ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9I513 | MSSKQPSLSYKDAGVDIDAGEALVERIKGVAKRTARPEVMGGLGGFGALCEIPAGYKQPVLVSGTDGVGTKLRLALNLNKHDSIGQDLVAMCVNDLVVCGAEPLFFLDYYATGKLNVDVAATVVTGIGAGCELAGCSLVGGETAEMPGMYEGEDYDLAGFCVGVVEKAEIIDGSRVQAGDALIALPSSGPHSNGYSLIRKIIEVSGADIAQVQLDGKPLADLLMAPTRIYVKPLLQLIKQTGAVKAMAHITGGGLLDNIPRVLPDNAQAVIDVASWNRPAVFDWLQEQGNVDETEMHRVLNCGVGMVICVAQSDAEKALE... | Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate
Sequence Mass (Da): 37123
Sequence Length: 353
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-... |
Q89W81 | MTTMLSSDLPLPKIGRGKVRDIYAVDDDRLLLLTTDRISAFDVVMGETIPMKGAVLTQISAFWFGELEGVVPHHMISADTDEIIAAVPALKPHRAEILGRAMLSRRTTVFPIECVIRGYLSGSAWKEYATSGTLAGEKLKAGLVESEKLEPAIFSPATKAETGHDENITIARMREVVGDETAYTLESMTRAIYTLGEELAREQGIIIADTKFEFGRDKDGRIILIDEVMTPDSSRFWAVDAYKPGQPQASFDKQPLRDYLDVERRAGRWNGDAPPPPLPASVVEATSKRYLEAYRRVTGKELKI | 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): 33701
Sequence Length: 304
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-ami... |
Q98I23 | MRTLSDAFIPELPGYYKGKVRENYDLADGRRIIIATDRLSAFDIILTSIPFKGEILTQTARYWFEETADICPNHVLEYPDPNVVVGTRLDILPVEIVVRGYLAGTTSTSILTRYRRGEREMYGMRLPDGLRDNEKLAAPVITPTSKAADGGHDEPLSRAEILAQGLLTQAQWDTVSDYALKLFARGQARAAERGLILADTKYEFGTDKNGTIILADEIHTPDSSRYWIAASYEQALASGTRPDSFDKDFIRSWVAARCDPYKDPIPRIPDEIVEQASRIYAQAYEAITGKAFVPDLSGDTVLDRIRSNLVRFF | 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): 35091
Sequence Length: 313
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-ami... |
Q9HNU7 | MASVKDRRVESPATDTDLGRGVFEFSDRYSVFDWGEMPDHVPGKGASLCTMGAYTFEQLAAAGVPTHYQGVRTPDGETVRLADAPEAPTQMVIDLTQVPTLPFEDGSYDYDRYHDAGGSNYLVPLEVVFRNAVPVGSSLRTRCAPADVGIDADEWPQGPVELPETIVEFSTKYEEQDRYLSRSMADEIAGDADIAELDALARRVNETITDCAADAGFVHDDGKLECVYVDGEVRVADVAGTFDENRFRFDGREVSKEAVRQFYKRSDPEWVGAVKDAKRAADERGVADWKSLCEPSPDPLPPEILQAAADLYAAGANRYT... | 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): 37124
Sequence Length: 338
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-ami... |
O68830 | MEKEKLLYEGKAKKLYFTDDSEVLWVEYCDQATALNGARKEQITGKGALNNQITSLIFEKLNAEGLETHFIEKLSKTEQLNRKVSIIPLEVVLRNVVAGSFAKRFGLEEGIVLQEPIVEFYYKDDALDDPFINDEHVRFLNIATYSEIEFLKSETRKINEILKKIWAEIGLTLVDFKLEFGRLADGRIILADEISPDTSRLWDANGQHMDKDVFRRNIGDLVETYTEVLNLLENAK | 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): 27136
Sequence Length: 236
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-ami... |
Q88U22 | MTAAIEKQALLYTGKAKAMYATNDPEILWVEYLDQATALNGKRKVPIDQKGRLNNRIASLIFKDLANHGIANHFIEQPSDYVQLVRRVTMIPLETVVRNAASGSFERKFAVPHLTKFAEPVLEFFYKSDQLDDPFINDSQIHALNVATPAIVAEIKRQALQVNQRLTAIFAAMGVQLVDFKIEFGLTTTGKVLLADEISPDSCRLVDLKTGASLDKDVFRKDLGDLTSVYQEVLTRLATVEEA | 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): 27081
Sequence Length: 243
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-ami... |
P12048 | MTIKRALISVSDKTNLVPFVKELTELGVEVISTGGTKKLLQENGVDVIGISEVTGFPEIMDGRLKTLHPNIHGGLLAVRGNEEHMAQINEHGIQPIDLVVVNLYPFKETISKEDVTYEEAIENIDIGGPGMLRAASKNHQDVTVIVDPADYSPVLNQIKEEGSVSLQKKRELAAKVFRHTAAYDALIADYLTNVVGEKEPEQFTVTFEKKQSLRYGENPHQEATFYQTALPVKGSIAQAEQLHGKELSYNNIKDADAAVQIVREFTEPAAVAVKHMNPCGVGTGKTIAEAFDRAFEADKTSIFGGIIALNREVDKATAEA... | 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): 55753
Sequence Length: 512
Domain: The IMP cyclohydrolase activity resides in the N-terminal r... |
Q8A155 | MSESKRIKTALVSVYHKEGLDEIITKLYEEGVEFLSTGGTRQFIESLGYPCKAVEDLTTYPSILGGRVKTLHPKIFGGILCRRDLEQDIQQIEKYEIPEIDLVIVDLYPFEATVASGASEADIIEKIDIGGISLIRAAAKNYNDVIIVASQAQYKPLLDMLMEHGATSSLEERRWMAKEAFAVSSHYDSAIFNYFDAGEGSAFRCSVNNQKQLRYGENPHQKGYFYGNLDAMFDQIHGKEISYNNLLDINAAVDLIDEYEDLTFAILKHNNACGLASRPTVLEAWTDALAGDPVSAFGGVLITNGVIDKAAAEEINKIFF... | 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): 55880
Sequence Length: 507
Domain: The IMP cyclohydrolase activity resides in the N-terminal r... |
Q6G5S5 | MGVVAKNFPIPDLHRVRRVLLSVSDKTGIVAFAQALQTYNVELISTGGTAKVLMAAGLPVRDVAEVTGFPEIMDGRVKTLHPLIHGALLGVREDPSHAVAMEQYGIHGIDLLVVNLYPFEETVQSGADGQTILENIDIGGPAMIRAAAKNHVYTGVITAVSDYDAVLSELKQHDGCLSFSMRQQLAMRAYAHTAAYDTAIAAWFAKNLKIETPSWQSFSGHLKNVMRYGENPHQKAAFYRNGDKRFGVATAKLLQGKALSYNNMNDTDAAFELVAEFDPQNTAAVALIKHANPCGVAEGQTLKEAYLKALLCDNVSAFGG... | 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): 57597
Sequence Length: 538
Domain: The IMP cyclohydrolase activity resides in the N-terminal r... |
Q1LU51 | MQRPIIIRRALLSVSDKTNICELAKSLLKRGVQLISTNGTARLLVNAGIHVTEVSNYTGFPEIMDGRVKTLHPKIHGGILARRNIDDTIMQQYKIEHIDMVVVNLYPFAEVVASATCNHEKVVENIDIGGTALLRSAAKNYSNVVVVVSINDYISIINEIDCNNGAVSLETRLNLAIKAFQHTATYDSQIKDYFTSQVYTDSSKCSSIFPPILNINFVKKQDMRYGENQHQLAAFYLDTRNKEKSIATTKQLQGRALSYNNIADADAALECVKEFSEPACVIVKHINPCSVAMGKTILVAYQRAYETDPTSAFGGVIAFN... | 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): 58384
Sequence Length: 526
Domain: The IMP cyclohydrolase activity resides in the N-terminal r... |
Q8G6B1 | MTNTNRPIRRALVSVFHKEGIEVLAEAFVKAGTEVVSTGSTAKKLAELGVKVTEVSDVTGFPECLDGRVKTLHPYIHAGILADMTNPEHAKQLEEFGIKPFDLVVVNLYPFADTVRSGANEADTIEKIDIGGPSMVRGAAKNHATVAIVTDPADYALVASRVADGTGFSLDERKWLAAKAFAHTAAYDATINEWTAKHWPKPASLDAVEVDKDDQGTEVDPAKFPAQFTRTWDRAHTLRYGENSHQQAALYIDPLNQTGFAHAEQLGGKPMSYNNYVDADAAWRTVWDMAPAIAVAVVKHNNPCGLAIGATAAEAHKKAH... | 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): 58413
Sequence Length: 545
Domain: The IMP cyclohydrolase activity resides in the N-terminal r... |
Q0VCK0 | MAPGQLALFSVSDKNGLVEFARNLASVGLNLIASGGTAKALRDAGLAVRDVSELTGFPEMLGGRVKTLHPAVHAGILARDIPEDSADMAKLDFNLIRVVVCNLYPFGKTVASPGVTVEEAVEHIDIGGVTLLRAAAKNHARVTVVCEPEDYAAVASEMQDSDSKDTSLETRRQLALKAFTHTAQYDEAISDYFRKEYSKGVSQMPLRYGMNPHQTPAQLYTLKPKLPITVLNGAPGFINLCDALNAWQLVKELKEALGLPAAASFKHVSPAGAAVGIPLSEDEANVCMVYDLYKTLTPVATAYARARGADRMSSFGDFVA... | 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). Can use both 10-formyldihydrofolate a... |
Q89WU7 | MTDHPRRVTRALLSVSDKTGLIEFAKALAAHDVELVSTGGTAKAIAAAGLKVKDVSELTGFPEMMDGRVKTLHPKVHGGLLAIRDNKDHADAMKAHGIAPIDLLVVNLYPFEATVDKGAGFEDCIENIDIGGPAMIRAAAKNHDDVAVVVEAEDYKAVLDELAANKGATTLKLRRRLAAKAYARTAAYDAAISNWFNRQLEIDAPDFRAFGGKLIQSLRYGENPHQTAAFYATPDKRPGVSTARQLQGKELSYNNINDTDAAYECIGEFDAKRTAACVIVKHANPCGVAEGSDLVSAYRKALACDSTSAFGGIIAMNRAL... | 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): 56465
Sequence Length: 530
Domain: The IMP cyclohydrolase activity resides in the N-terminal r... |
A6WXV3 | MAVSSKHIPAPDLHRVRRALLSVSDKTGLIDFAKALHAQGVEILSTGGTAKSIAAEGIPVKDVSEVTGFPEIMDGRVKTLHPAVHGGLLAVRNDREHVAAMEEHGIGGIDLAVINLYPFEEVRFKGGDYDTTVENIDIGGPAMIRASAKNHAYVATVVDPADYADVVAELEKHAGSLPLAFRKKLAAKAFSRTAAYDAAISNWFAEAINEETPVYRSVAGKLHSVMRYGENPHQTAGFYLTGEKRPGVATATQLQGKQLSYNNINDTDAAFELVAEFDPARTAAVAIIKHANPCGVAEAATIKEAYLKALACDPVSAFGG... | 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): 56639
Sequence Length: 538
Domain: The IMP cyclohydrolase activity resides in the N-terminal r... |
Q1H4G7 | MAVIKRALISVSDKTGILEFAKALAEFGVEILSTGGTAKLFRDNGIPVTEVSDYTGFPEMLDGRVKTLHPKIHGGLLGRRDLPEHVTAMQAAGIPDIDMIVVNLYPFEATVARPDATLEDAIENIDIGGPAMVRSAAKNWQDVAVLTDASQYEEVLAEMRSTGGATSKATRFALSVAAFNRISNYDGAISDYLSSFNADGTRNEFPGQINGRLVKVQDLRYGENPHQQAAFYRDLYPAPGSLVTAQQLQGKELSYNNIADADAAWECVKSFDSTACVIVKHANPCGVALGATPLEAYQKAFQTDPTSAFGGIIAFNHTLD... | 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): 56430
Sequence Length: 528
Domain: The IMP cyclohydrolase activity resides in the N-terminal r... |
Q8D244 | MEQSFLPIRCALISVSDKTGIFSLAKNLIKHKVKLITTSGTYKYLLEKGIFSTSVSEYINHPEIINGRVKTLHPKIHGGILSNNKNINENKNLNIKKIDMVITNFYPFKKKVKKENIKIENIIDNIDIGGVALARSAAKNYKYVTVVVNINQYSKLSSEMDKNSGSVSFKTRFYFSTLAFQYSYSYDKEIFNYFNKIYFKEIELKKNLKNKKFPELFSISFSKKEDVLYGENYHQKAAFYTDPVIHPGTVPFSIQRQGKKLSYNNIVDSDIAINCVMNFSEIACVIVKHSTPCGVSSGKNIIDAYRSAYYSDPDSAFGGI... | 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): 59775
Sequence Length: 529
Domain: The IMP cyclohydrolase activity resides in the N-terminal r... |
Q9PC10 | MASDFLPVHRALLSVSDKTGLVELARALLAYNIELLSTGGTATIIREAGLPVQDVADLTGFPEMMDGRVKTLHPMVHGGLLGRAGIDDAVMAKHGIAPIDLLILNLYPFEQITAKKDCTLADAVDTIDIGGPAMLRSAAKNFARVAVATSPDQYPDLLAELQAHHGQLSAEKRFALAVAAFNHVAQYDAAISNYLSSVSDMHTTLPLRHEFPAQLNNTFVKMTELRYGENPHQTGAFYRDVHPQPGTLATFQQLQGKTLSYNNLVDADAAWECVRQFEAPACVIVKHANPCGVAVGKACSDAYEEAYATDPTSAFGGIIA... | 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): 56715
Sequence Length: 527
Domain: The IMP cyclohydrolase activity resides in the N-terminal r... |
P91134 | MGSVTSKTNDELESFLNKRLGGSMTSSNKTVSVLLGAQWGDEGKGKIIDYLIENHKINVTARCQGGNNAGHTVVANGRKYDFHILPSGIISPTCFNVIGNGVVVNLDAFFSELAHNGILEESGWEKRIMISSEAHLVFGVHSQVDGRQEDSLAAKNKIGTTNRGIGPTYSSKCFRNGIRVADLMADFEEFSEKYRRLVEHYKKQFPSIEVNVDEELAKFKQHREKLAELKLVGDTVGFIHEQRNAGKQVLVEGANGALLDIDFGTYPYVTSSNSTVGGACTGIGVPPTAVGNVIGVVKAYQTRVGTGPFPTELFDSDGEK... | 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.
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-... |
Q1IJT2 | MVSKGKTAVVIGAQWGDEGKGKIVDVLSENFRVVARYAGGHNAGHTVLIGGKKFVLQLIPCGVLRPGCRGVIGNGVVLDPIAFLNEVQRLRDLGVAVDGNLFVSSRAHVILPYHRMVELASENAPGRVKIGTTSRGIGPSYEDKMGRRGLRVADLLDSTLLKKHIENACKEKNTIVHALFNAEPIDPDKMYNEYAKAAEKVAPFVTDTAVLLNNAINSGESVMFEGAQGTMLDIDHGTYPFVTSSSATSGGAVIGTGVPPTSISTVIGVTKAYCTRVGEGPFPSELHDAMGDAIRKKGNEFGAVTGRPRRTGWLDLPLLR... | 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... |
Q71YP9 | MPNMEPTTKEIKEQKIYQEMGLTDSEYELVCSILGREPNYTETGLFSVMWSEHCSYKNSKPVLRKFPTEGKQVLQGPGEGAGIVDIGDGLGVAFKVESHNHPSYVEPYQGAATGVGGIIRDVFSMGARPIAMLNSLRFGELDTPHAKYLVSEVVAGIAGYGNSIGIPTVGGEIQFDPCYTKNPLVNAMCVGLIEAKDIQKGQAKGIGNPVMYVGAKTGRDGIHGATFASVEFSEEGEQQRSAVQVGDPFMEKLLLEACLDVIRDHSDILVGIQDMGAAGLVSSSSEMASKAGAGLELIMDDVPQRELNMTPYEMLLSESQ... | 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... |
Q58660 | MDENDLKYIEKVLGRKPNHIELAMFENLWSEHCAYRTSKKLLRMFAKTVNEKTSKNIVVGIGDDAAVIRLKNDICLAIAMESHNHPSYIDPYNGAATGVGGIVRDVLSMGAKPIALLDPLRFGDIFGKEGDKVRWLIEGVVKGIGDYGNRIGVPTVGGECEFDSSFDYNNLVNVVCVGLVKENEIITGKAKEPGLSLILIGSTGRDGIGGASFASKDLTEESEEERPSVQVGDAFSEKCLIDAVLEAVKTGKVKAMKDLGAAGLSGASSEMCYGGGVGCELYLENVVLREPLTPYEIMVSESQERMLLAVEPGSEEEIIE... | 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... |
Q8TY09 | MTLDERDLELIREELGRDPNATERAMFENMWSEHCAYRSTRHLLRQLPSEADHVIVGPGDDAAVVAIDDEWAVVVGIESHNHPSYVDPYNGAATGVGGIVRDVLSMGAFPIALLDPLRFGPLDGERVPYLVDGVVRGISDYGNRIGVPTVGGELEFDPSYERNPLVNVMCVGIVRRSEIVRGRADRPGDVLVLVGARTGRDGIGGAAFASEELGEESEEEDRPAVQIGDPFTERQLIIAIREAVERGLVKGCKDLGAAGLTCAATEMAADGGTGVEIDVFKVPLREEGMEPWEIMLSESQERMLLVVAPEDVDEVIEICR... | 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... |
Q8PYK1 | MLPEEDLKIIKKELGREPTLVEQGCFLNLWSEHCSYRSSAPLLKTFTTTGENVIIGPGDDAAIIKFEDGYVLAIGMESHNHPSYVDPYNGAATGVGGIVRDIISMGARPIALMDPLYFGPLDTPKNLFLFEQIIKGIAGYGNCIGVPVVNGETFFDRRYSGNPLVNVVAVGLCKEEKVMTSRSQKAGNKLILAGSSTGKDGLGGASFASRDLSESAEAEDRPSVQVGDPYTEKLVMEMTLEAIDKGYIKSCKDLGAAGLGGASSELAAKGGLGAYIIADAVPQREPEMNAYEILLAESQERMVFEVAPEDVDAVLALVQK... | 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... |
Q8CSX5 | MKERFIKKTHYLDYQFDEPTDIKLGFTTRENGLSPYPNHSFNMARYISDSAHHITHHQDILANLIGYPRDEWVFPIQTHDSRIVEVTSEHKGTNIDELTDDLHGIDGMYTFDSHILLTMCYADCVPVYFYSEPHGYIGLAHAGWRGTYGQIVKEMLKKVDFDYEDLKIVIGPATSNSYEINDDIKNKFEELTIDSTLYIETRGKNQHGIDLKKANALLLEEAGVPSKNIYVTEYATSENLDLFFSYRVEKGQTGRMLAFIGRK | 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... |
P45497 | MIGQRDTVNGAHFGFTDRWGGVSAVPYEELNLGGAVGDDPGAVTANRELAAKSLGVDPARVVWMNQVHGADVAVVDAPWGDRPVPRVDAVVTAERGLALAVLTADCVPVLLADPVSGVAAAAHAGRPGLVAGVVPAAVRAMAELGADPARIVARTGPAVCGRCYEVPEEMRAEVAAVEPAAYAETGWGTPALDVSAGVHAQLERLGVHDRAQSPVCTRESADHFSYRRDRTTGRLAGYVWLD | 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... |
P45496 | MIVQHRTAPVTGSAHFAFTDRWGGVSAAPYGELNLGGAVGDDPAAVGANRERAARHLGLDPAHVVWMNQVHGRDVAVVDGPWGADAEIPAVDAVVTARRGLALAVLTADCTPVLLADPVAGVVGAAHAGRPGLVAGVVSAAVEAMVALGAHPSRITAHTGPAVCGRCYEVPEEMRAEVAGAVPGTWSETSWGTPAVDVTGGVHAQLAALGVTDRHASPFCTLESGDHFSYRRDRTTGRLAGYVWLD | 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... |
P74606 | MTMGDDLWGWQNINGSPYLTCALLAPWPHAFFTRAFYPQLPEQLITYLDPQGKAFRVKQVHGDVTLTATEIGQTPLAPDSTHPPADGIISDAPHQGVWVASADCTPVLIGDLIGKRVAAIHAGWRGTKARIVPKTIDKFLALGSELKDLRVALGPAIAGEVYQVDPWVALEVGQSVQAVQKLATEEQQWDHLSTMVNPPVLPDAEPEKYRLDVRRINQLQLLELGFAQEQIAVAPHCTFQMEELFFSYRRTHTKEVQWSGIVSY | 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... |
Q1EIR0 | MIELEKLDFAKSVEGVEAFSTTRGQVDGRNAYSGVNLCDYVGDDALRVLDARLTLAMQLGVDLDDLVMPRQTHSCRVAVIDERFRALDIDEQEAALEGVDALVTRLQGIVIGVNTADCVPIVLVDSQAGIVAVSHAGWRGTVGRIAKAVVEEMCRQGATVDRIQAAMGPSICQDCFEVGDEVVEAFKKAHFNLNDIVVRNPATGKAHIDLRAANRAVLVAAGVPAANIVESQHCSRCEHTSFFSARRLGINSGRTFTGIYRK | Cofactor: Binds 4 Cu cations per subunit.
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 (By similarity). Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into ... |
Q9PET8 | MGRFPSWVLVADWPAPPGVMVLSTLRGGPGVSVAPFDRLNLGNCSGVAGDAPVCVERNRSRLVEMLGLPSVPHWLRQVHGVEVLRVDALLQSIARVVEPTADAAVTSVVGAVLAILTADCLPVVLAAVDGSEIGVVHAGWRGLADDVLGRTVAALRTSPEYLQAWLGPAAGPQAYEVGVDVYAAFVERDSGAACAFSVTRPGHWYVDLYALARQRLMRAGLSAVSIYGGGLCTISDPQRFFSHRRDRRSGRFATLAWIGC | 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... |
Q5UZ65 | MYVGRFVVVSPEVGAYRVSSRSFPNRQAVQRDGTVTVEPTPDAPETDNPYISYNGVRVTERGAVVGNGSHVDPIAEKLELGYPARDAIAEPLLSLDFEKDDYDTPRVAGIVGVDAADPTTNADGPGAVIGTVRRDALLVEEVTEPTLVATYEENSPTAFDLAATDASDVAREVYDHEYEHAVCSAGVAGSAGEFDVAVYNGE | Function: Catalyzes the cyclization of 5-formylamidoimidazole-4-carboxamide ribonucleotide to IMP.
Catalytic Activity: H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 21452
Sequence Length: 202
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formam... |
Q92PI1 | MKSAVVQLPGLNRDCDMIAALTKISGKAPVTVWQTETEIPDVDLIVIPGGFSYGDYLRCGAIAARMPVMQAIKAKAEQGVRVLGVCNGFQILVEAGLLPGALMRNASLKFVCREVKLEVVNADTAFTRAYAKGQVIRSPVAHHDGNYFADAETLKAIEGNGQVVFRYAEGTNPNGSVNDIAGVLNAKGNVLGMMPHPENLIESAHGGADGRGLFASALDVIAA | 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... |
Q5LS78 | MRAAVVVFPGSNCDRDLAVAFEQAGFDVSMVWHKDADLPQGIDIVGIPGGFSYGDYLRCGAIAAQSPICKAVVAHTARGGYALGVCNGFQVLTETGILPGALLRNAGLKYICKTVGLKVETSNSVFTEGYNAGDVIGIPIAHHDGNYYADDETLAALKAEDRIAFTYTDNPNGARDDIAGILSANRRVLGMMPHPERAADAGHGGTDGVALFRALAGALTPA | 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... |
Q9UX21 | MIAIIKFPGTTCETDVYKALIEAGVPTVIVKYKDFDPDRYNGVILPGGFSFGDYLRAGSIAASTETMKKVKQMAEDGKIVIGICNGFQILVESGLLKGALLPNLKLRFISKWVYLKVIRADTILTKGLDKKIIRMPIAHAEGRYYVDDIDYAKTHMVLQYCDENGNISEDVNPNGSLLNIASIANEEGNVIGMMPHPERASFKLTSIDGTVDGLILLRRLGEWA | 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... |
Q2N8K3 | MPHTAKILLLGSGELGREFVISAKRLGAYVVACDAYAAAPAMQVADASEVLSMLDADALRAVVAKHHPDYVVPEIEAIRTEVLAEIEADGFNVVPSAYATQMTMNRDAIRDLAAQELGITTSRYRYAKNLEEVRAAAEFTGYPCVIKPVMSSSGKGQSTVRSADKLEEAWDYAVANMRGDRKRVIVEQFIDFDYEITLLTVRHKDGITFCPPIGHRQERGDYRESWQPATMSKPAIAAAQEMAEKVVTALQGNGKGFGLFGVEFFVKGEEVIFSELSPRPHDTGMVTSVSQNLSEFDLHARAIMGLHVPSEILARPSASA... | 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... |
Q9VSK9 | MGKDRGRGRRNNHSGPYNKSNWRGQKKDRPQNNGGGQRNSAPQQKSTLLETQVGITEFTNPEAPGFTGILKSRFSDFHVNEIDSNGKVLELNDLSVPKVAIVAVAENELDNWRKELEAVIGPEVWQDIANLAKAKNDPAIEQKVEIDVTTLDKEQRTQVHQMIKQLYKGKLLSTTIGQQQAKPKVQEEASLENKDAAEGETSTQKDSQVPAEEKKTIKVFKPKPGRGDKRWSFPADYVTFLVHKTNLVTSDVASTLAARLNLRPSQVNYSGIKDKRAKTTQKFSVKRRTPESILVAARSQRNVHIGNFGFESNTLKLGDL... | Function: Pseudouridylate synthase that catalyzes pseudouridylation of RNAs, such as tRNAs and mRNAs.
Catalytic Activity: a uridine in tRNA = a pseudouridine in tRNA
Sequence Mass (Da): 82800
Sequence Length: 734
EC: 5.4.99.-
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Q96PZ0 | MEMTEMTGVSLKRGALVVEDNDSGVPVEETKKQKLSECSLTKGQDGLQNDFLSISEDVPRPPDTVSTGKGGKNSEAQLEDEEEEEEDGLSEECEEEESESFADMMKHGLTEADVGITKFVSSHQGFSGILKERYSDFVVHEIGKDGRISHLNDLSIPVDEEDPSEDIFTVLTAEEKQRLEELQLFKNKETSVAIEVIEDTKEKRTIIHQAIKSLFPGLETKTEDREGKKYIVAYHAAGKKALANPRKHSWPKSRGSYCHFVLYKENKDTMDAINVLSKYLRVKPNIFSYMGTKDKRAITVQEIAVLKITAQRLAHLNKCL... | Function: Pseudouridylate synthase that catalyzes pseudouridylation of RNAs . Acts as a regulator of protein synthesis in embryonic stem cells by mediating pseudouridylation of RNA fragments derived from tRNAs (tRFs): pseudouridylated tRFs inhibit translation by targeting the translation initiation complex . Also catal... |
Q91VU7 | MEMTSTSLKRGCLVVEDNDSVTPHDETKKQKVSEGCLTSSQDGVENDGLHRSENEPGPPEAESTVKDDENSSAQVQEEEEEEEEEDGLSEAGEEEEAESFADMMKHGLTELDVGICKFVSSHHGFSGILKERYSDFVVHEIGKDGRISHLDDLSVPVDEEDPPEDALTVLTAEDRQQLEELQLFKNKETSVAIEVIEDTKEKRTVIHQAIKSLFPGLETKTEDREGRKYIVAYHAAGKKALANPRKHSWPKSRGSYCHFVLYKENKDTMDAINVLSKYLRVKPNIFSYMGTKDKRAITVQEIAVLKISAQRLAHLNKCLM... | Function: Pseudouridylate synthase that catalyzes pseudouridylation of RNAs. Acts as a regulator of protein synthesis in embryonic stem cells by mediating pseudouridylation of RNA fragments derived from tRNAs (tRFs): pseudouridylated tRFs inhibit translation by targeting the translation initiation complex. Also catalyz... |
O74343 | MSQENHVDVPRKRIRIDQSESSRNLERNGLEDEANAPSDLSGQKFYMTESDVGIDAFLNPNLPSIDGIIKARFTDFAVFEVDTDGNIVHLTDMEAHDPILSKATGDKETEDAKDSSNQDISNDQKAPSFKEQEPATLPILPNDLQSIIPKGIGNEFIQSLHKLSVGEITDPISLILPENTPPMDKGQRTILHQFIRNNFSGLESSTKGNGTFTVSKTTRKNQPRSRRDPRLSWKALGGEYCHFHLYKENRDSMDCLGKIARLLKVPTRTLSIAGTKDRRGVTCQRVAIHHVRASRLAQLNSGSLKNSTYGFLLGNYSYKN... | Function: Catalyzes pseudouridylation at position 35 in U2 snRNA stem-loop II region which induces particular conformation of the mRNA-U2 snRNA duplex and places the nucleophile in an accessible position for the first step of splicing. Also catalyzes pseudouridylation at position 56 in U2 snRNA. Catalyzes also pseudour... |
Q08647 | MSDSSEATVKRPLDAHVGPSENAAKKLKIEQRTQADGIHEADVGITLFLSPELPGFRGQIKQRYTDFLVNEIDQEGKVIHLTDKGFKMPKKPQRSKEEVNAEKESEAARRQEFNVDPELRNQLVEIFGEEDVLKIESVYRTANKMETAKNFEDKSVRTKIHQLLREAFKNELESVTTDTNTFKIARSNRNSRTNKQEKINQTRDANGVENWGYGPSKDFIHFTLHKENKDTMEAVNVITKLLRVPSRVIRYAGTKDRRAVTCQRVSISKIGLDRLNALNRTLKGMIIGNYNFSDASLNLGDLKGNEFVVVIRDVTTGNSE... | Function: Catalyzes pseudouridylation at position 35 in U2 snRNA stem-loop II region which induces particular conformation of the mRNA-U2 snRNA duplex and places the nucleophile in an accessible position for the first step of splicing . Also catalyzes pseudouridylation at position 56 in U2 snRNA . Catalyzes also pseudo... |
Q12069 | MQRNNRLRNLFTVPVIMARQLKRNALSAGLAFAGNATSNEFDEHLQNEVEREREIQKKKKIKRTQSKKSPDLINKSTFQSRTIGSKKEKHRQLDPEYEIVIDGPLRKIKPYHFTYRTFCKERWRDKKLVDVFISEFRDRESEYYKRTIENGDVHINDETADLSTVIRNGDLITHQVHRHEPPVTSRPIKVIFEDDNIMVIDKPSGIPVHPTGRYRFNTITKMLQNNLGFVVNPCNRLDRLTSGLMFLAKTPKGADNIGDQLKAREVTKEYVAKVVGEFPETEVIVEKPLKLIEPRLALNAVCQMDEKGAKHAKTVFNRIS... | Function: Responsible for synthesis of pseudouridine from uracil-32 in mitochondrial transfer RNAs.
Catalytic Activity: uridine(32) in tRNA = pseudouridine(32) in tRNA
Sequence Mass (Da): 53399
Sequence Length: 462
Subcellular Location: Mitochondrion
EC: 5.4.99.28
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A2X8M8 | MADTGGRPEVSLATVRSPGHPAASTTAAAAADLGHADTGQEKPTVESAQPANGAAPMGECGTEYRGLPDGDAGGPMPSSARTVSMIPLIFLIFYEVSGGPFGIEDSVGAAGPLLAIIGFLVLPVIWSIPEALITAELGAMFPENGGYVVWVASALGPYWGFQQGWMKWLSGVIDNALYPVLFLDYLKSGVPALGGGAPRAFAVVGLTAVLTLLNYRGLTVVGWVAICLGVFSLLPFFVMGLIALPKLRPARWLVIDLHNVDWNLYLNTLFWNLNYWDSISTLAGEVKNPGKTLPKALFYAVIFVVVAYLYPLLAGTGAVP... | Function: Cell membrane polyamine/proton symporter involved in the polyamine uptake in cells. Possesses high affinity for spermidine and lower affinity for spermine and putrescine. Transports paraquat, a polyamine analog, and thus confers sensitivity to this chemical which is used as herbicide (By similarity).
Location... |
P09368 | MIASKSSLLVTKSRIPSLCFPLIKRSYVSKTPTHSNTAANLMVETPAANANGNSVMAPPNSINFLQTLPKKELFQLGFIGIATLNSFFLNTIIKLFPYIPIPVIKFFVSSLYCGGENFKEVIECGKRLQKRGISNMMLSLTIENSEGTKSLSSTPVDQIVKETISSVHNILLPNIIGQLESKPINDIAPGYIALKPSALVDNPHEVLYNFSNPAYKAQRDQLIENCSKITKEIFELNQSLLKKYPERKAPFMVSTIDAEKYDLQENGVYELQRILFQKFNPTSSKLISCVGTWQLYLRDSGDHILHELKLAQENGYKLGL... | Function: Converts proline to delta-1-pyrroline-5-carboxylate.
Catalytic Activity: a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a quinol + H(+)
Sequence Mass (Da): 53271
Sequence Length: 476
Pathway: Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 1/2.
Subcell... |
P78568 | MATAQLATFKIPPVSNEPMLSYAPGSPERAGLQAALAEMQSQLPFEVPCIINGQEVRTNNIQKQPMPHDHARHLCTFHEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLASGKYRYKLMAATMLGQGKNTWQAEIDAAAELADFFRFGVSYVEELYAQQPPKNAPGCWNRTEYRPLEGFVLAVSPFNFTAIGGNLPGSPALVGNVVVWKPAPAATYSNYLVFKILSEAGVPPGVIQFIPGGAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDKYKVYPRIVGETGGKNWHVIHKSAEVRNAVLQSV... | Catalytic Activity: H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-glutamate + NADH
Sequence Mass (Da): 59757
Sequence Length: 546
Pathway: Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2.
Subcellular Location: Cytoplasm
EC: 1.2.1.88
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Q9P8I0 | MQSSMLLRVRALPKTASVLSRTKTATYATYKVPRIDNEPNKHYAAGSPDRKALQEALARTQRNAPLSVPLVIAGKEVKSSSSLTQSNPASHGPVATYSNATAKDVQAAIESALEARKSWASTPFADRASVFLKAADLISTKYRYDVMALTMHGQGKNAWQAEIDSAAELCDFFRFGVKYAEDLYAQQPVHHAPGVWNRVEYRPLEGFVYAISPFNFTAIGGNLAGAPALMGNVVVWKPSPSAIASNWLVHQILLEAGLPKNVIQFVPGEAEEVTKTVLDHPDFAALHFTGSTNVFRNLYGQISTRVAAGKYRSYPRIVGE... | Catalytic Activity: H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-glutamate + NADH
Sequence Mass (Da): 61936
Sequence Length: 572
Pathway: Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2.
Subcellular Location: Mitochondrion matrix
EC: 1.2.1.88
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O74766 | MSQFAEFKLPAIKNEPPKHYGPNSADREGIVKAYKELEAELPVTIPVIIDGKEVETNTIGEQRCPFEHKKVVARYHRAGAKHVEDAIEAALRGKKVWESLPFADRSAIFLKAAHLISTKYRYKLMAATMIGQGKNIWQAEIDAGMEIIDFLRFNTKYASELYASQPPENTPGVWNRMEYRPLEGFVYAITPFNFTAIAGNLAAAPLLMGNVVLMKPSDHAVLSSYIVYQIFREAGLPAGALQFIPGDAVEVSKVCFNHPEFAGLHFTGSTAVFRSLWGTIGENVANGKYRTYPKIVGETGGKNFHLVHSSAEIKSAVVNA... | Catalytic Activity: H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-glutamate + NADH
Sequence Mass (Da): 60219
Sequence Length: 548
Pathway: Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2.
EC: 1.2.1.88
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P07275 | MLSARCLKSIYFKRSFSQLGHIKPPKHIRNEPVKPFRNIDLKDWDLLRASLMKFKSSSLEVPLVINGERIYDNNERALFPQTNPANHQQVLANVTQATEKDVMNAVKAAKDAKKDWYNLPFYDRSAIFLKAADLISTKYRYDMLAATMLGQGKNVYQAEIDCITELSDFFRYYVKYASDLYAQQPVESADGTWNKAEYRPLEGFVYAVSPFNFTAIAANLIGAPALMGNTVVWKPSQTAALSNYLLMTVLEEAGLPKGVINFIPGDPVQVTDQVLADKDFGALHFTGSTNVFKSLYGKIQSGVVEGKYRDYPRIIGETGG... | Catalytic Activity: H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-glutamate + NADH
Sequence Mass (Da): 64435
Sequence Length: 575
Pathway: Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2.
Subcellular Location: Mitochondrion inner membrane
EC: 1.2.1.88
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Q9C9M3 | MTTTPDWIMIGGDGPESYNQQSSYQRALLEATKDKMTKAISANLDLDLISNRFIVADFGCASGPNTFVAVQNIIDAVEEKYRRETGQNPADNIEFQVLFNDFSLNDFNTLFQTLPPGRRYFSAGVPGSFFERVLPKESFHIGVMSYAFHFTSKIPKGIMDRDSPLWNKDMQCTGFNPAVKKAYLDQYSIDTKILLDARAEELVPGGLMLLLGSCLRDGVKMSETPKGTVMDFIGESLSDLAKQGVTEQEKVDTFRTSIYFAEQGEIRQIIEENGKFTIEAFEDIIHAKNEFPFDPKTLAISFKAFYGAFISAHFGVEVMR... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Methyltransferase that may methylate 1,7-paraxanthine . Prevents seed germination and modulates root architecture during early seedlings development . Plays a minor role in defense responses toward pathogenic bacteria (e.g. P.syringae) .
Sequence Mass (Da): 39780
Sequ... |
O04200 | MSDALINGLAGAGGGIIAQLLTYPLQTVNTRQQTERDLKREKRKLGTIEHMCQVVKQEGWERLYGGLAPSLAGTAASQGVYYYFYQVFRNRAEATALARKKKGLGDGSVGMFASLLVAAFAGSVNVLMTNPIWVIVTRMQTHRKMTKDQTAAPESPSSNAEALVAVEPRPYGTFNTIREVYDEAGITGFWKGVIPTLIMVSNPSMQFMLYETMLTKLKKKRALKGSNNVTALETFLLGAVAKLGATVTTYPLLVVKSRLQAKQVTTGDKRQQYKGTLDAILKMIRYEGLYGFYKGMSTKIVQSVLAAAVLFMIKEELVKG... | Function: Mediates the NAD(+) import into peroxisomes. Favors the NAD(+)(in)/AMP(out) antiport exchange, but is also able to catalyze a low unidirectional transport that might be essential under special conditions. Transports CoA, dephospho-CoA, acetyl-CoA, adenosine 3',5'-diphosphate (PAP), NAD(+), AMP, ADP and NADH, ... |
Q9Y7M1 | MSISFSELVAKTLLDLEVKVVFGIVGIPVIEICEAIQASGIRFVGFRNEQSAAYAATAYGYLTQRPGVCVVVGGPGVVHAMAGVFNSKTNRWPLLLLAGSSETFQQNCGAFQELDQVSYLSPHTKLAVRPPSPKMVVDSIRRAYRVSMTGTPGTCYVDLPANYIESTVDDFPKDPLPPIPSSPKCAPDPTQLQKAAYYLKNAKAPLLVVGKGAAYACAEKQLLEFVEHTGIPFLPSPMGKGLLPESHPLNVSSARSAALRNADVVLLAGARLNWIFQYGLPPKWSPNAKFIQIDTNAETLGNNAADLDLAIWADVGLTID... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes a carbon-carbon cleavage reaction; cleaves a 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde.
Sequence Mass (Da): 61937
Sequence Length: 568
Domain: Peroxisomal targeting signal 1 (PTS1) is a tripeptide located at the C-term... |
P39994 | MTTTATQHFAQLLQKYGIDTVFGIVGIPIVQLADTMVANGIKFIPCRNEQAASYAASAYGYISDKPGVLLIVGGPGLIHALAGIYNSMSNRWPLLVIAGSSSQSDIHKGGFQELDQVSLLSPFLKFTGKLTPDNIDMITQKALNYCIQGTAGVSYIDVPADFIEYEKPLEGNDRTGNELPMILTPNICGPDPSKIKKVVQLILQHKNKNILIVIGKGAVKNSHEIRRLVNTFNLPFLPTPMAKGIVPDSSPLNVSSARSQALKIADIVLVLGARLNWILHFGTSPKWNSESIFIQFDSNPETLGDNNVSPGADLSIWGDI... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes a carbon-carbon cleavage reaction; cleaves a 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde.
Sequence Mass (Da): 61288
Sequence Length: 560
Domain: Peroxisomal targeting signal 1 (PTS1) is a tripeptide located at the C-term... |
O74758 | MTHNTMLQRFNGLLEPTHLYIVSVVAYSACNRPDKISGIAKEAMEHVGPSIYPKLREALVKSSPLVGFPRTINSLREMTTNIPPPFPDEFARAADADIDTGKRGKIYFEKTYGKVTQRVLRSMQSSSLDLANIALDYAYGKVLSFNEVVSPLETSLMIIAALVPQDVNPQLRGHLKGALNHGATKEQVMSARNIALEISKECGIQFKGDIETL | Function: Probably involved in peroxisome formation or maintenance as well as in amino acid metabolism.
Sequence Mass (Da): 23489
Sequence Length: 213
Domain: Peroxisomal targeting signal 1 (PTS1) is a tripeptide located at the C-terminus of more than 95% of all peroxisomal matrix proteins. The prototypical PTS1 is the... |
P47148 | MNQILNAQRLIQLSQFHPKLKNIWYLVAAATFSVCNEPQEIPKLYHYAMLLSNDNAHMYRFTLASQTIDLLRSELPMRKTLINENYQQPTFFQKQLTAKFREVILKTGPLAGLPRAINGLTMLKETTPDILVPHLDPIDPWEAAMGNSSPLSETSMRRKHDKTIQERDHTIQNGLRHWNSIYNKVSTRVVNNLNSSYPDLWYYTLVHVYGPLFAFDEILSAQETSLVIIASLVPQDVNPQLRGHLKGALNIGCDKETVEAVRGLAILISQWCGVSWKSGVVKL | Function: Probably involved in peroxisome formation or maintenance as well as in amino acid metabolism.
Sequence Mass (Da): 32208
Sequence Length: 283
Domain: Peroxisomal targeting signal 1 (PTS1) is a tripeptide located at the C-terminus of more than 95% of all peroxisomal matrix proteins. The prototypical PTS1 is the... |
Q8U920 | MAAIDLNSDLGESYGAWRMGDDEAMLAIVSSANIACGFHAGDPAGIYRTVKAAAEKGVVVGAHVSYPDRVGFGRRDLDATSEELIADVIYQIGALKGVAAAAGTTVRYVKPHGALYNRIANDAKQGQAVIDGIKAIDPSLVLMGLANAPILDLARKAGLAVVAEAFADRAYTPEGQLVSRREAGAVLHDAAKIAERMVQLAREGTLEAIDGSIIKIEAQSICVHGDSPGAVAIAQEIRRRFEADGIAIRSFASDR | Function: Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
Catalytic Activity: 5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 26709
Sequence Length: 255
EC: 3.5.2.9
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Q89P49 | MKIGINSDMGEGFGNYRICDDEALMSIVSSANVACGFHAGDPIIMDRMVRLAKQKGVEVGAHPGLPDLLGFGRRVIQMDAAELEKHMVYQIGALQAIAANAGHRVTHVSFHAAMGNMVNADPDMADVVARAIATINRDFIVFSQPDAEIVRAARKVGLRTLTLFLADRAYDENGHLVSRKLPNSVVTSTEAVAERVKRFLDSGTVQTIEGKSIKVEARSILIHSDTPGSVNLAGTVRRVIEQGGGEVTPATVLLN | Function: Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
Catalytic Activity: 5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 27341
Sequence Length: 255
EC: 3.5.2.9
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Q9I626 | MTEVDLNSDMGEGFGPWTIGDGVDAAIMPLISSANIATGFHAGDPSSMRRTVEMAAEHGVAIGAHPGFRDLVGFGRRHIAAPAIELVNDMLYQLGALREFARLQGLSLQHVKPHGALYMHLARDEVAARLFVETLQRLEPELLLYCMPGSATWRIGRELGQPLVREFYADRDYDRSGSIVFTRRVAALDPQQVADKVLRACREGKVRTVEGEDLDIAFDSVCIHSDTPGALELVASTRARLEGAGIRIKAPR | Function: Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
Catalytic Activity: 5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 27559
Sequence Length: 252
EC: 3.5.2.9
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Q881H6 | MRIDLNADLGEGFGAWTMGEDEALMQLISSANVACGFHAGDPLIMDSTVRRAKALGIDLGAHVGFPDLQGFGRRRMNIELKELCAIVVYQLGALAGIATAAGYRVTHMSFHGALGNMAAADAELAGPLVKAVARFDPQMIISSSSSEAIEQAAQACNLRVATTFLADRAYDENCLLVPRGIAGAVVKDPEQVRARVAQLLQDGTVTTLSGKRVAVNAQSILLHGDTPGAVELARSIRHSIEEQGGVITPVSQLLGS | Function: Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
Catalytic Activity: 5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 26890
Sequence Length: 256
EC: 3.5.2.9
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B2GE66 | MTRIDLNSDLGESFGRYTIGNDDQVLDLITAANVACGFHAGDPDVMAQTVALAETKGVAIGAHPGFPDLGGFGRRKLDMTPAEVKNMVTYQVSALMGFTKDHRLHHVKPHGALYNAAAKDLALARAICEGVAQVDDQLPLYGLAGSQLLEAAKEVGLPAYSEVFADRGYQADGSLVPRSQPNAVLTDPLAVAERALSMVQTQSVTAVTGETVPLKVDTICVHGDNQAALALVDQLRQTFTANGITIQAC | Function: Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
Catalytic Activity: 5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 26271
Sequence Length: 249
EC: 3.5.2.9
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B9E7M7 | MYIDLNADLGESFGNYKIGNDEAIIPLITSANIACGMHAGDFNVLNQTIELCKAHGTGIGAHPGYPDLQGFGRRNLDMTYDEVENLITYQLGAIDAFCIKHGMKMNHVKPHGALYNATSGNEGLAEAIVNAIYNFNPELKVMGISGGTLVKATEAKGMTAINEVFADRNYTDAGTLVSRKQSNAMIHHQQAAVEHVLRMVRDNQVKTETGKLIDLRADSICVHGDGPEALAFVKAIIETLNNEGIKVQTI | Function: Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
Catalytic Activity: 5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 27043
Sequence Length: 250
EC: 3.5.2.9
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A4T5K5 | MSSVDLNADLGEGFGVWALGDDDAMLDIVTSANVACGFHAGDPATLRRVCEAAAARGVRIGAQVSYRDLAGFGRRFIDVSSEDLIADVMYQIGALSALAAAAGSSVSYVKPHGALYNAVVTNRLQAHALAAAVHAVDPALPVLGLAGSVFFGAAEELGLRTVPEAFADRAYRPDGRLVSRRERNSVLHDVDEIAERVISMVSRGRVHAVDGSTIPITVESVCVHGDSPGAVQIATAVRKRLVAEGVTLASFS | Function: Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
Catalytic Activity: 5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 26252
Sequence Length: 252
EC: 3.5.2.9
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B8ZUB2 | MACIDLNADLGEGFGVWRLGDDEAMLRIVTSANVACGFHAGDPAGLLRVCRLAAERGVRIGAQVSYRDLVGFGRRFIDVTADDLLADVVYQIGALQAIAQTAGSAVSYVKPHGALYNTIVTNREQGAAVAAAIQLVDSTLPVLGLAGSTFFDEAARIGLRTVAEAFADRTYRPDGQLISRREPGAVLHDPAVIAQRVVTMVTTGKATAVDGTQLAVTVESICLHGDSPNAIQMATAVRDQLNAAGIDIRAFC | Function: Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
Catalytic Activity: 5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 26453
Sequence Length: 252
EC: 3.5.2.9
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B2HJ17 | MPYIDLNADLGEGFGIWQLGDDDAMLGIVTSANVACGFHAGEPAGLLRVCRAAAERGVRIGAQVGYRDLAGFGRRFIDVDPEDLVAEVVYQIGALQAIAQSCGSTVSYVKPHGALYNTIVTHRDQAAAVAEAVQMVDATLPVLGMTGSVFFQQATDLGLRTVAEAFADRAYRSDGQLVSRREHGAVLADAAAIAQRAVSMVASGKVTAVDGTQVPITMESICVHGDSPGAVQIATAVRDRLTAAGNEIRAFC | Function: Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
Catalytic Activity: 5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 26337
Sequence Length: 252
EC: 3.5.2.9
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Q8WXC3 | MGTKREAILKVLENLTPEELKKFKMKLGTVPLREGFERIPRGALGQLDIVDLTDKLVASYYEDYAAELVVAVLRDMRMLEEAARLQRAA | Function: Associates with PYCARD/ASC and modulates its ability to collaborate with MEFV/pyrin and NLRP3/cryopyrin in NF-kappa-B and pro-caspase-1 activation. Suppresses kinase activity of NF-kappa-B inhibitor kinase (IKK) complex, expression of NF-kappa-B inducible genes and inhibits NF-kappa-B activation by cytokines ... |
A0A8F4NV97 | MLQEDKSSETMHDPSTRGVETRNVTAVDSPLETATTSESPETERTNVAPAKRDWRFWALLVSISLAGLLTALEGTITSTALPSIVNDLGGGHLYVWVVNGYLFAMTAMQPMYGQLANIFGRRWPMLGATALFVLGSGICGGATNIETLIAGRILQGIGASGTTVLTETIICDVVPLRERSKFLAIVMGMIFLGTALGPFFAGLIVQYSTWRWTFYLALPVGGAALVALFSFLKVKYQKETNLATKISTIDWAGNALFVAAISSVLIGLSWAGSVYAWSSFRVLVPLFVGIAGMGLFMVFEGSRFAPNPTVPLHLFGNRTS... | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of pyrrocidines, fungal natural products containing a macrocyclic para-cyclophane connected to a decahydrofluorene ring system that show potent antibiotic activities toward Gram-negative bacteria.
Location Topology: Multi-pass membr... |
A0A8F4NVX8 | MSSTMRGWVRQHRGPYESSLKLIDSLPVPPDPGSDSSDIIVRVSYVALEFSIAHIMGIFPALPFAPPLVPEICVSGTVASAGGKAPEELRQPGTQVLAMTDPMSMMLFGTGALKEYMRLPEQYVVPLLQPSHSVTTDHPHGTAERPQALTLAEGAGLISNGSAAQAVVRAANVLSGQRVLVNGASGSVGHIVSQLCRARGAYVVGVASGVNQDFVRRYGCNEFVDYTKHTDLPEYLASTYGSQPFDSILDCVGSQDLYANSPRYLLPGRPLVNIGAFSMTDSLLSTLYQWSMNSWCPTWLGGVPRPYILFSNTPDMQGVL... | Function: Medium chain reductase; part of the gene cluster that mediates the biosynthesis of pyrrocidines, fungal natural products containing a macrocyclic para-cyclophane connected to a decahydrofluorene ring system that show potent antibiotic activities toward Gram-negative bacteria . Within the pathway, pydE functio... |
A0A8F4NUC6 | MATPGNVTFKNTHDSWGMNWGLCDSSEQMLTMQGMPWIMRKLASWISVTVVIKTWTDPETGETRFLLQHNPPMGLPGMSEERALDYVPDELTVPNLGKLRVRTRWGTAKELDQLDKYLARGLEKGPHSMIHMMTEHLDIDAVTHQIFGYEEIDGTRYHVRRIVVRKGHEVARLRLVYNYLGPRAG | Function: Pericyclase; part of the gene cluster that mediates the biosynthesis of pyrrocidines, fungal natural products containing a macrocyclic para-cyclophane connected to a decahydrofluorene ring system that show potent antibiotic activities toward Gram-negative bacteria . Within the pathway, pydY is involved in the... |
O30130 | MMRHLISIGDLDREDINYILKKAEEFEDVARGEKKLRILEGKILGNLFFEPSTRTRMSFETAMKRLGGDVINMTAQEASSIAKGETLADTIRVVSGYCDAIVIRHPLEGAARFAAENSSVPVINAGDGAGQHPTQTLLDLYTIKKECGRLDGITIALMGDLKYSRTIHSLIKALALFDMRIYLISPEALALPEDIIEDVSAEIRRARLEEVISEIDVLYVTRIQKERFPDEEEYRKVSGSYRITAETLKSAKDSMIVMHPLPRVDEIHPSVDSTKHARYFQQSFYGVPVRMAILSEVML | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 33634
Sequence Length: 299
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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A0JX76 | MKHLLSTEDLSLANAIRILDTAEEMAAVGDREVKKLPALRGRTVVNLFFEDSTRTRISFEAAAKRLSADVINFAAKGSSVSKGESLKDTAQTLAAMGADAVVIRHWASGAPHRLAATDWIDAAVINAGDGTHEHPTQALLDAFTMRRHWARLHGTPSAGADLKGMRVAIAGDVLHSRVARSNVWLLRTLGAEVTLVAPPTLLPIGVGQWPCSVSYDMDETLAKGVDAVVMLRVQGERMNASFFPTTREYSRRWGFDDNRLRALDSLGLKDTIIMHPGPMNRGLEISSAAADSPRSTVLAQVRNGVSVRMAALYLLLSGDT... | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 36429
Sequence Length: 337
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
|
Q2GGK2 | MKTLLEVSNLTSDDIESIFNLTIQYFNNTNLNHNILTGKVIVNLFFESSTRTLSSFEIAEKSLGAHSITLNINTSSINKGESIIDTISNIDAMNPDLIIIRSQYSQFIKKISEYLPSCSIINAGDGHHEHPTQALTDYCTIRYIKKDINNLNISICGDILHSRVARSNIRLLSRYGANISLVAPPTLSCNLTGISHIYHNLIEGIRNADVIMLLRLQKERIINCVIPSEQEYSHLYMLNHEKLLHAKKDVIVMHPGPTNKGIEISNNVAEKNSVILLQVKMGVAARKAILHYLLYNKSI | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 33550
Sequence Length: 299
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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A6H0I8 | MKELSVNNLLGIKYINENDINLVFETADHFKEVINRPIKKVPSLRDITIANIFFENSTRTKLSFELAQKRLSADVINFAASSSSVTKGETLVDTVNNILSMKVDMVVMRHASPGAAVFLSKNVKASIVNAGDGAHEHPTQALLDAYTIREKLGDVAGKKIVIVGDILHSRVALSNIYSLQKLGAEVRVCGPKTLIPKYIEALGVKVEPNLRKALEWCDVANMLRVQNERLDISYFPSTREYAMQYGLDKNLLDSLNKEIVIMHPGPINRGVEITSDVADSRQSVILNQVENGVAVRMAVIYLLASKIK | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 34072
Sequence Length: 308
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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Q2J833 | MGSTSRVRGTGVNRHLLSTEDLDRDDALLVLDTAERMARVAEASVRKLPTLRGRTVVNLFFEDSTRTRTSFEVAAKRLSADVINFSARGSSVSKGESLKDTAQTLEAMGADAVVCRHAASGAPHRLASWVRGSVVNAGDGTHEHPTQALLDAFTMRRRLGRIDGLAVTIVGDVLHSRVARSNVWLLATLGATVTVVAPPTLVPLGISSWPVEVSYNLDAVLPKSDVVMMLRVQRERMSAAFFPTEREYSRRYGLDADRAEMLPDHALVMHPGPMVRGMEIASRVADSARSTVVEQVANGVSVRMAVLYLLLGGSGEVS | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 34343
Sequence Length: 318
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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B9M4S3 | MAFKHKDIIGLQDLTREEIELLLSTAENLKEINSREIKKVPTLRGKTVVNLFYEASTRTRTSFEIAAKRLSADTINITASTSSVTKGETLSDTARNVLAMNPDIIVMRHAVSGAHHYLAKRVSCSVINAGDGAHEHPSQGLLDMLTMRQQFGKLEGLKVAIVGDITHSRVARSDIYGLTRMGANVFLAGPPTMMPPGIERLGNVTVCKDMREAVADADVVMMLRIQLERQGKTLLPTMKEYSRYFGLNQSVLKLAKKDAMVMHPGPINRGVELSSDVADGSQSHILKQVENGVAVRMSMLYHVSGGELPTE | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 34095
Sequence Length: 311
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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Q59711 | MTPIDAKRPLQLNDQGQLRHFLSLDGLPRELLTEILDTADSFLEVGARAVKKVPLLRGKTVCNVFFENSTRTRTTFELAAQRLSADVISLNVSTSSTSKGETLFDTLRNLEAMAADMFVVRHSDSGAAHFIAEHVCPDVAVINGGDGRHAHPTQGMLDMLTIRRHKGSFENLSVAIVGDILHSRVARSDMLALKALGCPDIRVIGPKTLIPIGIEQYGVKVYTDLAEGLKDVDVVIMLRLQRERMAGGLLPSEGEFYRLFGLTTARLACAKPDAIVMHPGPINRGVEIESAVADGKHSVILNQVTYGIAVRMAVLSMAMS... | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 36410
Sequence Length: 334
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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Q4FUA5 | MSNSIDSQSIPTISPTDYTKFDPDTIHEKLDASLSRPQLNTDGSIRHFLGIEGLNKAQLRAIIAKAETFFDDKGQLINRPELEGYTVMNLFFEPSTRTRTTFEVAEKRLGANVLNIDIERSSTKKGESLRDTLWNLQAMTADIFVVRHSASGAAHFMATEVTPDIAIINGGDGWHAHPTQGMLDMLTIHREAPRPFEELSVAIVGDIKHSRVARSDISALQTLGVKDIRVCAPRTLLPKGIERFGVQVYENMNECVTDCDVIMGLRIQNERIGSPLLASSSEYYKHYGITPERMALAKPDAFVMHPGPMNRGVEIASSVA... | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 39238
Sequence Length: 357
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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Q9PBB8 | MNLKAITLMQFDSNGRLRHLLTLEGLSRDTLLQLLDCAAQNCALGVDPMGKRNVLAGMAVCTLFFEPSTRTRHSFHLAAQRLGADVLNFDASMSSTSKGESACDTLKNLEAMGVRGFIVRHPEEIVIAQLAAVVGEGTVLINAGAGRSTHPTQALLDMLTLCQAKGNDFSKLKLLFVGDIKHSRVARSNLHALRTLGAGQIRVCGPTALLPHDGLLSGCVVSQDFDAMLEGVDVLMMLRLQRERMEEGLVPSLEHYHANYGLTAARLARAAPDAVVLHPGPINRGVEITDEVADGPQSWILRQASNGVMVRMAVLETLLG... | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 34637
Sequence Length: 322
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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O81355 | MASKSQILFIGGTGYIGKFIVEASAKAGYPTYVLVREASLSDPAKSKVIENFKALGVNFVLGDLYDHESLVKAIKQVDVVISTVGHGQLADQGKIIAAIKEAGNVKRFFPSEFGNDVDRSHAVEPAKSAFETKAKIRRAVEAEGIPYTYVSSNFFAGYFLPTLNQPGASSAPRDKVVILGDGNPKAIFNKEDDIGTYTIRAVDDPRTLNKVLYIRPPANTISFNELVSLWEKKIGKTLERIYVPEEQLLKNIQEAAVPLNVILSISHAVFVKGDHTNFEIEPSFGVEATALYPDVKYTTVDEYLNQFV | Function: Oxidoreductase involved in lignan biosynthesis . Catalyzes the NADPH-dependent reduction of phenylcoumaran benzylic ethers . Converts dehydrodiconiferyl alcohol (DDC) to isodihydrodehydrodiconiferyl alcohol (IDDDC) .
Catalytic Activity: (-)-dehydrodiconiferyl alcohol + H(+) + NADPH = (S)-isodihydrodehydrodico... |
A5D1A4 | MKLLIKGGTVVDPVAGKIEEKDVFIVDGKIARAGAHVNTAGAEVLDASGKLVVPGLIDMHVHLREPGFEARETIYTGTRAAARGGFTSVACMPNTSPVADNGAVISFIKACGLKGAVNVYPIGAITRGSKGEELAEMGDMKEAGAVAFSDDGMPVMNAGLMRRALQYAGMLGMVVISHCEDKNLSAGGVMHEGYVSTMLGLKGIPASAEEVMVARDILLAEETGSRVHIAHVSTAGSVRLIREAKARGVRVTAEVAPHHFTLTDEAVLGYDTSTKVNPPLRSAGDVAAVREGLADGTIDVIATDHAPHTEEEKDVEYDLA... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Catalytic Activity: (S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate
Sequence Mass (Da): 44760
Sequence Length: 427
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pa... |
A8MIU4 | MTRRNMGVHIAGIQLKNPVMTASGTFGSGREYSEFVDLNQLGAVVVKGVANEPWSGNPTPRIAETYGGMLNSVGLQNPGVEAFIKDDIQFLRQYDTKIIVNIAGRTVADYCKVTEKLGDADIDLIELNISCPNVKAGGVNFGTNPAMVEEVTKAVKKVARQPLIVKLTPNVTDIVEIAKAAVAGGADAISLINTLLGMAIDIHGRKPILANVVGGLSGPAIKPVALRMVYQVANAVQVPIIGMGGIATGEDAIAFMLAGATGVAVGTANFMNPRATMEVLEGIEDYMDQYNIEDIHEIIGKL | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate
Sequence Mass (Da): 31887
Sequence Length: 302
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway... |
O29513 | MNPLETEIGGLRMKNPLMLASGIMGSKVHSLNLIARDAGAVVTKSVGVEEREGYRNPTVVNWKCGLINAVGLASPAAKDFAEELKDYTNEAPLLISLYGHSVEEFSDLVDTFDSALPYLHGYELNLSCPHVKGAGLDIGMDLELSAAIVEELKGKTKNPVFAKLSAMHDYLKLAKVLEDAGVDGITISNTLRGMKIDIMSGKPVLSNLSGGVSGPAIKPIALKCVYDLYKEIEVPIVGCGGITSFEDVLEFIMAGARAVQIGSAVYYSRRIFYSLKESLIAFTRARDCTISDLIGIAHS | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate
Sequence Mass (Da): 32114
Sequence Length: 299
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway... |
B6YRL9 | MADLNINIGKLKFKNPVLAASGTFGYGIEYSDFVDLSKIGGIFTKGITLYHREGNDYPRMAETSSGMLNAVGLQNRGVTYFIKNIYPKVKNIETNIMVNISGSTIEDCVSCAEKINELDKIPAIELNISCPNMKQGGMAFGTNCSNASEIVNAVRKVYHKILIVKLSPNVTDITEIAKAVEIAGADAVSLINTLIGMAIDIKIKKPILSTVTGGLSGPCIKPIALRMVYQTYKIVKIPIIGLGGISNSDDAIEFILAGASAIQVGTYNFIDPTISTKIVDGINAYLDKYHLLSIKELVGELL | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate
Sequence Mass (Da): 32512
Sequence Length: 302
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway... |
P57443 | MFYYFIRKLLFLLEPEKAHFLTLKYLNIKNIQFFDFFFYKTIILSKKIKCMGLIFDNKLGTAAGIDKNGEYIDALSKLGFGFIEVGTVTPLPQVGNPKPRMFRIVSMEGIINRMGFNNLGIDNLIRNIKKSNFKGIIGVNIGKNKSTSLENSVDDYLICIEKIYCYAGYIAINISSPNTTNLRNLQYGILFKKLLYKIKKKQKELHKKYLKYVPIAIKISPDLSIKELVDISKQLIRYKIDAVIATNTTLDHSSLFGLKNSSEQGGLSGLPLQKKSTNTISILSKSLQKKIPIIGVGGINSINSAKEKIESGATLIQIYS... | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37955
Sequence Length: 337
Pathway: Pyrimidine ... |
Q92S77 | MIGQLEHLARRGLFLFDPEAAHGLSIKALKSGLVPSCAAPADPRLGQTVAGLVFSNPIGMAAGYDKNAEVPEALLKIGFGFTEIGTVTPRPQAGNDKPRLFRLVEDEAVINRLGFNNEGHGAALARLKACSREALIGVNIGANKDSADRIADYVTGIRTFYAVARYFTANISSPNTPGLRDLQARESLSALLSAVLAARDDEARKGGRQVPVFLKIAPDLTEEGMDDIAAEVLAHGLDGLIVSNTTLSREGLKDRRQANEAGGLSGKPLFEKSTAVLARMRKRVGPHLPIIGVGGVCSAETAAEKIRAGADLVQLYSCMI... | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38635
Sequence Length: 362
Pathway: Pyrimidine ... |
Q07TQ6 | MIRAFDALSLPLLRLLDPEDAHRLAIQGLRLLPQAAPPADQPNLSVRAFGLNFSNPVGIAAGFDKNAEAPDALLRMGFGFVEIGTVTPKPQSGNPRPRLFRLERDEAVINRMGFNNDGGEVVLRRLAARSARGGIVGVNVGANKDSEDRVADYVRLIEMFAPVASYFTVNVSSPNTPGLRNLQQAAALDDLLAKVIEARERVRAIAGDTPVLLKIAPDLTLNELDDVVHIARSRKVDGMIVANTTLSRTHTLREQARAKEQGGLSGRPLFRLSTRMVAETYVRAEGAFPLIGVGGIDSGGAALTKIRAGASLIQLYSALI... | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39111
Sequence Length: 364
Pathway: Pyrimidine ... |
Q2RX27 | MADWYRLAWPLICGLDPERAHHLAIRALALGLAGHDRAADDPVLACSLWGRRFANPLGLAAGFDKNGEVADALFDLGFGFVEVGTVTPRPQAGNPRPRLFRLTQDRAVINRMGFNNQGMEAMAARFVRARPRGVLGINLGKNKTTEDAAGDYEAGIAKLAPLADYLVINVSSPNTPGLRALQGREPLSLLIARARAALDAACPGLRPPLLLKVAPDLTDEDMADIAEVALGGGLDGLICTNTTIARPKSLVSDHAGETGGLSGLPLRYRARQVIARLYGLTKGALPLIGVGGIGDGAEAYARIRAGASLIQIYSALVYEG... | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38648
Sequence Length: 367
Pathway: Pyrimidine ... |
A7NLW9 | MLYHLIRPLLFRLDAERAHDVVTAMFRATSRMPLLPRLISALYAWDDPALMVEWAGLRFASPLGVAAGFDKRADLVDALALLGFSHVEVGTVTPRPQPGNPGPRLFRLPEDMALINRLGFNSHGMVAVAKALRARRSRRVIVGVNIGKNRDTPLERAVEDYAATFVALAPLADYVAVNISSPNTPGLRRLHERAALEELLRELMRLNHGLLYPRPIALKISPDETLDQIEEVVRAGCEAGVAAFIATNTTLAREGLRSRLANETGGLSGRPLAPRARQVIRAIYRLTRGTPPVIGVGGVLTADDAYAHIRAGARLVQLYT... | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40043
Sequence Length: 367
Pathway: Pyrimidine ... |
A5UX75 | MTSLYALIRPLLFRLDAERAHDLTAKALRVTSRAPLLPRLIRALYAWEDPLLAVDWSGLHFANPVGVAAGFDKRADLVDGLALLGFGHIEVGTVTPRPQPGNPRPRLFRLPEDTALINRLGFNSPGMVAVARALRARRSRDVIVGVNIGKNRDTPLERAVEDYVATFVALAPIADYVAVNISSPNTPGLRRLHERAALETLLHELTRLNRALPHPRPIALKVSPDETPDQLEAVVRAGCDAGIAAFIATNTTLARDDLHSRLAIETGGLSGRPLTQRARQVIGAIYRLTHGAPPVIGVGGIATAEDAYQHIRAGARLIQI... | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39052
Sequence Length: 361
Pathway: Pyrimidine ... |
Q7WEU9 | MSASASTAADFVRFALDEGVLRFGSFKVKSGRISPYFFNAGLFNSGRSVGALAGFYAQALVDSGVAFDMLFGPAYKGIPLATATSVALAGHRAMAGRDVPFAFNRKEAKDHGEGGTLVGAPLTGKVVIIDDVITAGTSVRESVEIIRAAGAEPAAVLIALDRMERAGPDDALSPHSAVQDVARTYGIPVVSIASLADIMTLLQDDAQFAEHREAVQAYRSKYGV | Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 23428
Sequence Length: 2... |
Q89BL4 | MSKSASRARLFEIIRRRSFGRGEVTLASGRKSDFYFNLKPTMLDPEGATLLAELTYEALKDDNLDFIGGLEMGAVPLAGALAQISWIKGHPIAAFFVRKKPKEHGAKLAIEGLPRGETLQGKRVVIVEDVTTTGGSAMKAVESVRETGAEVVLVLTMVDREEGATDTFGAAGLPFRSLYKASEFLKA | Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 20219
Sequence Length: 1... |
Q8Y342 | MSQNSELRQSFIRFAVEAGVLSFGEFVTKAGRTSPYFFNAGKFSDGALLGQVAQFYAKTLLDSGVQFDMLFGPAYKGITLASATAVALAGMGRNVGFAYNRKEAKDHGEGGSLVGAKLQGRVVIVDDVISAGTSVRESVELIRNAGATPAAVLILMDRMERSGNAVDIGERSAVQDVQAQYGMPVVSIANLDDLLGYLDHAGDPALAGYRAKAAAYRDKYGVSAVV | Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 23827
Sequence Length: 2... |
P42719 | MIQTTFPDRAVMAELLAKMLWEIKAVHFNAAQPYKLASGMASPVYIDCRKLLSFPRIRSTVMDFAASTLLRDAGFEQFDCIAGGETAGIPFAALLADRLGLPMIYVRKQPKGHGRNAQIEGNMPEGSRVLVIEDLTTAGGSMFKFIDAVRAAGGIVDHGIALFFYGIFGEQRFADGKVRLHHIATWRNVLPSPGSRSSSTTRRCRKSSPSSMRRWLGRERMVA | Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 24623
Sequence Length: 2... |
Q92SC6 | MFSNAFTDKAVMAELVAKMLWEIKAVHFRADEPYRLASGMASPVYIDCRKLVSYPRIRSAVMDFAAATILREAGFEQFDVVAGGETAGIPFAAMLAERLGLPMIYVRKAPKGHGRNAQIEGYMPEGARVLVIEDLTTAGGSMFKFIDAIRAAGGVVEHGIALFYYDIFPEARGNMKSKGVDLHYIATWRNVLAVARELALFDEKTLNEVEAFLNAPLDWSGRNGGVRALAVQ | Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 25466
Sequence Length: 2... |
A5VD53 | MTDEQVLAEFRAAEALLEGHFILSSGLRSSRYLQCARVLMNPARAARLAEALAFKIPDKLKIQLGSVVSPAMGGVIAGHEMGRALGLDAMFVERPDGVFHLRRGFRLEPGQKVLLMEDVVTTGLSSREAIKAVEEAGGQVIAAAALVDRSNGTADLGVPFYPLIRLDVPTYQPESLPPELAAIPAVKPGSRAAVAA | Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 20811
Sequence Length: 1... |
Q7UYX5 | MSSDSANRDLAPLIALMETEALQRGEFTLASGKKANYYLDCRRVTLHPKGACLIGRAMLDVVLANAKESGVMPAAVGGMAIGADPITASIVTLAGGDDVDLKGFMVRKEPKGHGMGQQVEGPVTPGQKVVIVEDVITSGGSALKAVEAVQAFGLEVQYVLAIIDRLAGGAEAFAQKGLELKTLTTIRDFGLEP | Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 20109
Sequence Length: 1... |
Q757S1 | MSTKSYAERAKAHNSPVARKLLALMHEKKTNLCASLDVRTSRKLLELADTLGPHICLLKTHVDILTDFDIETTVKPLQQLAAKHNFMIFEDRKFADIGNTVKLQYSSGVYRIAEWADITNAHGVTGPGVIAGLKEAAKLASQEPRGLLMLAELSSQGSLARGDYTAGVVEMAKLDKDFVIGFIAQRDMGGRADGFDWLIMTPGVGLDDKGDGLGQQYRTVDEVVSDGTDVIIVGRGLFDKGRDPNVEGARYRKAGWEAYLRRIGETS | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 29210
Sequence Length: 267
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
O13410 | MSSKSQLTYGARASKHPNPLAKRLFEIAEAKKTNVTVSADVTTTRELLDLADRLGPYIAVIKTHIDILTDFSVDTINGLNVLAQKHNFLIFEDRKFIDIGNTVQKQYHGGALRISEWAHIINCSVLPGEGIVEALAQTASAQDFPYGPERGLLVLAEMTSKGSLATGEYTKASVDYARKYKNFVMGFVSTRALTEVQSDVSSASEDEDFVVFTTGVNLSSKGDKLGQQYQTPASAIGRGADFIIAGRGIYAAPDPVEAAQRYQKEGWEAYMARVCGKS | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 30267
Sequence Length: 278
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
P07817 | MSSKSQLTYTARASKHPNALAKRLFEIAEAKKTNVTVSADVTTTKELLDLADRLGPYIAVIKTHIDILSDFSDETIEGLKALAQKHNFLIFEDRKFIDIGNTVQKQYHRGTLRISEWAHIINCSILPGEGIVEALAQTASAPDFSYGPERGLLILAEMTSKGSLATGQYTTSSVDYARKYKNFVMGFVSTRSLGEVQSEVSSPSDEEDFVVFTTGVNISSKGDKLGQQYQTPASAIGRGADFIIAGRGIYAAPDPVQAAQQYQKEGWEAYLARVGGN | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 30196
Sequence Length: 277
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
Q9P8X9 | MSRHATITQSYQERASLPKTSPVASYLLRLIAAKKTNLCVSADVSTTRELLQLAEEVGDSICMLKTHADIINDFGPRTIEGLKEIAAKKHFLVFEDRKFGDIGSTVQKQFTAGPLQIVRWANIINAHIFPGPAIITALSQARPRCRQLLILAEMSSAGNLMTGSYTEQCVVEARKNPEFVMGFIAQRTLNEQPGDNFITMTPGVQIGATGDGLGQQYNTPEKVIGEAGTDIIIVGRGVYGAQDKRAKAEEYRVRAWKAYEGNWRCYCNKR | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 29840
Sequence Length: 270
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
Q39VY5 | MTRDQAREKVIFALDTGEFAHVQYWAETLSDKVGMYKIGKQLFTACGPAAVRMIQKFGGEVFLDLKFHDIPNTVAMASVEAARMGVKLFNLHALGGYEMMAKTVEALDKEFKGGDRAKVLAVTILTSSTEETLKDLGIEHTVPDMVVRLATLARKAGIDGVVASPREIPLIREACGSDFLIVTPGVRPSFAALNDQKRVMTPAEAVKAGSDYLVIGRPIGDAPDPAAAAELILGEIVAG | Function: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 25631
Sequence Length: 239
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC... |
Q74D58 | MTRDQAREKVIFALDSSEFAHVQYWAETLSDRVGMFKVGKQLFTACGPATVRMIQKFGGEVFLDLKFHDIPNTVAMASLEAARLGVKLFNLHALGGYEMMARTVEALDKEFKGGERAKVLAVTILTSSTEETLRQVGIESPVEEMVVRLATLARKAGIDGVVASPREIPLIREACGPDFLIVTPGVRPAFAALNDQKRVMTPAEAVRAGGDYLVIGRPIGDAPDPAGAAEMILDEIMAG | Function: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 25818
Sequence Length: 239
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC... |
A5G5A2 | MTRDEARAKVIFALDVHEFSDVEQWADMLAPHVGMFKVGKQLFTSCGPAAVRMIQKCGGEVFLDLKYHDIPNTVAMASLEAARMGVKLFNLHALGGYEMMAKTVETLDKEFKGGERGKVLAVTILTSSNEQTLQDVGINIPVPEMVVKLALLARKAGIDGVVASPQEVPLIRKACGKDFLIVTPGVRPAFASSDDQKRIMTPAEAVRTGADYLVIGRPIAAAPKPVEAAEAIIDEIMAVEG | Function: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 25932
Sequence Length: 241
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC... |
Q7NK22 | MGGAERVIVALDLADAQAARALVERAPAVRFWKVGLELFTAAGPGLIEWLKARGCRVFLDLKFHDIPNTVAGACRAATRLGVDLLTVHATGGQPMLMAAVSACTGEAARLGSPAPAVLAVTLLTSLDAQLLEQQLLVNVGVSGYVEHLAVLAVSSGVQGVVCSPLETALLRERCGNDFLIVTPGIRPGGSGEGDQRRTLTPGEAFARGADYLVVGRPVTTAPDPQVAFKAIVAEVGG | Function: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 24470
Sequence Length: 237
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC... |
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