ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P38025 | MAQCVRSTLNPVRTPQSFTRKAYVKSPAFASVSFLRAVPEFNKYPKPCSLVMSCQGKAQNQQEERPQLSLDDLVTSNRKGEVLGTIKDSLSNCLSETNLLATVPGLKSRIKGKVRDIYDAGDYLVLITTDRLSAFDRNLASIPFKGQVLNETSLWWFNNTQHITPNAIVSSPDRNVVIAKKCSVFPIEFVVRGYVTGSTDTSLWTVYNKGVRNYCGNELSDGLVKNQKLPANILTPTTKAADHDVPISPNEIVEGGFMTQAEFDEASMKALSLFEFGQGVAKKHGLILVDTKYEFGRSSDGSILLIDEIHTPDSSRYWLA... | 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-ami... |
O28996 | MGSVKDLVVLKEPAEKPGLGRFIFSNRYSVFDYGEMPDKIEDKGRALCMVTAYFFEKLEEAGIATHYLGLVEGGKVRRFDEVENAVNEMEVKLVRVIKPKNGDYSIFKTLKGNFLVPLEIIYRNSIPEGSSLLRRIERGEAKPEDFGLTKIEAGMRLERPIVDFSTKLEDVDRYLSHSEAKEISGLSDEEFEALKELVVKVDEIITREVSKAGLINEDGKIEVALDDERNLMVVDAVGTPDECRFSFDGFEVSKELLREYYRKTEWYDKVRQLKGQEGWREAVGLPPPLPDEVREGVSNLYRAFCNEVTGRKFFDAPKLK... | 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-ami... |
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-ami... |
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-ami... |
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-ami... |
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-ami... |
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-ami... |
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-ami... |
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-ami... |
O67775 | MRAIISVYRKEGIDKLAKALQELGYEIVSTGGTAKYLREKGISVKEVSEITGFPEILEGRVKTLHPVVHGGILFRDWVEKDKEEIEKHGIKPIDVVVVNLYPFEEKLKEGLTDKDLMEFIDIGGPTLIRAAAKNFFRVVILVDPEDYDWVIEKLKKGNLTLQDRAYLAWKAFSHTAYYDGVISQAFKKLYSIDTFGKEEALPLKRMQKLRYGENPHQRGFLYENPLEDIGITKAQVLQGKEMSFNNYLDADSAVRLVAEFPNQTVCAIIKHNNPCGVALGSSVKEAFLRAKEADPVSAFGGIVAFNDKVDGETAKELTSM... | 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 r... |
Q81IP9 | MKKRALVSVSDKTGVVEFVKGLLEQGIEVISTGGTKKLLEENGLQVIGISEVTGFPEIMDGRVKTLHPNIHGGLLAVRDNETHVTQMNELGMEPIDFVVVNLYPFKETIAKPDVTFADAIENIDIGGPTMIRSAAKNHKFVSVIVDPVDYDIVLAELKENGEVAEETKRKLAAKVFRHTAAYDALISNYLTEQMGEESPETLTVTFEKKQDLRYGENPHQKATFYKAPFAATSSVAYAEQLHGKELSYNNINDADAALSIVKEFTEPAVVAVKHMNPCGVGVGTDIHEAYTRAYEADPVSIFGGIIAANREIDKATAEKL... | 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 r... |
Q8X611 | MQQRRPVRRALLSVSDKAGIVEFAQALSARGVELLSTGGTARLLAEKGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRRGQDDAIMEEHQIQPIDMVVVNLYPFAQTVAREGCSLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYDAIIKEMDDNEGSLTLATRFDLAIKAFEHTAAYDSMIANYFGSMVPAYHGESKEAAGRFPRTLNLNFIKKQDMRYGENSHQQAAFYIEENVKEASVATATQVQGKALSYNNIADTDAALECVKEFAEPACVIVKHANPCGVAIGNSILDAYDRAYKTDPTSAFGGII... | 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 r... |
B2KCF7 | MTQERKIKRALISVSDKTGLEVFAKGLHKLGVELVSTSGTAKFLKAAGLPVRDLSDLTGFPEILDGRVKTLHPRVHGAILYKRDDDAHCKVIKDMGIEDIDMLVVNLYPFRETAAKAKHSFDAEVIENIDIGGPSMLRSAAKNFAHVAVLCRPKDYEVVLSEMAASQGALSYATRQRLCVEAFTHTAEYDAAISEEFKKGLNHEFPESKIVVLHKTQDLRYGENPHQKAVLYSQKKDFSFEQLHGKELSYNNILDAFGTWDAVCDFDLPACVIFKHVTPCGIGTGKVLTEAFNNAWACDPKSAFGGIIALNKPMQRDIAE... | 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 r... |
O74928 | MYALLSVYDKTGLLELAKALTSKGVKLLGSGGTAKMIRESGMEVADVSSITNAPEILGGRVKTLHPAVHGGILARDIPSDEKDLVEQSIEKIDIVVCNLYPFRETIAKPNVTIPEAVEEIDIGGVTLLRAAAKNHARVTILSDPADYATFTDKFLSDKLTQDDRNTYALKAFASTASYDAAITDYFRKQYAAGVDQLTLRYGANPHQSPAQAFMEQGPLPFKVLCGSPGYINLMDALNSWPLVKELRENIGIPAAASFKHVSPAGAAVGLPLSDVEKKVYFVSDITEFTPLACAYARARGADRMSSFGDFIALSDTVDVC... | 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 FAI... |
Q8EJM1 | MTVANHARPIRRALLSVSDKTGILEFAKALHAQGVELLSTGGTARLLADNGVPVIEVSDYTGHPEIMDGRVKTLHPKVHGGILARRGLDENVMAANNINAIDLVAVNLYPFADTVAKAGCTLEDAIENIDIGGPTMVRAAAKNHKDVTIVVNAADYNRVLAEMAVNNGSTTHATRFDLAIAAFEHTAGYDGMIANYFGTMVPMHRVPAHSTDECFQDSLSVEGSKFPRTFNTQLVKKQDLRYGENSHQAAAFYVDTKIDEASVATAVQLQGKALSYNNIADTDAALECVKEFSEPACVIVKHANPCGVALGKDLLDAYNR... | 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 r... |
Q3IIQ6 | MPSIVVVGANWGDEGKGRIVDFLAENASASIRFQGGNNAGHTVVNDFGTFKLHQLPSGIFNPDCIAVLGPGMVISPSALSEEIAEVKAAGVNVKLCISDRATLCLPLHALEDTLEELRLGDAAYGSTRQGISPAYGDRVMKKGILVGWLNQPDVLLERIQFMLDWKMPQLKALYPSCDFSQTAEEMTQWLLDVTAPWRAFICNVTEPLKALQKQNANLLFEAQLGAGRDLVYGEYPYTTSSNVTAAYAGIGSGLPALRPERVVAVAKSFSSSVGTGTLVTAMEEQDNFRESANEYGAVTGRPRDMGYFDAVATRNGVELQ... | 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 Ma... |
A3DK09 | MATRVVVGTQWGDEGKGKYIDMLAKDSDMVVRFSGGNNAGHTIVANGVKYALHLIPSGILNEGKTCIIGNGVVVDPAVLLKEIKELNEKGISTDRLLISDRAHVIMPYHKLLDELQEKFRGENSIGTTKRGIGPCYSDKTERSGIRMCDLVDEDEFVRKVRENLKVKNLIIEKVYGGQKLDEEQVISEYLEYGRKLKEYVADVNSIIFEAIEQGKNILFEGAQATFLDLDFGTYPYVTSSNPVAGGVCTGAGVGPVFINEVYGVLKAYTSRVGAGPFPTEQNNEIGDRIRELGWEYGTTTGRPRRCGWLDLVMIKYAARV... | 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 Ma... |
Q6AN65 | MSSVVVVGAQWGDEGKGKIVDLLTKYSDYIVRFQGGNNAGHTLVVDGKKFVFHIIPSGILYEEKTCMIGNGVILDPGVLLEEMASLKERGLEVKPNRLMISDNAHLIMPYHSQLDQAKESALSASNKIGTTGRGIGPCYMDKVGRVGIKAGDLLDEDLFREKLRCAIEEKNFILTKKFGAPAVDFDSVYRQFMDFAEQLSPYFGNVSVTLDEARRADKNILFEGAQGTQLDIDHGTYPFVTSSNTVAGNACAGSGFGPSHIDAVVGIVKAYTTRVGSGPFPTELFDEKGEELQNKGSEFGATTGRRRRCGWFDGVVANDA... | 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 Ma... |
A4J9P7 | MSTVVIIGAQWGDEGKGKITDFLAEKAEIIVRYQGGNNAGHTVVVDDAEFKLHLIPSGILHPEKLCVIGNGVVIDPQVLKQELDSLAERGVKTGRLCVSQRSHIIMPYHRKMDAVEEEQKGEGKIGTTKRGIGPTYTDKASRVGIRVVDLIDKEEFPKLLKNNIECKNEIFEKLYNTKGFEYEEVLKEYQGYAEMLEPMTEDVSVLVHNAIKEGKNVLFEGAQGTLLDLDHGTYPYVTSSHPTAAAACLGSGVGPTKINRALGIVKAYTTRVGEGPFPTELNDGLGEEIRKNGNEYGTTTGRPRRCGWFDAVIVRYAARI... | 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 Ma... |
A1V9U1 | MSNVVVMGAQWGDEGKGKIVDLLTRESDVIVRFQGGNNAGHTVLVGEKQYILHLIPSGILHEGKKCLIGNGVVLDPEVFCREIDSLRAQGVDMSPARLMISRKTHLIMPYHKVLDQAREAHKCKDAKIGTTGRGIGPCYEDKSARIGVRAADLAMPELLRSKIEAALVEKNALFTGLYGQQPLDADAVFEEVMAHGAKLVPYLADVSSEIHDAWAEGRSVLFEGAQGTHLDIDHGTYPFVTSSNTVSGNAAAGSGVPPTKLDRIIAIVKAYTTRVGAGPFPTELDDATGEYLQQKGHEFGATTGRKRRCGWLDAVVLRES... | 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 Ma... |
P21900 | MASIIIGSQWGDEGKGKLVDILSQQFDVVARCQGGANAGHTIVVDGKKIALHLIPSGILNEKASCILGNGMVIHLPTFFKEVQGLQDKGINYKGRLFVSDRAHLVFDLHQMIDAMKEAELSNGTSNDSIGTTKRGIGPCYSSKASRGGLRVCDLYSPEHFRKTFTRLVENKHKRFGSFEYDVEAELKRYQEFAEMLKPFVIDSVYYLNQAFKDGKKVLIEGAQSTMLDLDFGCYPYVTSSASSVGGACTGLGISPNKVVTQIGVVKAYTTKVGSGPFPTEQNDHVGDSLRKAGSEFGTTTGRPRRIGWLDAVVLRYTSMI... | 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-... |
Q9Y0Y2 | MSASATNGTHYEQLHQGRTKMYKSKVDVVLGAQWGDEGKGKVVDMLASDVDIVCRCQGGNNAGHTVVANGTEFDFHLLPSGVVNEKCVSVIGNGVVIHLPSLFDEVLKNEAKGLQHLENRLIISDRAHLVFDFHQHVDGMQEAEKGGKSLGTTKKGIGPAYSSKATRNGIRVGELLGDFNLFSEKFKSIVATHVRLFPSINVDVEAELARYKDYADKVRPYVKDTICFLHTALRNGKTILVEGANAAMLDIDFGTYPYVTSSNCSIGGVLTGLGLPPQTIGEVIGVVKAYTTRVGDGPFPTEQLNDIGDLLQTRGFEVGV... | 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: ... |
Q6F243 | MREINSLVVVGSQWGDEGKGKMTDYFAQKADVVVRFAGGDNAGHVINFNGQKHKVTIIPSGIFNSEVTSVIGNGCAVNLINLVKELETIKNSGVKLGKLLISDRAQLILPYHILIDGAQEESRGARKIGTTKRGIGPTYQDKAARLGIRVADIEEEDFKETFKEIFEYQMMFLDRMFNVESIDFEETYANLINAYNVIKDCVTDTGIFVEQAIKNGKKVLFEGAQGALLDIDHGTYPYVTSSNTSANNASTGTGISHKLINNTLGVVKAYSTRVGAGAFPTELLNEVGDGIRERGHEYGSNTKRPRRVGWLDLVALKHAI... | 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 Ma... |
Q9U8D3 | MNIFDHQIKNVDKGNVVAILGAQWGDEGKGKIIDMLSEYSDITCRFNGGANAGHTISVNDKKYALHLLPCGVLYDNNISVLGNGMVIHVKSLMEEIESVGGKLLDRLYLSNKAHILFDIHQIIDSIQETKKLKEGKQIGTTKRGIGPCYSTKASRIGIRLGTLKNFENFKNMYSKLIDHLMDLYNITEYDKEKELNLFYNYHIKLRDRIVDVISFMNTNLENNKKVLIEGANAAMLDIDFGTYPYVTSSCTTVGGVFSGLGIHHKKLNLVVGVVKSYLTRVGCGPFLTELNNDVGQYLREKGHEYGTTTKRPRRCGWLDI... | 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 + phos... |
B2AWF0 | MPTTIILGSQWGDEGKGKLSDILCQKAQICARAAGGHNAGHSVVANGVSYDFHLLPSGLINPNCENLIGSGVVVNVEAFFKELNALEEKGLKHVREKILISDRAHVNLTLHAAVDRAEEAQLEGNKKIGTTGRGIGPSYATKASRKGIRVHEIFKEAVFEKKLRTLAEGYKKQFGELFEYDVEEEIARFREYRKLLPNFVCDGPNFIDQAQKSGRDLLIEGANALMLDIDYGTYPYVTSSNTGFGGAVTGLALDYKQIKEVIGVVKAYTTRVGGGPFKTEDLGDAGTKLQEIGREWGVSTGRRRRCGWLDLVVLKYSQLI... | 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-... |
B9IJ21 | MNLSSLRLESNPRWSYHAAHFPAHHGLNPSFRRNFVSCSSIKPSASSSLSVAESFTRDSASRIESLSQVSGVLGSQWGDEGKGKLVDILAEHFDIVARCQGGANAGHTIYNSEGKKFALHLVPSGILNEDTLCVIGNGVVVHLPGLFKEIDGLEANGVSCTGRILVSDRAHLLFDFHQEVDGLREAELAKSFIGTTRRGIGPCYSSKVIRNGIRVCDLRHMDTFPQKLDALLSDVASRFESFKYGPEMLKEEVERYKRFAERLEPFITDTVHFMNESIAKKKKILVEGGQATMLDIDFGTYPFVTSSSPSAGGICTGLGI... | 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-... |
Q7MWW8 | MEKVDVLLGLQWGDEGKGKIVDVLTPHYDIVARFQGGPNAGHTLEFNGEKYVLRSIPSGIFQGEKTNVIGNGVVLDPLLFKEEAEALARSGHDLTKRLVISRKAHLIMPTHRLLDAANEMAKGSGKIGTTGKGIGPTYTDKVSRNGLRVGDLEHGFEEAYSVAKERHLRILNSLNYPTDKLADLEERWMEATKYLRKFEFVDSEFLINGALLSGKKVLAEGAQGSLLDIDFGSYPFVTSSNTICAGCCTGLGVAPRNVGDVYGIFKAYCTRVGAGPFPTELFDETGDKLCELGREFGSVTGRKRRCGWIDLVALRYTIML... | 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 Ma... |
Q386E7 | MAAAPSATAPKHNYTLGTNASQLELYKYLKTVPPIPELRQAVTIKKYEEASVDDTLYPLIDEHQIIMVVGAFFGDEGKGKTVDAVARHPACTCVARVNSGENAGHTVFDDIGRKYVFNLAPSSLLTPNTRNYVSSECVMDPISFMEREIGQFIKSNMPYKDKLFVGNVFVVTPYHKLLDLLGSAPNSSTLKGMSPIHASKVTKRGIRLDHIFNDEGVLRARLAKDMDTYYGLLKVKGLTDKDVVRRCQEENADGVERVPGYVVDFARAENKIDYLVKLYTERVKNNKDFPRRCDVTHELRAALARGEKLLLEGPQSYWLS... | 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 + phos... |
Q4P7R2 | MAAMPKPSDSKTGGKATVLLGSQWGDEGKGKLADVLSGQMDVCARCAGGNNAGHTIVADVNGVKTKFDFHLLPSGLVNPRCAGFIGSGVVVHVPSFFAELDTIQKKGLNCDGRLFISDRAHLVFDFHQVVDGLKEVELGGSSIGTTKKGIGPAYSSKASRSGLRVHHLYDPELFATKFRKLVEGRFKRYGHFEYDTEGEIARYRAFAERLRPHIVDGVTFIHTALAQNRKVLVEGANALFLDIDFGTYPFVTSSSTSIGGVLTGLGIPPTAIGDVIGVMKAYTTRVGMGPFPTELHEEIGHHLQEVGAEYGVTTGRRRRC... | 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-... |
A7TID0 | MVNVVLGSQWGDEGKGKLVDLLVGKYDIVARCAGGNNAGHTIVVNGIKYDFHMLPSGLVNPNCSNLLGNGVVIHVPSLFSELNNLSEKGLKDCDKRLFISSRAHIVFDFHQHTDKLRELELKGISKDGKNIGTTGKGIGPTYSTKASRSGLRVHHLVNDQPGAWEEFEAKYRRLLKTRRERYGDFEYDPEEELNRYKKYKELLKPMVVDSVFFINNAIANGKKILVEGANALMLDIDFGTYPFVTSSSTGIGGVITGLGVSPRHINEVYGVVKAYTTRVGEGPFPTEQLNEQGEKLQTIGAEFGVTTGRKRRCGWLDLVV... | 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-... |
P40607 | MGNNVVVLGTQWGDEGKGKIVDLLTEDAKYVVRYQGGHNAGHTLVIDGEKTVLHLIPSGILRDNVKCVIGNGVVLSPEALLKEMKPLEERGIPVRERLFISEACPLILPYHVAMDQAREIARGKKAIGTTGRGIGPAYEDKVARRGLRVGDLFDMEAFAEKLKEVMEYHNFQLVNFYKAEPVSYEAVLEEAKGYAELLTSMVIDVTDELDAARKRGDKIMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVAAGSGFGPRHIGYILGIAKAYCTRVGAGPFPTELYDGLEKQDPVGKHLGTVGHEFGATTGRLRRTGWFDAV... | 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 Ma... |
O24396 | AAAAAGRGRSFSPAAPAPSSVRLPGRQAPAPAAASALAVEADPAADRVSSLSQVSGVLGSQWGDEGKGKLVDVLAPRFDIVARCQGGANAGHTIYNSEGKKFALHLVPSGILHEGTLCVVGNGAVIHVPGFFGEIDGLQSNGVSCDGRILVSDRAHLLFDLHQTVDGLREAELANSFIGTTKRGIGPCYSSKVTRNGLRVCDLRHMDTFGDKLDVLFEDAAARFEGFKYSKGMLKEEVERYKRFAERLEPFIADTVHVLNESIRQKKKILVEGGQATMLDIDFGTYPFVTSSSPSAGGICTGLGIAPRVIGDLIGVVKAY... | 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-... |
Q8D322 | MKKNIIVLGAQWGDEGKGKVIDFLSKNINYVVRCQGGNNAGHTVVIKEEKTVLHLLPSSILNKNTINIISSGVVISPIDLVKEINMIEKKGISIKNRILISELCPLVLKYHVSMDVAREKNRKKKEIDSIGTTHRGIGPAYEDKIARRALRIHHLINKDKFKKKLKNIVEYYNFQLINYYKEQPVNHEKIFNELINKSKLLNNISIDIPSYLNSINKKNKSIIFEGAQGALLDIDYGTYPYVTSSNTTVGGIISSTGISPFSIKYILGIIKAYSTRVGNGPFPTEIFDETKNIILEKGKEFGSTTGRKRRIGWFDAVAVK... | 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 Ma... |
Q2J4M9 | MTGNPAAPAATSVSPPAEQPYQELGLTDDEYARIIATLGRRPSDAELAMYSVMWSEHCSYKSSKVHLRQFRDTPLTDRLLVGMGENAGVVDVGEGLAVTFKIESHNHPSFVEPYQGAATGVGGIVRDILTMGARPIGVLDPLRFGEADAADTARVLPGVVAGIGGYGNCLGLPTIGGEVVFDPTYAGNPLVNALCVGVMPVDRVQTSAATGVGNAVVLLGAKTGRDGIGGVSILASATFDEGGGPARRPSVQVGDPFTEKILIETCLELFDRKLVTGIQDLGGAGLTCALTETTAAGIATGQPGGMEVDLDLVPLREASM... | 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 o... |
Q7NIR9 | MTAPTESSPFSPADLARHRLSPQEYRRITELIGRHPNLNELGMFSVMWSEHCCYKNSRPLLKGFPTTGPRVLVGPGENAGVIDIGDGLRVAFKIESHNHPSAVEPFQGAATGVGGILRDIFTMGARPIASLNSLRFGPLEDARNRALFRGVVHGIGHYGNCVGVPTVGGEVYFDPTYSGNPLVNAMAIGVLETPEIVRSGAAGIGNPVLYVGSTTGRDGMGGASFASAELSDASQKDRPAVQVGDPFTEKSLIEACLEAFRTGAVVAAQDMGAAGLTCSSSEMAAKGGVGIEMDLDLVPVRETGMVPYEFLLSESQERML... | 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 o... |
A8ABX6 | MPLTEEELKLIEETLGRKPNQVELAMFEAQWSEHCSYKSSRKHLRKLKMDSPWVVKGGDAAVVDFGSVYVAFRIESHNHPSAVDPYNGAATGVGGIIRDILSSGAKPIALLDDLIFGDLDENLVKWHVKGVVKGISDYGNRVGVPTVGGETWFDPDFTRNPMVSVACVGVCPKDKLINGTPRPGDLIVIAGNYTGKDGLLGSSFASKNLEEGVEEEYAAIQVPDPLMEKLLIDSILEMRDERLLVFVKDLGGGGLATALSEVAASFGLGVEARLDALHLREPMEAWEIVVSESQERMMLVIRPEDLERAKKVLEKYDVPY... | 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 o... |
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. Al... |
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. Al... |
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. Al... |
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. Al... |
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. Al... |
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 . ... |
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 hypoxan... |
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. Al... |
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. Al... |
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. Al... |
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. Al... |
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. Al... |
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 o... |
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 o... |
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 o... |
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 o... |
Q0W4L8 | MGITARKVLGTPYANGAKLMFLGAGELGKETMIEAQRMGIEIVAVDRYANSPGMQVAHRSYVTNMKSERALLAIVEKEKPDAIIPEIEAINTDTLFKLEKEGFFVAPCANAVWTAMHRERLREAIASTGARTSKYEYATDLESFKAACKKIGFPCVSKPIMSSSGKGSYVLKSSKDVEKAFKEAAKARGSSDKIIVEEFIDFDVEITALSVRYLNGKGKPESKFVRPLGHYQIEGDYHASWHPWTDATDKKIDKLEKEIYDYAGRIMDKLGGYGLFAHEMFVDTKNGKVYANETACRPHDTGLVTIASMPFGYSEFALHA... | 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-ri... |
Q59S63 | MGDKFSVPTNQSKERQPIVKKKKKKKRTNIYSYILIISFPVIDQFQMSESLNIQELTDNSSIIPIPTESTDVQDVTSVSNKDTTTTTTTTTTTTESTTRVRKSSPSPSANENDKKRLKKEFQPRQKIEYTPLVDENGQPIPKAPRKPKRKVAVMLGYCGTGYNGMQVQNDPNVKTIEKDIYDAMATAGAISAENAVDLKKSGFQRAARTDKGVHAAGNVISLKMIIEDPEIINKINDLLPKQIRIWGIQRTTKGFDCRKCCSSRIYEYLLPTFSLLPPKPKSVLSELVKEKKLENPDLFEDDQEGIDWWENVKSKILASG... | 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 snR... |
Q9Y606 | MGLQLRALLGAFGRWTLRLGPRPSCSPRMAGNAEPPPAGAACPQDRRSCSGRAGGDRVWEDGEHPAKKLKSGGDEERREKPPKRKIVLLMAYSGKGYHGMQRNVGSSQFKTIEDDLVSALVRSGCIPENHGEDMRKMSFQRCARTDKGVSAAGQVVSLKVWLIDDILEKINSHLPSHIRILGLKRVTGGFNSKNRCDARTYCYLLPTFAFAHKDRDVQDETYRLSAETLQQVNRLLACYKGTHNFHNFTSQKGPQDPSACRYILEMYCEEPFVREGLEFAVIRVKGQSFMMHQIRKMVGLVVAIVKGYAPESVLERSWGT... | 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... |
Q9WU56 | MGFPRLWAALLRNWGRWTARPGPRVPGLPPMAGNKVPPALASHQPDRKGRGGWVWEETEHPAKRVKGGEDEEPPRKLPKRKIVLLMAYSGKGYHGMQRNLGSSQFRTIEDDLVSALVQAGCIPENHGTDMRKMSFQRCARTDKGVSAAGQVVSLKVWLIDDILDKINSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPTFAFAHKDRDVQDESYRLSAETLQQVNRLLACYKGTHNFHNFTSQKGPREPSARRYILEMYCEEPFVREGLEFAVIKVKGQSFMMHQIRKMVGLVVAIVKGYAPESVLERSWGEEKVD... | 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... |
Q4KM92 | MGFPRLWAALLRAWGRWTARPGPRVPGLPPMAGNKVPPALPSHQPDRKGRGGWVWEETEHPAKRVKGGEDEEPPRKLPKRKIVLLMAYSGKGYHGMQRNLGSSQFRTIEDDLVSALVQAGCIPENHGTDMRKMSFQRCARTDKGVSAAGQVVSLKVWLIDDILDKINSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPTFAFAHKDRDVQDESYRLSAETLQQVNRLLGCYKGTHNFHNFTSQKGPREPSARRYILEMYCEEPFVREGLEFAVIKVKGQSFMMHQIRKMVGLVVAIVKGYAPESVLERSWGEEKVD... | 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'-... |
O94396 | MGRGGKRTWYNGDRREAKRNRPNSIYNGEGRPENLVVGEKKPKRKVACLVGYCGSGYHGMQLNPPSKTIEGDLFDAFVKAGAVSSYNADDPKKVALARAARTDKGVHAAGNVISLKLIMEDEKLIEKVNEHLPPSIRLWDVIRTINSFNPRTYCESRIYEYMVPTYAFVPPKPSSILGNCIMKNSPMPAEPINKENINQLSRSLFYEEGKEFWDDYDIAAKEILSLYEQDPEGFVNPYSKRGAAALANSENNKGSEAGVSAKTNPDMDSDSSAIVNEFLKPDSVEDESAGSKIDPSYRLERALKHIEVLKLKNYRISADR... | 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 sn... |
Q6CC39 | MSEPTTTPVVGNSASGDSAEQHDLGQKRGKGGNWNRPRGDHQAKKQKMDRRGDRQREQEKQGEGRDTRRKTDGPLVADEVRQPKRKVACMIGYCGTGYHGMQLNPPQKTIEGDIFQAFVKAGAISQNNADDPKKSAFMRAARTDKGVHAAGNVISLKMIIEDENIVEKINSHLPEQLRVWGVSRTNKAFECRKLCSSRVYEYLMPTYSFLNPRPGTVMSEKLLKDGTSPDEEGKKYWESVAADLESQGVSYDEWMKRACIDEIKGEETKEVAESEVKTDSKTDAATLEKIKAVERRHREEFRISGERLAKIREILKIYEG... | 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 snR... |
Q12211 | MSEENLRPAYDDQVNEDVYKRGAQSKLTKARKADFDDEKDKKKDNDKHIDKRPKSGPRLDENGNPLPKEPRLPKRKVAVMVGYCGTGYHGMQYNPPNPTIESALFKAFVEAGAISKDNSNDLKKNGFMRAARTDKGVHAGGNLISLKMIIEDPDIKQKINEKLPEGIRVWDIERVNKAFDCRKMCSSRWYEYLLPTYSLIGPKPGSILYRDIEESKTELPGVLDEDLESKEFWEEFKKDANEKFSTEEIEAILAYVPPARDEFDINEELYQKVKKYKQLENAHRRRYRISAAKLAKFRASTSQYLGAHNFHNFTLGKDFK... | 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 sn... |
Q3ECD0 | MLSISQLPSFSLTTAKSLRYPSSPSSSLSIFFSFFPKVSNFVRASSGIPNLVACSPTEIIIPRVNNAGLRIEEIVDAAKGKIRLDSWISSRINGVSRARVQSSIRLGLVTVNGRVVDKVSHNVKSGDEVNCTISELQPLKAEAEDIPLDIVYEDKHVLVVNKPAHMVVHPAPGNPTGTLVNGILHHCSLPCVDYSNSEEDDDSDEETFSDDEEMTTSPSSYAASVRPGIVHRLDKGTTGLLVVAKDEHSHAHLAEQFKLHTIERVYVSLTTGVPSPPQGRIEIPIGRDSSNRIRMAAIPGGVRGGRARHAASRYKVIETF... | 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 | MATTAAASPPAIATALSALLRRQRRRSSRCVGASHARCLAADANAEAVAPSRRGGHGGTRLEEAVPAGEGRSRIDAWISARLGGGGVSRARIQASIRAGLVVVNGRPVSKVSHMVKGGDIVSCTVLELQPLRAEPEDIPLDIVYEDDHLLVVNKPAHMVVHPAPGNANGTLVNAILHHCKISTFTCLARNSIDDECPDSSDDDIDVFDIDQFTTGEVSSEVREALVRPGIVHRLDKGTSGLLVVAKDEHSHAQLAEQFKLHTIRRVYISLTCGAPNPNSGRIEVPIARDPNNRIRMIATPGSGHRYARHAASRYKVREVF... | 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 | MTSISKRKNQQEHIPAEDLETPKLPKREKIEGTKESNKVRIIILLGYSGYGYHGIQINNPLKTIEGDVVAVLKKLGYLKTNNIDAEHLCIARAARTDKGVHTLRNLISLNLFVDKPLDISLLKTELNEALCSQIRVWSVFPAPKYFNPRISCESRTYEYLIPSFALLPPKPSCPLFKKMQKNLSRKLDNELERNLVYSMNDLISFWNTVKLKQKEIQEMFDTNKDAFTNPFKGMFYEKPIPAGIVIPPQAKLKKALKQAEYYCYMNYRIKEDRLKVLQQLLKKYEGRHNFHNFTVTDDSTSPSNYRFIESVTCGTPFVYE... | 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 pseudourid... |
P53167 | MLLGYCGSGYYGMQYNPPHKTIEGEILTKLFDVGAISEENSLAPKKNSFMAAARTDKGVHAMLNLLSLKITLREDTVAKLNAALPPEIRVWGIQPVNKKFNARSACDSRWYQYLIPEFILIGPPRSSLLHRNVGGCYREDGSQEVWDTFLEQTRGRFSGDELCRLQDTAQKLSESDPLVQDYVGLLSGTLSGYCLSPSKLDAFEAAMQEYVGTHNFHNFTTGKLWGDPSAQRHIKKVVVSQASPGWICVRIHGQSFMLHQIRRMVALAVLAARCQLPPNIVRNYFNAGPRKYIPRAPAQGLLLEGPVFDGYNTKLRNLLY... | 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... |
Q5XET6 | MWKAKTCFRQIYLTVLIRRYSRVAPPPSSVIRVTNNVAHLGPPKQGPLPRQLISLPPFPGHPLPGKNAGADGDDGDSGGHVTAISWVKYYFEEIYDKAIQTHFTKGLVQMEFRGRRDASREKEDGAIPMRKIKHNEVMQIGDKIWLPVSIAEMRISKRYDTIPSGTLYPNADEIAYLQRLVRFKDSAIIVLNKPPKLPVKGNVPIHNSMDALAAAALSFGNDEGPRLVHRLDRETSGLLVMGRTKESIDYLHSVFSDYKGRNSSCKAWNKACEAMYQQYWALVIGSPKEKEGLISAPLSKVLLDDGKTDRVVLAQGSGFE... | 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 | MAYNDTDRNQTEKLLKRVRELEQEVQRLKKEQAKNKEDSNIRENSAGAGKTKRAFDFSAHGRRHVALRIAYMGWGYQGFASQENTNNTIEEKLFEALTKTRLVESRQTSNYHRCGRTDKGVSAFGQVISLDLRSQFPRGRDSEDFNVKEEANAAAEEIRYTHILNRVLPPDIRILAWAPVEPSFSARFSCLERTYRYFFPRADLDIVTMDYAAQKYVGTHDFRNLCKMDVANGVINFQRTILSAQVQLVGQSPGEGRWQEPFQLCQFEVTGQAFLYHQVRCMMAILFLIGQGMEKPEIIDELLNIEKNPQKPQYSMAVEF... | 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 | MAENTDRNQIEKLLNRVKELEQEVERLKKKKEQANNIKDSSIRENSLGSGKAKRAFDFSAHGRRHVALKIAYLGWGYQGFASQENTSNTIEEKLFEALTKTRLVESRQTSNYHRCGRTDKGVSAFGQVISLDLRSQFPTSRDSEDSNLKHEADDLAKEIRYTHILNRVLPADIRVLAWAPVEPSFSARFSCLERTYRYFFPRADLDIATMNYAAQKYVGTHDFRNLCKMDVANGVINFQRTILCAQVQLVAQSPGEERRQEPFQLCQFEVIGQAFLYHQVRCMMAILFLIGQGMEKPEIIDELLNIQKNPQKPQYSMAVE... | 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 | MLCRRRRVGAAVRWLSRLAPPAPAEADPVVVRVDGSNVARLGKPKPGPRPRQLLSLPPFPGGGDGDPLPGRKAAAPRRVTAVSWVKHYLADVPQEVVQAHFNKRLVYSECSDHEVSVETIKSQKHHLKKIKHNDVMEPGMRIHLPVSVAEGEIKKRYETIPTATLHPNKDEIEYLRRLVIHKDSAILVLNKPPKVPMKGNLPVHNSMDVLAAAALSYGNEEGPKLVHRLDRESSGLLLFGRTKESFTRLHWLFTSVNLAKTNSQVWNAACEAYMQRYWALVIGTPKEREGIISAPLSKVLLDDGKAERVILAHPSGIDGA... | 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 | MARFRRADLAAAGVMLLCHFLTDRFQFAHGEPGHHTNDWIYEVTNAFPWNEEGVEVDSQAYNHRWKRNVDPFKAVDTNRASMGQASPESKGFTDLLLDDGQDNNTQIEEDTDHNYYISRIYGPADSASRDLWVNIDQMEKDKVKIHGILSNTHRQAARVNLSFDFPFYGHFLNEVTVATGGFIYTGEVVHRMLTATQYIAPLMANFDPSVSRNSTVRYFDNGTALVVQWDHVHLQDNYNLGSFTFQATLLMDGRIIFGYKEIPVLVTQISSTNHPVKVGLSDAFVVVHRIQQIPNVRRRTIYEYHRVELQMSKITNISAV... | 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. C... |
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 wi... |
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. C... |
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: Phosphorylat... |
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 respon... |
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 ... |
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... |
D7A0Y0 | MDEPVRLSLAEVHVLCRDTLVAAGLGEEHAQAIARSITRAEADECHSHGLYRLIGYVASVRSGKAERHALPALARATPAVLRVDAKHGFAPLAVETGVPALIAAAKEIGIAALAIHDCYHFSALWADIEPAVEAGLAAWCFTVGQCCVAPAGGTTPLLGTNPFAFGWPGPSGRPFIFDFATSAAARGEIELKRRGGEKIPPGWAVGPDGAPTTDPAAALAGALLPFGGHKGSALSMMVELIAGPLIGDLTSRQSKAVENGDGGPPLGGELFIAIDPAVFGTGNLSSRLADADELFALAKAQPGVRLPSERRYQARERSRT... | 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 ... |
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 Topol... |
O30019 | MFSKILVANRGEIAVRVMRACRELGIKTVGVYSSADKRAFHRVYADECYYIGKADPRDSYLNIDRIIEVAKKSGAEAIHPGYGFLAENAEFAERCEEEGIVFIGPSPEVIRIAGSKVRSRESMQRAGVPVIPGSPKIDTVDEAKEWAEKIGYPVAVKASGGGGGIGIVVVNSQEELEEAFRKSKKLGESYFKDSTVYLEKYLARPRHIEVQILADQHGNVIHLGERECSIQRRHQKLIEEAPSPALNEEMREELGKLAVKGAREIGYTNAGTFEFLYENGNFYFLEINSRLQVEHTITEVVTGIDIVKYQIRIAYGEELR... | 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
Seque... |
Q58626 | MFNKVLIANRGEIAIRIIRACWELGIKTVAVYSEADKRSLHATLADEAYCIGPAPAAKSYLNIDAILNVAEKAKVDAIHPGYGFLAENAEFARAVKKAGFEFIGPNPDAIEAMGSKINAKKIMKKAGVPLIPGSEGAIEDIDEAIEIAEAIGFPVVVKASAGGGGMGMSVAYSKEELKEVIESARNIAKSAFGDPTVFIEKYLENPRHIEIQLLGDKHGNIIHLGDRECSIQRRHQKLIEEAPSPIMTEELRERMGEAAIKAGKAINYDSAGTVEFLYENGNFYFLEMNTRIQVEHTVTEQVTGIDLVKAMIKIAAGEEL... | 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
Seque... |
Q58628 | MVKIVDTTFRDAQQSLIATRMRTEDMLPIAEKMDEVGFYSMEVWGGATFDACIRYLNEDPWERLRALKKRIQNTPLQMLLRGQNLVGYRHYPDDIVEKFVIKAHENGIDIFRIFDALNDVRNMETAIKTAKKVGAEVQGAICYTISPVHTIDQYVELAKKLEEMGCDSICIKDMAGLLTPYEGYELVKRLKEEISLPIDVHSHCTSGLAPMTYLKVIEAGADMVDCAISPFAMGTSQPPTESIVVALKGTKYDTGLDLKLLNEIRDYFMKVREKYKMLFSPISQIVDARVLVYQVPGGMLSNLVSQLKEQGALDKFEEVL... | 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
Seque... |
O27179 | MKGIKVVETAFRDAHQSLLATRLRTRDMTPIAEEMDRVGFFSLEAWGGATFDTCIRYLNEDPWERLRELKEHVKRTPIQMLLRGQNLVGYKHYPDDIVRKFIEKSYENGVDVFRIFDALNDIRNMEYAIKVAREQEAHVQGVICYTISPYHTLESYVDFARELEALECDSVAIKDMAGLISPHDAYELVRALKEETDLMVNLHCHCTSGMTPMSYYAACEAGVDILDTAISPLSWGASQPPTESIVAALRDTPYDTGLDLEILKNIKKYFEEIRKKYSSILDPIAEQIDTDVLIYQIPGGMLSNLVAQLKEQNALDRYEE... | 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
Seque... |
P0DV24 | MSFKDVTAKNFKGLKNVSLKKSMAMEGHTLVGTEARLGDAFELCESFSTSPSNIIEYEYQEEIRPFFQKAGLNKHSIGTHPELTGLGVGMIYNQYTVTMFVDIRKSSRLSLLLPLEQVYVVKNRILQACIDIVRALDGYPHRLMGDALMAFFGRSDVSKEDAIADAINAASTLRLILMDYIFPSLNEDIGEQIDLGVRIGLDYGAEDEVVWGNFGLGSFCEVTALGLPVDMTAKLQQLADKNTAMLGQGILDYIDFPEEYTKPKVKSGEELKYIIPNITNKEGQPINRRIRLLNMARYQELLPFKLNDKKMASAILYPNQ... | 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 adjacen... |
A4D9R2 | MVSSFSSKRLGDTMDSLALGSNWAGGVAIVLFLAPLALHLVSSYLFPSTSTVINSGRAWDIFRTTAKKRFRSDAARLLQNGFEKSPDAFRILTDNGPLLVLSPRYAREVRSDDRLSLDHFIASEFHPDIPGFEPFKLILDPRNPLNTILKTSLTQALEDLSVEVADALSTALTDDSEWHEISPCQTALKLVAQMASKAFIGPEKCRDPKWHNVIITYTHNVYRAAQALHFWPKFLRPIVARFLPACQTLQAQIAEAREILEPLVAQRRADRACRAAQGKPVPSRADVIDWLEDSHGDQPYDPVAAQLLLSFAAIHGTSNL... | 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 . Nicot... |
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 th... |
Q4WLD1 | MRVLIIGGSIAGLTLAHCLEKAKIDYVLLEKKEEIAPQEGASIGILPNGGRIMEQLGLYHQIEQLIEPLARAHVTYPDGFHFTSQYPALLQQRFGYPLAFLDRQKLLQILAAGPVQSGRVKLGHQVVNIESTPDGVTVRTSHGHVYQGDLVVGADGVHSRVRAEMWRLATASQGEIFRSEYNKLTIDYACIFGISSPVDQLEPGEQITCYNDGWSILSVIGQNGRVFWFLFIKLDKESVYDGSRKNGPRFSPADARAHCERLAHEPVWNGVKFGHVWAQCEVFQMTPLEEGLFSKWYWRNIVCIGDSMHKFAPHIGQGAN... | 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 . Nicotin... |
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).
Lo... |
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-Co... |
Q4WLC9 | MSVQTTYSPVNQDEQVHDGLASRHVSCEGAPSDDSPYALSSLDHNPLGINVSFLLCFHAAQPEEGIRVLEDGINQLLKAHPFLAGDVTRPTRLSQRTNTMQIEPDAPESLLKIPMLQIRHHPATSIEELESKRLLPGAEEQEIIRQLAPLPIDMDLSLPQRPVLRFQANIMRDGVILAMTFHHAAMDGAGAARVLGLLADYCRDPAAPSVGVIPDRQLRSQIDRLATGCSPSASRADFSQHYCGLGDWAALLAENWPGFLQARATELVTWRLTIPGFKVQYLKGACNALLQGQTSALAGGTLTPTILSNNDIVSALMAMI... | 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 i... |
Q4WLC8 | MDLVPSSTLWSIAQELALYLAFTVPTAFVIITTPKSSFLRLAWTPCLLYILYRFSLQVPSLTTSQFLNGVAAGQATVAALQCLNLLLITKLDERELVHAGLCIPSSSLLVRVACAWALLVNFRGIGTVWEVKNVPQHAAYLQKPKQHRLSRRRYVLRESAIIIWQYLLLDLIHMSTKDTPPGDLARLFGPGLEYRYLDATAEQWFGRVSVGIFSWLVPSRVCLNIVSRIYCLVLVVLRISAPESCRPSFGRVRDACTIRGFWGKFWHQSFRWPLTSVGSFVARDVLRLPRPSLLERYTNIFFTFFTSAVLHLACDAILGI... | 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 ... |
A4D9R3 | MIRVEDASIGTVWVTCLLAVGLYFIRSRLLSDQFAGFPSVNSRKPWEVLNVFAHRRFQQNGPEYLKAGFAKSPVFGVVTDLGPKLVVSGAFIEDFKDEKLLDHYRAMVEDFMAEVPGFESMFLGNLHNTVLRDVISVITRELDQFTLPLSDEVSTALGDTWSDSPDWTEVTLLPSMLGLIARVSSLIFVGEPLCRDPAWLETVVNFTIVRHQAILALHMCPAVLRPVLHWFLPPCQKLRREIKTARSLINSALEELRKNPPTDRFSSLAWVDAFASGKKYDATMVQLRLANASIHSSADLLAKVLINLCEQPGLIQDLRD... | 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 . Nicot... |
Q43086 | MTVASMLSSNSMNVGVSNPKMSSKTSACCLLNRPWPSSCSMSISSCGQFGVSEKSKLLCGAGALQVESAPLFSVGQKFQLDDVIEAQQFDRETLSAIFEVARSMENIRGNSSGSQMLKGYLMATLFYEPSTRTRLSFESAMKRLGGDVLTTENAREFSSAAKGETLEDTIRTVEGYSDIIVLRHFESGAARRAAATANIPVINAGDGPGQHPSQALLDVYTIEREIGKLDGIKVGLVGDLANGRTVRSLAYLLAKYRDVKLYFVSPNVVKMKDDIKEYLTSKGVEWEESSDLMEVASKCDVVYQTRIQKERFGEKLNLYE... | 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
|
Q43064 | MTASSSLFSCSMHMEVLTPKISKWPKDFVSCHSKISYVETNYLKSTCYPISRFLCINNLSKCDKMIKTRQRDGIHCFSEGQKFQLDDVIEAQQFDRDILNAIFEIARDMENIERNSPESQILKGYLMATLFYEPSTRTRLSFESAMRRLGGEVLTTENAREFSSAAKGETLEDTIRTVEGYSDLIVLRHFESGAARRAAAIAGIPIVNAGDGPGQHPSQALLDVYTIEREIGKLDGIKVGLVGDLANGRTVRSLAYLLAKYKDVKIYFVSPEVVKMKDDIKDYLTSKGVDWEESSDLVEVASECDVVYQTRIQKERFGER... | 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
|
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
|
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
|
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
|
C5C683 | MRHLLSAADLGRDEAVALLDTAETMADTQSRAIKKLPPLRGLTVVNLFFEDSTRTRISFEAAAKRLSADVINFSAKGSSVSKGESLKDTAQTLQAMGADAVVVRHWASGAPHRLAHAGWIAAPVINAGDGTHQHPTQALLDAFTLRRRLAGPDGPIGTDLAGRHVVVVGDVLHSRVARSNVDLLSTLGARVTLVAPPTLLPVGVESWPCEVGYDLDAAIDAGPDAVMMLRVQRERMSSGFFPSEREYARAYGLDAARVSRLGKHALVMHPGPMNRGLEISADAADSARSTVVEQVTNGVSVRMAVLYTLLAGGPDGDSTT... | 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
|
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
|
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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