGEQIDLGVRIGLDYGAEDEVVWGNFGLGSFCEVTALGLPVDMTAKLQQLADKNTAMLGQGILDYIDFPEEYTKPKVKSGEELKYIIPNITNKEGQPINRRIRLLNMARYQELLPFKLNDKKMASAILYPNQFNFECFVIEDNKEVLYNSVSRFLPKKRRLTFKLSIYPGPGIGDLKIIFCKRNHGQEAKDDLSEDYSISIEDNKLIRVKNADNLSLLRKDGCYVLTVPEETLFRGLHTMEVIVRGNHETLFYRNIIGVYIK | Cofactor: Cannot be replaced by Mg(2+).
Function: Pycsar (pyrimidine cyclase system for antiphage resistance) provides immunity against bacteriophage. The pyrimidine cyclase (PycC) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signal activates the adjacent effector, leading to bacterial cell death and abortive phage infection. A clade E Pycsar system.
Catalytic Activity: CTP = 3',5'-cyclic CMP + diphosphate
Sequence Mass (Da): 50981
Sequence Length: 450
Domain: Has an N-terminal nucleotide cyclase domain and a C-terminal nucleotide sensor domain (AGS-C); removal of the latter leads to loss of phage P1 and T5 resistance.
Subcellular Location: Cytoplasm
EC: 4.6.1.6
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A4D9R2 | MVSSFSSKRLGDTMDSLALGSNWAGGVAIVLFLAPLALHLVSSYLFPSTSTVINSGRAWDIFRTTAKKRFRSDAARLLQNGFEKSPDAFRILTDNGPLLVLSPRYAREVRSDDRLSLDHFIASEFHPDIPGFEPFKLILDPRNPLNTILKTSLTQALEDLSVEVADALSTALTDDSEWHEISPCQTALKLVAQMASKAFIGPEKCRDPKWHNVIITYTHNVYRAAQALHFWPKFLRPIVARFLPACQTLQAQIAEAREILEPLVAQRRADRACRAAQGKPVPSRADVIDWLEDSHGDQPYDPVAAQLLLSFAAIHGTSNLLAQALMDLCTAPDLIRDIRAEITSVLGDAGLTRAALYRLKLMDSALKESQRLAPNRLLSMGRIAQSDMHLSDGLRIPRGTTLMVSAHAMWEPQIYPDPRRYDGYRFYKLRQVPGQEGQHQLVSATEKHMGFGYGKHACPGRFFAAAEIKVALCHILLKYDLEHRGGGPPPRVWSQGIHLFPDPTARIRVRRRKEEISL | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of pyripyropene A, a specific human acyl-coenzyme A:cholesterol acyltransferase 2 inhibitor . The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase pyr1 . Nicotinyl-CoA is then a substrate of polyketide synthase pyr2 to produce 4-hydroxy-6-(3-pyridinyl)-2H-pyran-2-one (HPPO) which is further prenylated by the polyprenyl transferase pyr6 to yield farnesyl-HPPO . The next steps consist of an epoxidation of farnesyl-HPPO to epoxyfarnesyl-HPPO by FAD-dependent monooxygenase pyr5 and a cyclization of the terpenoid portion by the terpene cyclase pyr4 to yield deacetyl-pyripyropene E . The 2 cytochrome P450 monooxygenases pyr3 and pyr9, and the 2 acetyltransferases pyr7 and pyr8 are involved in the conversion of deacetyl-pyripyropene E into pyripyropene A through several cycles of oxidation and acetylation steps . Pyr7 acetylates deacetyl-pyripyropene E to pyripyropene E which is oxidized to 11-deacetyl-pyripyropene O by pyr3, which is in turn acetylated into pyripyropene O by pyr8 . Pyripyropene O is then oxidized to deacetyl-pyripyropene A by pyr9 . Deacetyl-pyripyropene A is finally acetylated to pyripyropene A by pyr8 .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57847
Sequence Length: 518
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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Q4WLD2 | MDGWSDLSSAPPQYREVAGIADWALLAQGLGWSINYLAMIYHSYKDRTYGMAILPLCCNFAWEFVYSVIYPSHNSAERAVLTTWMILNLFVMYTAIKFAPNEWQHAPLVRQCLPWIFPVAIAAFTAGHLALAATVGVSKAANWGAFLCFELLTSGAVCQLMSRGSSRGASYTIWLSRFLGSYIGGIFLHVRETHWPQEFGWISHPFVTWHGLMCFSLDIAYVTFLWRIRRQEHRSQRKKAL | Function: Terpene cyclase; part of the gene cluster that mediates the biosynthesis of pyripyropene A, a specific human acyl-coenzyme A:cholesterol acyltransferase 2 inhibitor . The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase pyr1 . Nicotinyl-CoA is then a substrate of polyketide synthase pyr2 to produce 4-hydroxy-6-(3-pyridinyl)-2H-pyran-2-one (HPPO) which is further prenylated by the polyprenyl transferase pyr6 to yield farnesyl-HPPO . The next steps consist of an epoxidation of farnesyl-HPPO to epoxyfarnesyl-HPPO by FAD-dependent monooxygenase pyr5 and a cyclization of the terpenoid portion by the terpene cyclase pyr4 to yield deacetyl-pyripyropene E . The 2 cytochrome P450 monooxygenases pyr3 and pyr9, and the 2 acetyltransferases pyr7 and pyr8 are involved in the conversion of deacetyl-pyripyropene E into pyripyropene A through several cycles of oxidation and acetylation steps . Pyr7 acetylates deacetyl-pyripyropene E to pyripyropene E which is oxidized to 11-deacetyl-pyripyropene O by pyr3, which is in turn acetylated into pyripyropene O by pyr8 . Pyripyropene O is then oxidized to deacetyl-pyripyropene A by pyr9 . Deacetyl-pyripyropene A is finally acetylated to pyripyropene A by pyr8 .
Catalytic Activity: 2-oxo-3-[(8S)-epoxy-(2E,6E)-farnesyl]-6-(pyridin-3-yl)-2H-pyran-4-olate + H(+) = deacetylpyripyropene E
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27440
Sequence Length: 241
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 4.2.3.-
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Q4WLD1 | MRVLIIGGSIAGLTLAHCLEKAKIDYVLLEKKEEIAPQEGASIGILPNGGRIMEQLGLYHQIEQLIEPLARAHVTYPDGFHFTSQYPALLQQRFGYPLAFLDRQKLLQILAAGPVQSGRVKLGHQVVNIESTPDGVTVRTSHGHVYQGDLVVGADGVHSRVRAEMWRLATASQGEIFRSEYNKLTIDYACIFGISSPVDQLEPGEQITCYNDGWSILSVIGQNGRVFWFLFIKLDKESVYDGSRKNGPRFSPADARAHCERLAHEPVWNGVKFGHVWAQCEVFQMTPLEEGLFSKWYWRNIVCIGDSMHKFAPHIGQGANCAIEDAAQLSNRLQAWLYGCGPNDPPTASDLSEILAGFVEDRLRRLGPVAVAARSAMRLHARQGVKNWILGRYLLPYAGDKPADWASQGIAGGGVTLDFVEPPERSGPGWVQFSQPRKRPTFPLTVAGLCLVAIVIRMLHSTLTV | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of pyripyropene A, a specific human acyl-coenzyme A:cholesterol acyltransferase 2 inhibitor . The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase pyr1 . Nicotinyl-CoA is then a substrate of polyketide synthase pyr2 to produce 4-hydroxy-6-(3-pyridinyl)-2H-pyran-2-one (HPPO) which is further prenylated by the polyprenyl transferase pyr6 to yield farnesyl-HPPO . The next steps consist of an epoxidation of farnesyl-HPPO to epoxyfarnesyl-HPPO by FAD-dependent monooxygenase pyr5 and a cyclization of the terpenoid portion by the terpene cyclase pyr4 to yield deacetyl-pyripyropene E . The 2 cytochrome P450 monooxygenases pyr3 and pyr9, and the 2 acetyltransferases pyr7 and pyr8 are involved in the conversion of deacetyl-pyripyropene E into pyripyropene A through several cycles of oxidation and acetylation steps . Pyr7 acetylates deacetyl-pyripyropene E to pyripyropene E which is oxidized to 11-deacetyl-pyripyropene O by pyr3, which is in turn acetylated into pyripyropene O by pyr8 . Pyripyropene O is then oxidized to deacetyl-pyripyropene A by pyr9 . Deacetyl-pyripyropene A is finally acetylated to pyripyropene A by pyr8 .
Catalytic Activity: 4-hydroxy-3-[(2E,6E)-farnesyl]-6-(pyridin-3-yl)-2H-pyran-2-one + H(+) + NADPH + O2 = 2-oxo-3-[(8S)-epoxy-(2E,6E)-farnesyl]-6-(pyridin-3-yl)-2H-pyran-4-olate + H2O + NADP(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 51415
Sequence Length: 465
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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Q52453 | MTSSAAAIRLGFEPFVNASPVELRTNWSDSDVQAVISATYRQVFGNEHLMLSERLTSAESLLASGNISVREF | Function: Rod linker protein, associated with phycocyanin. Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 7877
Sequence Length: 72
Subcellular Location: Cellular thylakoid membrane
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Q4WLD0 | MATAQSPTQLVRTLIDVSRFDKYNCLFAIFPGVWSIFLAAASRHADGVHLPSDWVLGRAGLAFAYTYLLSGAGMVWNDWIDRDIDAQVARTKNRPLASGRLATRAAIIWMLVQYAASVWLMDRMLSGQNLWTFMLPLTTGIILYPFGKRPTTRKLGIYPQYILGASSALTILPAWASVYGDSVAPPDLLAKCLPLCVFLFLWTIYFNTAYSYQDVKDDCRLSVNSSYVLAGQYVHGLLLLQAVAVVMVIPWILHENGSAWLWFSWLGVWTAALAEQLYLFDTKDPSTGGRVHRRNFALGIWNVLACFVELLLVSGSLDMF | Function: Polyprenyl transferase; part of the gene cluster that mediates the biosynthesis of pyripyropene A, a specific human acyl-coenzyme A:cholesterol acyltransferase 2 inhibitor . The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase pyr1 . Nicotinyl-CoA is then a substrate of polyketide synthase pyr2 to produce 4-hydroxy-6-(3-pyridinyl)-2H-pyran-2-one (HPPO) which is further prenylated by the polyprenyl transferase pyr6 to yield farnesyl-HPPO . The next steps consist of an epoxidation of farnesyl-HPPO to epoxyfarnesyl-HPPO by FAD-dependent monooxygenase pyr5 and a cyclization of the terpenoid portion by the terpene cyclase pyr4 to yield deacetyl-pyripyropene E . The 2 cytochrome P450 monooxygenases pyr3 and pyr9, and the 2 acetyltransferases pyr7 and pyr8 are involved in the conversion of deacetyl-pyripyropene E into pyripyropene A through several cycles of oxidation and acetylation steps . Pyr7 acetylates deacetyl-pyripyropene E to pyripyropene E which is oxidized to 11-deacetyl-pyripyropene O by pyr3, which is in turn acetylated into pyripyropene O by pyr8 . Pyripyropene O is then oxidized to deacetyl-pyripyropene A by pyr9 . Deacetyl-pyripyropene A is finally acetylated to pyripyropene A by pyr8 .
Catalytic Activity: (2E,6E)-farnesyl diphosphate + 4-hydroxy-6-(pyridin-3-yl)-2H-pyran-2-one = 4-hydroxy-3-[(2E,6E)-farnesyl]-6-(pyridin-3-yl)-2H-pyran-2-one + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35777
Sequence Length: 320
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 2.5.1.-
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Q4WLC9 | MSVQTTYSPVNQDEQVHDGLASRHVSCEGAPSDDSPYALSSLDHNPLGINVSFLLCFHAAQPEEGIRVLEDGINQLLKAHPFLAGDVTRPTRLSQRTNTMQIEPDAPESLLKIPMLQIRHHPATSIEELESKRLLPGAEEQEIIRQLAPLPIDMDLSLPQRPVLRFQANIMRDGVILAMTFHHAAMDGAGAARVLGLLADYCRDPAAPSVGVIPDRQLRSQIDRLATGCSPSASRADFSQHYCGLGDWAALLAENWPGFLQARATELVTWRLTIPGFKVQYLKGACNALLQGQTSALAGGTLTPTILSNNDIVSALMAMILRQAGQLAGKSTELSIAVDMRPSFHAPAFNNYLGNMVLLTYTPIPAAKDQAPVDGPRPPTELRQEDLEELTGIAARIRQSLLKVDAEYIQGVLSHLHSQTDWANIGFRGVPIPLSSFRNFEMIGLDFGETLGSQPRGFQLHLPVLGGMCFVLPKRQDRTEPWDLHLTLHRDDVSRIANDPLFRWAAGEHF | Function: O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of pyripyropene A, a specific human acyl-coenzyme A:cholesterol acyltransferase 2 inhibitor . The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase pyr1 . Nicotinyl-CoA is then a substrate of polyketide synthase pyr2 to produce 4-hydroxy-6-(3-pyridinyl)-2H-pyran-2-one (HPPO) which is further prenylated by the polyprenyl transferase pyr6 to yield farnesyl-HPPO . The next steps consist of an epoxidation of farnesyl-HPPO to epoxyfarnesyl-HPPO by FAD-dependent monooxygenase pyr5 and a cyclization of the terpenoid portion by the terpene cyclase pyr4 to yield deacetyl-pyripyropene E . The 2 cytochrome P450 monooxygenases pyr3 and pyr9, and the 2 acetyltransferases pyr7 and pyr8 are involved in the conversion of deacetyl-pyripyropene E into pyripyropene A through several cycles of oxidation and acetylation steps . Pyr7 acetylates deacetyl-pyripyropene E to pyripyropene E which is oxidized to 11-deacetyl-pyripyropene O by pyr3, which is in turn acetylated into pyripyropene O by pyr8 . Pyripyropene O is then oxidized to deacetyl-pyripyropene A by pyr9 . Deacetyl-pyripyropene A is finally acetylated to pyripyropene A by pyr8 .
Sequence Mass (Da): 55983
Sequence Length: 510
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 2.3.1.-
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Q4WLC8 | MDLVPSSTLWSIAQELALYLAFTVPTAFVIITTPKSSFLRLAWTPCLLYILYRFSLQVPSLTTSQFLNGVAAGQATVAALQCLNLLLITKLDERELVHAGLCIPSSSLLVRVACAWALLVNFRGIGTVWEVKNVPQHAAYLQKPKQHRLSRRRYVLRESAIIIWQYLLLDLIHMSTKDTPPGDLARLFGPGLEYRYLDATAEQWFGRVSVGIFSWLVPSRVCLNIVSRIYCLVLVVLRISAPESCRPSFGRVRDACTIRGFWGKFWHQSFRWPLTSVGSFVARDVLRLPRPSLLERYTNIFFTFFTSAVLHLACDAILGIPPSGSGAMPFFCVVPLAIMFEDGVQEVWRRVTGPSQGAVPFWQRLVGFLWVGSWMYATSPWYLYPAARQPPERTWMVPVSVVGEIGLRVAQKVLLVYGVVLYWAIGGEI | Function: Acetyltransferase; part of the gene cluster that mediates the biosynthesis of pyripyropene A, a specific human acyl-coenzyme A:cholesterol acyltransferase 2 inhibitor . The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase pyr1 . Nicotinyl-CoA is then a substrate of polyketide synthase pyr2 to produce 4-hydroxy-6-(3-pyridinyl)-2H-pyran-2-one (HPPO) which is further prenylated by the polyprenyl transferase pyr6 to yield farnesyl-HPPO . The next steps consist of an epoxidation of farnesyl-HPPO to epoxyfarnesyl-HPPO by FAD-dependent monooxygenase pyr5 and a cyclization of the terpenoid portion by the terpene cyclase pyr4 to yield deacetyl-pyripyropene E . The 2 cytochrome P450 monooxygenases pyr3 and pyr9, and the 2 acetyltransferases pyr7 and pyr8 are involved in the conversion of deacetyl-pyripyropene E into pyripyropene A through several cycles of oxidation and acetylation steps . Pyr7 acetylates deacetyl-pyripyropene E to pyripyropene E which is oxidized to 11-deacetyl-pyripyropene O by pyr3, which is in turn acetylated into pyripyropene O by pyr8 . Pyripyropene O is then oxidized to deacetyl-pyripyropene A by pyr9 . Deacetyl-pyripyropene A is finally acetylated to pyripyropene A by pyr8 .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48320
Sequence Length: 429
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 2.3.1.-
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A4D9R3 | MIRVEDASIGTVWVTCLLAVGLYFIRSRLLSDQFAGFPSVNSRKPWEVLNVFAHRRFQQNGPEYLKAGFAKSPVFGVVTDLGPKLVVSGAFIEDFKDEKLLDHYRAMVEDFMAEVPGFESMFLGNLHNTVLRDVISVITRELDQFTLPLSDEVSTALGDTWSDSPDWTEVTLLPSMLGLIARVSSLIFVGEPLCRDPAWLETVVNFTIVRHQAILALHMCPAVLRPVLHWFLPPCQKLRREIKTARSLINSALEELRKNPPTDRFSSLAWVDAFASGKKYDATMVQLRLANASIHSSADLLAKVLINLCEQPGLIQDLRDEVISVLEENGWRASTLNQLKLLDSVLKESQRLHPITTGTFSRFTRQNIKLTNGTEIPTGTPVMVTNDVAGDAAIYPDPEVFDGYRYLRMREGADKARAPFTTTGQNHLGFGYGKYACPGRFFAATEIKIALCHMLLKYEWRLVKDSPHDMLTSGFASFRDPRARIEVRRRAPDPQEVVLTIK | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of pyripyropene A, a specific human acyl-coenzyme A:cholesterol acyltransferase 2 inhibitor . The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase pyr1 . Nicotinyl-CoA is then a substrate of polyketide synthase pyr2 to produce 4-hydroxy-6-(3-pyridinyl)-2H-pyran-2-one (HPPO) which is further prenylated by the polyprenyl transferase pyr6 to yield farnesyl-HPPO . The next steps consist of an epoxidation of farnesyl-HPPO to epoxyfarnesyl-HPPO by FAD-dependent monooxygenase pyr5 and a cyclization of the terpenoid portion by the terpene cyclase pyr4 to yield deacetyl-pyripyropene E . The 2 cytochrome P450 monooxygenases pyr3 and pyr9, and the 2 acetyltransferases pyr7 and pyr8 are involved in the conversion of deacetyl-pyripyropene E into pyripyropene A through several cycles of oxidation and acetylation steps . Pyr7 acetylates deacetyl-pyripyropene E to pyripyropene E which is oxidized to 11-deacetyl-pyripyropene O by pyr3, which is in turn acetylated into pyripyropene O by pyr8 . Pyripyropene O is then oxidized to deacetyl-pyripyropene A by pyr9 . Deacetyl-pyripyropene A is finally acetylated to pyripyropene A by pyr8 .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 56439
Sequence Length: 502
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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Q43086 | MTVASMLSSNSMNVGVSNPKMSSKTSACCLLNRPWPSSCSMSISSCGQFGVSEKSKLLCGAGALQVESAPLFSVGQKFQLDDVIEAQQFDRETLSAIFEVARSMENIRGNSSGSQMLKGYLMATLFYEPSTRTRLSFESAMKRLGGDVLTTENAREFSSAAKGETLEDTIRTVEGYSDIIVLRHFESGAARRAAATANIPVINAGDGPGQHPSQALLDVYTIEREIGKLDGIKVGLVGDLANGRTVRSLAYLLAKYRDVKLYFVSPNVVKMKDDIKEYLTSKGVEWEESSDLMEVASKCDVVYQTRIQKERFGEKLNLYEEARGKYIVNQDVLKVMQNHAVVMHPLPKLDEIEADVDNDPRAAYFRQAKNGLYIRMALLKVLLLGW | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 42618
Sequence Length: 386
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
Subcellular Location: Plastid
EC: 2.1.3.2
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Q43064 | MTASSSLFSCSMHMEVLTPKISKWPKDFVSCHSKISYVETNYLKSTCYPISRFLCINNLSKCDKMIKTRQRDGIHCFSEGQKFQLDDVIEAQQFDRDILNAIFEIARDMENIERNSPESQILKGYLMATLFYEPSTRTRLSFESAMRRLGGEVLTTENAREFSSAAKGETLEDTIRTVEGYSDLIVLRHFESGAARRAAAIAGIPIVNAGDGPGQHPSQALLDVYTIEREIGKLDGIKVGLVGDLANGRTVRSLAYLLAKYKDVKIYFVSPEVVKMKDDIKDYLTSKGVDWEESSDLVEVASECDVVYQTRIQKERFGERLDLYEKARGKFIVNQNILNAMQRHAVIMHPLPRLDEITVDVDADPRAAYFRQAKYGLYIRMALLKLLLVGW | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 44344
Sequence Length: 391
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
Subcellular Location: Plastid
EC: 2.1.3.2
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A3DE08 | MILKSKDLLGLKDLTAEEIQYILNTAKTMKVILLSKNKKAPHLQGKSIITLFYENSTRTRLSFELASKYLSANAANISVAASSVAKGETLIDTGKTIDMMGADVIVIRHSMSGAPHLLARNVKASVINAGDGMNEHPTQALLDMFTIIEKKGSLKGLKVAIIGDIYHSRVARSNIWGMTKLGAEVSVAGPSTLMPPELDKTGVKVFTTVQEALIDADVVMGLRIQKERQKSGLFPSLREYSRFFGLDEKRLKLAKEDALILHPGPVNRGVELPSSVIDSERSFINEQVTNGVAVRMALLYLLTRRDSGESVN | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 34076
Sequence Length: 312
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
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P05654 | MKHLTTMSELSTEEIKDLLQTAQELKSGKTDNQLTGKFAANLFFEPSTRTRFSFEVAEKKLGMNVLNLDGTSTSVQKGETLYDTIRTLESIGVDVCVIRHSEDEYYEELVSQVNIPILNAGDGCGQHPTQSLLDLMTIYEEFNTFKGLTVSIHGDIKHSRVARSNAEVLTRLGARVLFSGPSEWQDEENTFGTYVSMDEAVESSDVVMLLRIQNERHQSAVSQEGYLNKYGLTVERAERMKRHAIIMHPAPVNRGVEIDDSLVESEKSRIFKQMKNGVFIRMAVIQRALQTNVKRGEAAYVISH | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 34224
Sequence Length: 304
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
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Q8A9S3 | MENRSLVTIAEHSKEKILYMLEMAKQFEMNPNRRLLQGKVVATLFFEPSTRTRLSFETAANRLGARVIGFTDPKATSSSKGETLKDTIMMVSSYADIIVMRHYLEGAARYASEVAPVPIVNAGDGANQHPSQTMLDLYSIYKTQGTLENLNIFLVGDLKYGRTVHSLLMAMRHFNPTFHFIAPDELKMPEEYKLYCKEHQIKYIEHTEFTEEIIADADILYMTRVQRERFTDLMEYERVKNVYILRNKMLENTRPNLRILHPLPRVNEIAYDVDNNPKAYYFQQAQNGLYAREAILCDVLGITLEDVKNDILL | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 36188
Sequence Length: 313
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
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C5C683 | MRHLLSAADLGRDEAVALLDTAETMADTQSRAIKKLPPLRGLTVVNLFFEDSTRTRISFEAAAKRLSADVINFSAKGSSVSKGESLKDTAQTLQAMGADAVVVRHWASGAPHRLAHAGWIAAPVINAGDGTHQHPTQALLDAFTLRRRLAGPDGPIGTDLAGRHVVVVGDVLHSRVARSNVDLLSTLGARVTLVAPPTLLPVGVESWPCEVGYDLDAAIDAGPDAVMMLRVQRERMSSGFFPSEREYARAYGLDAARVSRLGKHALVMHPGPMNRGLEISADAADSARSTVVEQVTNGVSVRMAVLYTLLAGGPDGDSTTSPGSGPEGGTTP | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 34907
Sequence Length: 332
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
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A1A1F7 | MVGKSVITLDDLSIRQIQEMLHKAQYIDSHRKEVAHTCEGRVLATLFYEPSTRTRLSFETAMLRLGGKVIGFAGAQLASVTKGETIADTLKTVSNYVDVVAIRHPKEGAALVASRAASVPVINAGDGGHMHPTQTLADLATLQSRFGRVTNLTVGLCGDLTFGRTVHSLIETLCRFGNVNFVLISPDELKTPQYVLDRINATESCSYTEVKDLVSVIGDLDVLYMTRVQKERFFNEDDYLRLRDTYILDEAKMAYAKKDMAVLHPLPRVNEIAVEVDDDPRAAYFEQVKNGMLMRMALESSVVGDELPGYEPLAAKEVEA | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 35386
Sequence Length: 320
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
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Q9HKM2 | MLKNRSVVSIEDVDIDDLNDLFDLSDSMLKTIEKGGSTDLLRNRIMATLFYEPSTRTRLSFESAMHRLGGSVITVSDVKTSSVAKGETLADTIRMASSYSDIIVIRHPLEGAARLASKFANKPVINAGDGSGQHPTQTILDLYTIKRETGSIDGKTITMVGDLRYGRTIHSLIIALSRFDVRINLVSPQILKLPEYVLTKIGDRSRIMEYDDLSKVIEDTDVLYVTRIQKERFSDQNEYQSVIGSYSVDRDLVSRMKKDAIIMHPLPRIDEIKPEVDELPQARYFKQAYYGVPVRMALIYRILGD | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 34398
Sequence Length: 305
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
|
Q5JHM9 | MDWKGRDVISIRDFSKEDIEFVLKVAERLEEELNEKGSLDYARGKILATLFFEPSTRTRLSFESAMHRLGGSVIGFSSASSTSVKKGESLADTIKTVEQYSDVIVIRHPMEGAARLAAEVAGIPVINAGDGSNQHPTQTLLDLYTIKKAFGKIDGLTIGLLGDLKYGRTVHSLAEALAFYDVELYLISPELLRMPKHIVDELRERGVKVYETTDLEGAIPKLDVLYVTRIQRERFPDEEEYLKVKGSYQVNLEVLKNAKETLKVMHPLPRVDEIHPEVDKTKHALYFRQVFSGVPVRMALLGLTLGVLGV | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 34701
Sequence Length: 310
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
|
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