ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9CF79 | MSVKNGLVQLENLTSMEKLSVDEVMGLIKRASAFKAGTAEFDLEKQTFASNLFFENSTRTHHSFHIAERKLGLDVLEFDAQASSISKGETLYDTVLTLDALGVDICVIRSGVEHYYEELVNSDNIHCAIVNGGDGSGQHPSQCLLDLMTIYEEFGKFEGLKIAISGDLTHSRVAKSNMMMLQKLGARLYFTGPAAWYSEEFDDYGHYANLDRILPELDVHMLLRVQHERHDSGESFSKEGYHNHFGLTEERAKMLKPTAIIMHPAPVNRGVEIADSLVESPQSRIVQQMSNGVYTRMAILEAILAGKKAK | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 34558
Sequence Length: 310
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
|
P77883 | MKTSQNLVSVEQFSNQDVMAYLKLAQAFKNGKTVQLSQPTFAMNLFFENSTRTHTSFEMAERRLGLQVIPFDPKTSSVTKGESLLDTLKTIEAIGVNLAVVRHPRDRYYQPLLDAGFDMSLINAGDGSGQHPSQSLLDMLTIYEEFGHFDGLKIAIVGDLAHSRVARSNMALLTQLGAQVYFGGPKEWYGRDFEAYGEYQTMDQLVATMDVMMLLRVQHERLSQVNNQTFDASAYHQQYGLTAERAARMPKHAIIMHPAPVNRGVELASDLVEAPQSRIFQQMTNGVYIRMAMVASVLAHQGLISATQVEV | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 34712
Sequence Length: 311
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
|
Q5ZXZ2 | MKHFLEISQLSSEQIESLLQRALYFKHTKQYPSYSQSIIANLFYENSTRTRISFELAERHLAMSVVNLDLQTSSETKGEAIEDTIRTLAAMGIQYFVIRHKQDGLQQNLANKLGDTVNIINAGDGTHAHPSQAILDMVTIIEQKKRLDKLKIAILGNIKHSRVANSFQCICSKLGVGELVLISPEIWQPSQVHFGRVTDNLNEGLEGADVVICLRVQKERLLQDDHLDLDFYRNNFALTQKSLSYAKPDAMVMHPGPMNRGVEIDSEVADGNQSCILQQVTNGVYARMAILESLIAS | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 33296
Sequence Length: 297
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
|
Q7UNR3 | MDASLSPDQLSFPAVWRHPHLLDLERLTAAEILAVLRTADQLKTMTEGCRRKVPLLTGKTCANLFFENSTRTRNSFSLAAKRLGADTVEFSSSGSSVAKGETFVDTAKTIEAMGVDWVVTRHSTPGTPHLLARELDCCVLNAGDGPHEHPTQGLLDMLTILQHRIGSDWKNEAADPEKVFAGMTVALVGDIAHSRTARSNLWGLRKLGAHVIICGPPTLVSHRWEELGFEVAHRLDEIVHRCDVLNLLRIQFERQKARPFPSVYEYAALYAMNGERLRLAKDDILIMAPGPINRGVEITPEVADGPHSVILEQVTNGIAV... | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 37676
Sequence Length: 343
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
|
A7NLW6 | MSVPAAAGAARHRRRHVLDLDDFSAQEIDEILETAVSMKEVLGRAIKQVPTLRGKTIVNMFFEESTRTRISFELAGKALSANVVNFTARGSSVEKGESLIDTVRTLQALGADMLVMRHSESGAPYLVAQHFHGSVINAGDGRHAHPTQALLDLFTVRQRLGRIEGLKVVIVGDILHSRVARSDLWGFTRMGALVTLCAPQTLIGPEAFWKATWPDLTITSNLDECVRDADVIMTLRLQKERMEAGLLPSLREYTRFFAITAERVARAAPHCLVMHPGPMNEGVEIMPDVAVSAQSVIEEQVANGVAVRMALLYRLSGE | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 34903
Sequence Length: 318
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
|
Q163C5 | MTFPHRHLLGIEALRPEEINTLLDLADKYAALNRQPDKHADALKGLTQINMFFENSTRTQASFEIAGKRLGADVMNMAMQASSVKKGETLIDTALTLNAMHPDLLVVRHPQSGAVDLLAQKVNCAVLNAGDGRHEHPTQALLDALTIRRAKGRLHRLSIAICGDIAHSRVARSNIMLLGKMENRIRLIGPPTLMPSGISEFGVEVFNDMNAGLKDVDVVMMLRLQKERMDGGFIPSEREYYHRFGLDADKLSNAKPDAIIMHPGPMNRGVEIDGTLADDINRSVIQDQVEMGVAVRMAAMDLLSQNLRLTRGAE | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 34628
Sequence Length: 314
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
|
Q1AVY6 | MGARDFLTLEGCDRGELREILELAAGCEAGRMDGALAGKTVCLAFFEASTRTAVSFELAARRCGADVISLSERGSSISKGESLVDTVVTLDRLGADAIVLRHPAAGAARLAARFAAAAVVNAGDGCGQHPTQALLDLYSLSRSVGGFEELAGVRAAVVGDILHSRVARSVIPAFRAAGVELALVAPRTLLPVEAGVWGLPVLSSVDEALEWGASVLYMLRLQRERMTGARVPSVAEYARYYAVGRRHLEAGVRVMHPGPVNRGVEIAGDVVLDGASLIPDQVAAGVAVRSAVLALATGVAQEVAA | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 31620
Sequence Length: 305
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
|
P25995 | MSYLIKNGWILNENGEKTQADIRVTGETITAIGKLDATDNETVIDAKGLLVSPGFVDLHVHFREPGGEKKETIETGAKAAARGGYTTVAAMPNTRPVPDTKEQMEWVQNRIKETSCVRVLPYASITIRQIGDEMTNFEALKEAGAFAFTDDGVGIQTAGMMYEAMKRAAAIDKAIVAHCEDNSLIYGGSVHEGTFSKANGLNGIPSVCESVHIARDVLLAEAANCHYHVCHISTKESVRVVRDAKKAGIRVTAEVSPHHLLLCDEDIPGLDTNYKMNPPLRSPEDRAALIEGLLDGTIDFIATDHAPHTEEEKNTEMKLA... | 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): 46533
Sequence Length: 428
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pa... |
P57416 | MSKFVKKIKIIKPDDWHVHLRDNEILNQVIKYTGKFYKRAVIMPNLNSPITSCLKSIAYRNRILKSMHLNYKFKPLMTCYLTNSTSPKELEFGFSKKIFVAAKFYPNGCTTNSKTGIKKISDITPVLECMEKIGMPLLIHGEEINQNIDIYDREAKFIEKTLDPLRKKFPKLKIVLEHITTKESVEYIKNNDVNYLSATITPHHLMLNRNDMFYGGIQPYLYCLPILKKNKHRMALRKAISNGDKHFFLGSDTAPHLHKNKINMLGCAGIFNAPSSLLSYVKVFEEMRALKYLQSFCSENGPKFYNMPINKETITIIKKP... | 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): 40416
Sequence Length: 350
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pa... |
Q8R9R6 | MRIVIKNGIVIDGFGGEEKADILINYGIIKGIDKNIDVSDAIVIDAEGKYVLPGFVDMHTHLRQPGFEEKETIRTGTESAAAGGFTTVACMPNTNPPIDSEVVVEYVKAVAQREGVVKVLPIGAMTKGMKGEEITEMAKLKKAGVVALSDDGFPIMSAGIMKRVMTYGKMYDLLMITHCEDKTLSGEGVMNSGIIATMLGLKGIPREAEEVMLARNIILAKATGAKLHIAHVSTKGSVELIRRAKEEGVSITAEVTPHHLTRTDEAVYNYDTNTKVFPPLRTREDVEALIEGLKDGTIDAIATDHAPHTKDDKKVPYDMA... | 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): 47024
Sequence Length: 431
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pa... |
Q3AC01 | MGMLIKNGNVVMVEDGKIRKMDVLIDKGIIVEISPEINRSDVEVIDIEGKFLIPGLIDMHVHFRDPGYTHKEDIHSGSNAALAGGFTGVLMMPNTDPPPDNATVIYYWKEKSKSIPLNILFSGCITKNRAGKELSKFYELKEAGAVAITDDGNWVADGAVFRHAMEYAAALDLLVITHPEEPTIANRGVINEGYWSTVLGLRGIPKAAENIAIYRDIEIAKMTGAKLHVAHLSTAEGVRLVAAAKKLGLKVTAEVTPHHLVLTDEALAGYDTNLKVNPPLREAEEQKALLKGLLEGVIDVIATDHAPHASYEKNVEFNDA... | 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): 47093
Sequence Length: 430
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pa... |
Q9UTI0 | MSLKIPGLADMHVHLRQDNMLKAVVPTVAEGGVSVAYVMPNLIPPITTVDACLQYKKEIEQLDSKTTYLMSLYLSPETTPEVIYEAAKKGIRGVKSYPKGATTNSESGVESYEPFYPTFAAMQETGMILNIHGEVPPSKDNTVFTAEPKFLPTLLDLHQRFPKLKIVLEHCTTADAVEAVKACGESVAGTITAHHLYLTQKDWQDDPYCFCKPVAKTERDRRALIEAATSKNPKFFFGSDSAPHPRSSKLKTPPAAGVFTQPFAASYLAEVFDKEGRLDALKDFACIFGRKFYCIPLDFKESNIVLKKESFRVPESVAND... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Catalytic Activity: (S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate
Sequence Mass (Da): 37552
Sequence Length: 337
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
EC: 3.5.2.3
|
A4J560 | MKLNLAVKIGQLDMINPVTTASGTFGYGQEYSPYVDLNQLGAIVVKGTTLEPREGNPTPRLVETPSGILNSIGLQNSGVDYLLEHYVPFFKKLQTNVIVNISGNTAEEYGQLAARLDEADGIAALEVNISCPNVKKGGMAFGGDFRTAAEVTKVVKNSTALPVIVKLSPNVTDIAEIARAVEGAGADGLSVINTLLGMAIDVRKRKPVLGNTMGGLSGPAVKPVALRAVWQVYKAVHIPIIGMGGIMNATDALEFILAGAQAVSVGTANFVNPYATKEIIQGMEKYLMENGIGDINELVGAAHL | 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): 31975
Sequence Length: 304
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway... |
B1GYY3 | MIPDLSVNFAGIKLKNPVLTASGTFGYGYELADLIPLKRLGGVVTKTVTLEPRAGNLQPRIAEVASGILNSIGLQNIGVRAFIEEPLEKLNKIGVPVIVSVAGVAVGEYVEIVKILSSQNGVSAIELNLSCPNLKKKIVCHDLPLMRDVIRGVKKVSRVPVIAKLSPLVTDISELALTAQNAGADGVTLTNTYPAMAVDIRTFKPKLSTVKGGMSGACIKPMSVRCVYDAYQDIKIPIIGCGGIMMGEDAVEFILAGATAVSVGSSSLVSPGNLIAIIDGIEDILKEKNIKSVKKIIGGINKVRNA | 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): 32168
Sequence Length: 306
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway... |
P0DH74 | MMKNPLAVSIPGLTLKNPIIPASGCFGFGEEYANYYDLDQLGSIMIKATTPQARYGNPTPRVAETPSGMLNAIGLQNPGLEVVMQEKLPKLEKYPNLPIIANVAGACEEDYVAVCAKIGQAPNVKAIELNISCPNVKHGGIAFGTDPEVAFQLTQAVKKVASVPIYVKLSPNVTDIVPIAQAIEAGGADGFSMINTLLGMRIDLKTRKPILANQTGGLSGPAIKPVAIRLIRQVASVSQLPIIGMGGVQTVDDVLEMFMAGASAVGVGTANFTDPYICPKLIDGLPKRMEELGIESLEQLIKEVREGQQNAR | 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): 33093
Sequence Length: 312
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway... |
P54322 | MTENNRLSVKLPGLDLKNPIIPASGCFGFGEEYAKYYDLNKLGSIMVKATTLHPRFGNPTPRVAETASGMLNAIGLQNPGLEVIMTEKLPWLNENFPELPIIANVAGSEEADYVAVCAKIGDAANVKAIELNISCPNVKHGGQAFGTDPEVAAALVKACKAVSKVPLYVKLSPNVTDIVPIAKAVEAAGADGLTMINTLMGVRFDLKTRQPILANITGGLSGPAIKPVALKLIHQVAQVVDIPIIGMGGVANAQDVLEMYMAGASAVAVGTANFADPFVCPKIIDKLPELMDQYRIESLESLIQEVKEGKK | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor. Cannot use fumarate as an electron acceptor.
Catalytic Activity: (S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate
Sequence Mass (Da): 32930
Sequence Length: 311
Pathway: Pyrimidine met... |
Q2N6N6 | MLFSLIRPAIHALDPERAHRFSIEALKLAPLPHSRHSDASLSVKVAGIRFPNPVGVAAGYDKDAEVPDALLGLGFGFVEVGSITPRPQEGNPKPRLFRLSRDRAVINRMGFNNAGADVAERRLRARAAKGGVIGINVGANKDSDDRIADYATMVRRMAPYASYLTANISSPNTPGLRALQDEGALTGLLDAVMEAPGADGPPVFLKVAPDLEPADVDAIARIAIDKGLGALIVSNTTIFRPDLQSRDRDETGGLSGAPLKPLALQRLRDFRSATGGAIPLVGVGGIATIDDAWERIRAGASLVQVYSAMVYEGPGLGRSI... | 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): 36304
Sequence Length: 343
Pathway: Pyrimidine ... |
A6H0L5 | MYKLIIRPILFCFDPEKVHYFTFSLIRTIAKIPGFTSIFKSLYEVNDKRLEREVFGLKFKNPVGLAAGFDKDAKLYKELSNFGFGFIEIGTLTPKGQEGNPKKRLFRLQEDSAIINRMGFNNGGVLEAVERLKKNNGVLIGGNIGKNKLTPNENATSDYEICFDALYDYVDYFVVNVSSPNTPNLRELQEKEPLTQLLNTLQNKNQNKQKQTRDGAQSSGAKPILLKIAPDLTNEQLLDIIDIVKTTKIAGIIATNTTISREGLQSINRIEMGGLSGKPLTNRSTEVIRFLSQKSNKAFPIIGVGGIHCVQDAIEKLEAG... | 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): 38966
Sequence Length: 350
Pathway: Pyrimidine ... |
Q7NC99 | MDLYRLARPLLFRADPEDAHRRALGALAWAAEQLWAGWLDSVFGYPDPRLEVKLWGLSFANPLGLAAGFDKNAEAVGAWEHLGFGFAEVGTVTRHAQPGNPRPRLFRLPADQAAINRMGFNNDGADALALRLAGRRWGIPIGINLGKSKVTPLEQASDDYLYSFERLYHLGDYFVVNVSSPNTPGLRELQQADRLGEILARLQCANRESKPLLVKIAPDLGWDAVDAVVDLCGEHRLAGVIATNTTIARSGLRSDLQETGGLSGAPLRNRSTEVIGHIWGRTRGQLPIVGVGGIFSGEDAWEKIAHGASLLQVYTGWIYE... | 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): 38641
Sequence Length: 353
Pathway: Pyrimidine ... |
P45477 | MYQLFRHGIFQMDAEKAHNFTIQCLKLAGNPLFQPILKSLIHAPKGFPKTVMGVNFPNPIGLAAGADKNGDAIDGFGALGFGFLELGTVTPVAQDGNAKPRQFRLIEAEGIINRNGFNNNGIDYLIENVKNARYKGVIGINIGKNKFTSLEQGKDDYIFCLNKAYNYAGYITVNISSPNTPDLRQLQYGDYFDDLLRSIKDRQAILANQYNKYVPIAVKIAPDLTESELVQIADTLVRHKMDGVIATNTTISRDTVTGMKNAEQQGGLSGKPLQHKSTEIIKRLHQELKGQIPIIGSGGIDGLQNAQEKIEAGAELLQVY... | 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): 37271
Sequence Length: 339
Pathway: Pyrimidine ... |
Q9KXR7 | MYKTFFKLVFSRMDPERAHHLAFRWIRLAVRVPVLRTFVAAALAPRHKELRTEALGLRMHGPFGLAAGFDKNAVAIDGMAMLGFDHVEIGTVTGEPQPGNPKKRLFRLVADRALINRMGFNNDGSLAVAARLASRTPVFRTVVGVNIGKTKVVPEEEAVGDYVKSAERLAPHADYLVVNVSSPNTPGLRNLQATEALRPLLSAVREAADRAVTARRVPLLVKIAPDLADEDVDAVADLAVELGLDGIIATNTTIAREGLGLTSSPALVGETGGLSGAPLKARSLEVLRRLYARVGDRITLVGVGGVETAEDAWERILAGA... | 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): 39562
Sequence Length: 368
Pathway: Pyrimidine ... |
Q30R79 | MINYQSIKPWLFKLEPEDAHMLAEAALRIPNVCQVAFNPFLESHFITNSILKQELFGRTFFNPIGLGAGFDKNATMIRAMQILGFGFTEIGTITPKAQAGNPKPRMFRHIEEQSIQNAMGFNNEGLLSAQKRLKKRFPFTTPIGINIGKNKLTPDTQAINDYTTLIKALHELGDYLVINISSPNTPGLRDLQNEEFITKLFEESKAITSKPILLKIAPDMSKEDAVALTKLAVLKGADGIIATNTTVDYSLVKEPKSIGGLSGAVLKEKSFEIFEAVAKELYGKTTLISVGGISSAKEVYRRIKAGASLVQIYSGLIYEG... | 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): 38726
Sequence Length: 352
Pathway: Pyrimidine ... |
P74782 | MLRFARSLYPLILSVTKSDPERGHQRLIQTLKKVDTMHRNGFAVAMEQLEQAFTHADPRLQQTCWGLNFPNVLGLSAGCDKEGEAAAVWPALGFGFAELGAVTKYAQPGNDRPRLFRLPQDQAVLNRLGANNEGAVAMAAKLKHTWDYYPRTIPIGINLCKSKITPLDQAVEDYVFSFQTLAPVADYFVVNVSSPNTPGLRSLQESDELPRIFAGLQSANHWQKPLLVKISPDLSWEAIAVIIDLVKEHNLSGIVATNTSTRRSGLKTKILPQTGQPIEQEAGGLSGQPIRDRATEVIRYIYQQTGGTIPIIGVGGIFTA... | 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): 41559
Sequence Length: 381
Pathway: Pyrimidine ... |
Q2S8N8 | MHDYQKAFIEFAIQREVLKFGQFTLKSGRSSPYFFNAGLFNTSTTLAQIGHFYAAALTSSPLQYDMLFGPAYKGIPLVSALAVTLANEKSMDVPYAFNRKEAKAHGEGGVIVGAPLKGKVLIVDDVITAGTAIREVISIIKANGAEPAGVLIALDRQERGQHQLSAIQEIEQNYQIPVTAIIQLDQILEFLKSDPHFSDNYKQVAEYRAVYGVQS | 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): 23599
Sequence Length: 2... |
A1WZE3 | MYEYQEDFIRFALDRGVLRFGRFTLKSGRESPYFFNTGLFNSGTALSKLGRCYVESLVRAQIDFDLVFGPAYKGIPLATAVAMALAETRNRDVPYAFDRKEVKDHGEGGRLVGAPVEGRRAVIVDDVISSGISIREAAELITAEGGTVAAVAIALDRKERGRDEVSAVHEVEQTLGAPVVPIITLDHLETYLADHGGKGDTLDAIRQYRARYGAA | 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): 23498
Sequence Length: 2... |
D4GZW2 | MANAALIEALRAADAVQFGEFELSHGGTSSYYVDKYLFETDPRCLKLIAEAFAERVADDDKLAGVALGAVPLVAATAVETNKPYVIARKKAKEYGTAKRIEGALDEGEEVVVLEDIATTGQSAVDAVEALREAGAVVDRVVVVVDRQEGAAELLADHDIALESLLTAEDLLADADG | 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): 18562
Sequence Length: 1... |
P56162 | MDIKACYQNAKALLEGHFLLSSGFHSNYYLQSAKVLEDPKLAEQLALELAKQIQEAHLNIECVCSPAIGGILAGYELARALGVRFIFTERVDNTMALRRGFEVKKNEKILVCEDIITTGKSAMECAKVLEEKGAQIVAFGALANRGICKRAHSHLKAQEGACLPSHLPLFALEDFVFDMHKPSSCPLCATSVAIKPGSRGN | 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): 21903
Sequence Length: 2... |
Q9UX09 | MNFAEVLLERKLLLIGSFVLTSGKVSPYYLDLRPLPNYPEFYDIVNQAIKKAKDIPHDIIVGIATGGVPLSAFIACNLKEPMGYIRIEKKGHGTNRTLELDVKGKRVLLVDDVATTGVSIEKATLEILNGGGKVSDALVIIDRQEGASQRLEKLGVKLHSLFKISEILDELLKSDKLKDNEKKSILDYLVKNVEK | 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): 21614
Sequence Length: 1... |
O94331 | MSYKLELLRRALEHNVLKFGTFTLKSGRKSPYFFNSGNFTHGADLCALAEAYAETIIAMNVDFDVIFGPAYKGISLAAITAVKLYEKTGKSYGFAYNRKEAKSHGEGGNLVGAEMEGKKVLLLDDVITAGTAIREAISFLEPKHVKLAGIVLLLDRQERLDPEVNESTIGRLKKELNLPVSSILTLDDIVDFTKSDLTAAESKAMDAYRQQYQAK | 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): 23716
Sequence Length: 2... |
Q8E9L5 | MKAYQREFIEFALERQVLRFGEFTLKSGRISPYFFNAGLFNTGRDLARLGRFYAAALVDSGIDYDLLFGPAYKGIPIATTTAVALCEHHNIDIPYCFNRKEKKDHGEGGSLVGSELKGRVMLVDDVITAGTAIRESMEIIEAHQAQLAGVLIALDRQEKGKGELSAIQEVERDFGCGIVAIIKLADLISYLSEKPRMEAQLAAVSQYREQYGIEA | 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): 23828
Sequence Length: 2... |
Q8NQ40 | MTFGEKLLNAASTRGRLCVGIDPHESLLTSWGLPVNVDGLAEFSRACVEAFADTVALVKPQVAFYERFGSAGFAILEETIQTLRERGCLVVSDAKRGDIGSTMAGYASAWLDPASPLSSDAVTVSPYLGFHSLDPVFELAEQHGRGVFVLAATSNPEARELQDQQNADGVSISQQIVDQAAALNAPYMAQGKAGNIGVVIGATLSKPPRLSTLGGAILMPGVGAQGGTASDVDEIAGDMAHLAFPNVSRSILATGPDIAEMKNSVAKNAADFPGFPRS | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 28920
Sequence Length: 278
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
B6J887 | MEKPDPKVIVAIDAGTVEQARAQINPLTPELCHLKIGSILFTRYGPAFVEELMQKGYRIFLDLKFYDIPQTVAGACRAVAELGVWMMNIHISGGRTMMETVVNALQSITLKEKPLLIGVTILTSLDGSDLKTLGIQEKVPDIVCRMATLAKSAGLDGVVCSAQEAALLRKQFDRNFLLVTPGIRLETDEKGDQKRVMTPRAAIQAGSDYLVIGRPITQSTDPLKALEAIDKDIKTR | 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): 25849
Sequence Length: 236
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC... |
Q0K6Y9 | MTFTEQLAAAWQRNDSLLCVGLDPDPQKLPLSLTGAGGAIFSFCREIVDATADLVCAFKPQIAYFHSQRAEDQLEQLIHYIHDAHPGIPVILDAKRGDIGSTAEHYALEAFERYHADAVTVSPYMGFDSMQPYLAYPDRGVIVLCRTSNPGGSDVQFLQVDGKPLYQLVAEAARERWNTTGQMGLVVGATFPNEIARVRQIVGDMPLLIPGIGAQGGDIEATVKAGRTADGTGMMINSSRAILYASREKDFAAAARNVALQTRETINRYRHG | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 29642
Sequence Length: 272
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
Q6BY69 | MVKTQTYTERASAHPSPVAQRLFKLMDNKKTNLCASVDVKSTEEFLTLIEKLGPYICLVKTHIDIIDDFSYEGTVVPLLALAKKHNFMIFEDRKFADIGNTVKSQYSGGVYKIAQWSDITNAHGITGSGIVKGLKEAAQESSKEPRGLLMLAELSSKGSLAYGEYTEKTIEIAKSDKEFVIGFIAQRDMGGTDEGFDWIVMTPGVGLDDKGDGLGQQYRTVDQVVTTGTDIIIVGRGLFGQGRDPTVEGKRYRDAGWNAYLKKTGSL | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 29320
Sequence Length: 267
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
Q3ZAI1 | MKFLEKLKQAGNSHNSLLCVGLDPDPKLMPVGMTALEFNREIIAATAPFVCGYKINLAFYEALGKQGWEILSETCKLIPPELLSIADAKRGDIGNTSKAYARAVFDELGCDGVTASPYLGYDSLEPFIEYQDKGIFILCRTSNQGSADFQMLKTEYLGQKRFLYEVVADKSLQWNRYENIGLVVGATQQEELKKLRLSYPKMPFLIPGIGAQGGDLKATVENGTNQSGQLALICASRGILYARSGSEFAQGAAEAAKQMRDAINHYRKRF | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 29786
Sequence Length: 270
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
Q9RSC5 | MTPTFAQAVTERTLSRRTRLCVGLDPRLGEYRDVAQLRQNTLDVLEASAPYAACVKPQLAFFEALGLPGFTLLEEVCAAARTLGLPVLLDGKRGDIGTTAAAYAQGWLGGTHAGDALTVNPFLGFQTLTPFVQAARENGGAIFVLVKTSNPDQQDLQGQGVSERIAVEIARLGDEEGLGDGDYASVGAVVGATHPGDLATFRALMPKALLLLPGLGAQGAQARDLAGAFHAGGTGALASASRAVQYARGLDVGAAREAALALRDELNGALGV | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 28066
Sequence Length: 272
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
B3DVI6 | MDLKPIVALDLPDPSEALKLVHLLRPHIDFFKVGSQLFLAGGTDIIRRIIDCGADVFLDLKFHDIPRTVFRAVTEVVKLKVKFTTVHILGGREMLKEALEASAGSDTEILGVTVLTSMDDRGLESIGIAHAVEEEVLLLASMALEVGLRGIVCSGKELPLLGKLKKRASILVVPGIRWRGAAAYDQKRIIEPGEAKKGGATHVVVGRPILEAHDKVGLVQKLLCELNAIN | 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): 24929
Sequence Length: 230
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC... |
Q57700 | MPKLMLALDVLDRDRALKIVEDVKDYVDAIKVGYPLVLSTGTEIIKEIKKLCNKEVIADFKVADIPATNEKIAKITLKYADGIIVHGFVGEDSVKAVQDVAKKLNKKVIMVTEMSHPGAVQFLQPIADKLSEMAKKLKVDAIVAPSTRPERLKEIKEIAELPVITPGVGAQGGKIEDILNILDENDYVIVGRAIYQSQNPKEEAKKYKEMLNK | 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): 23592
Sequence Length: 213
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC... |
B8IFW8 | MPDTPSPRDRLIVALDMATTDEAERLIDRLGDAASFYKIGYRLGYAGGLALAERLVKGGAKVFLDLKLHDIGNTVEEGVQSLARLGAHLLTVHAYPQTMRAAVRGRDSVPGSALRLLAVTVLTSYDDADAREAGYALSVSELVAIRALAAREIGIDGIVCAATEAAQVREIVGPDGLIVTPGIRPAGSDTGDQKRVVTPAAAIRAGVDYIVVGRPITAAADPRAVAQSIVAEIAAA | 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): 24561
Sequence Length: 236
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC... |
O26232 | MRSRRVDVMDVMNRLILAMDLMNRDDALRVTGEVREYIDTVKIGYPLVLSEGMDIIAEFRKRFGCRIIADFKVADIPETNEKICRATFKAGADAIIVHGFRGADSVRACLNVAEEMGREVFLLTEMSHPGAEMFIQGAADEIARMGVDLGVKNYVGPSTRPERLSRLREIIGQDSFLISPGVGAQGGDPGETLRFADAIIVGRSIYLADNPAAAAAGIIESIKDLLNP | 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): 24915
Sequence Length: 228
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC... |
Q2RK39 | MPTLMYLQEMIRMHAKDKIIVALDVPDLAAGEKLVDRLSPYAGMFKVGLEFFTAAGPAAVRMVKERGGRVFADLKFHDIPNTVAGAARALVRLGVDMLNVHAAGGKAMLQAAAAAVREEAAALNRPAPVIIAVTVLTSLDREALRCEVGIEREVEEQVARWALLAREAGLDGVVASPREIRAIREACGPEFVIVTPGVRPAGSDRGDQRRVMTPAEALREGASYLVIGRPITAAPDPVAAARAIAAEIEMVK | 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): 26861
Sequence Length: 252
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC... |
P32431 | MNTYKTYSERGQQHPNACARSLFELMERNESNLSVAVDVTTKKELLSIADAVGPFVCVLKTHIDIVEDFDHDLVAQLEQLAKKHDFLIFEDRKFADIGNTVKHQYANGIYKIASWSHITNAHTVPGEGIIKGLGEVGLPLGRGLLLLAEMSSKGALTKGSYTSESVEMARRNKDFVFGFIAQHKMNEHDDEDFVVMSPGVGLDVKGDGLGQQYRTPHEVIVESGGDIIIVGRGIYGNPDQVEAQAKRYRQAGWDAYLERVRLHKK | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 29514
Sequence Length: 265
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
P0A5M7 | MTGFGLRLAEAKARRGPLCLGIDPHPELLRGWDLATTADGLAAFCDICVRAFADFAVVKPQVAFFESYGAAGFAVLERTIAELRAADVLVLADAKRGDIGATMSAYATAWVGDSPLAADAVTASPYLGFGSLRPLLEVAAAHGRGVFVLAATSNPEGAAVQNAAADGRSVAQLVVDQVGAANEAAGPGPGSIGVVVGATAPQAPDLSAFTGPVLVPGVGVQGGRPEALGGLGGAASSQLLPAVAREVLRAGPGVPELRAAGERMRDAVAYLAAV | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 27377
Sequence Length: 274
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
P0CB75 | MREHRPIIALDFPSFEAVKEFLALFPAEESLYLKVGMELYYAAGPEIVSYLKGLGHSVFLDLKLHDIPNTVKSAMKILSQLGVDMTNVHAAGGVEMMKAAREGLGSQAKLIAVTQLTSTSEAQMQEFQNIQTSLQESVIHYAKKTAEAGLDGVVCSAQEVQVIKQATNPDFICLTPGIRPAGVAVGDQKRVMTPADAYQIGSDYIVVGRPITQAEDPVAAYHAIKDEWTQDWN | 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): 25423
Sequence Length: 233
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC... |
A3CN89 | MREERPIIALDFPSFDDVKDFLEHFPEDEKLYVKIGMEFFYAIGPEIVHYLKGLGHSIFLDLKLHDIPNTVRSAMSVLGTFGIDMVTVHAAGGVEMMSEAKKVLGDKAKLVAVTQLTSTSEEDMRDCQNIQTTVQESVVNYARKAKEAGLDGVVCSAQEVELIKAATADDFLCVTPGIRPAGSEIGDQKRVMTPQEAHQIGSDYIVVGRPIIQAENPWDAYHEIKKQWNS | 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): 25541
Sequence Length: 230
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC... |
Q9PJ84 | MKQTKYIFVTGGVLSSLGKGIAAASIATLLKNSGLKVSILKADPYINVDPGTMSPFEHGEVFVTDDGAETDLDLGHYERFLDESLSQDNNFTTGRVYQSVIEKERRGEYLGKTIQVIPHIVGEIKDRIKKAGEGKDILIVEIGGTVGDIEGLPFLEAIRALRLEVGKNNAMNIHLTLVPFIKAAGELKTKPTQHSVGELRRIGISPDMIICRSEKALDRDLKDKIAISCGVEKNCVIESVDAASIYQIPLNFLKQDILSPIAEILDLKNLKPNMENWDSLVKRVIAPSNEVKIAFVGKYVDLKESYKSLTEAIIHAGAAL... | Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate... |
Q2FSE6 | MKYIFVTGGVMSGLGKGITAASIGRLLKNRGYQVTAVKIDPYLNIDAGTMNPAQHGEVFVLHDGGEVDLDLGNYERFLDIELNSSHNITTGKVYRMVIDKERRGDYLGQTVQIIPHITDQIKDCIRSAAEEKVFDGKPADICIVEVGGTVGDIESMPFLEAVRQMRSELATADRALVHVTLMPSDSMGDLKTKPTQHSIKALRELGIFTDIIVGRSERPLNSHTKKKLSSLCDIPQNGIISAATAPDIYQVPMELEKEGMADVLCQLLQLRKDGADPEWYRIVTREYTHRITIGIVSKYGKEDVYLSIKEALRHAGRKLS... | Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate... |
Q58574 | MKIMKFIFITGGVISSLGKGITAASLGRLLKARGFKVNMIKIDPYLQIDAGTMSPYEHGEVFVTEDGGESDLDLGHYERFIDENLTKNNNITTGKIYWSVLTKERKGEYLGKTVQVIPHITNEIKDWIKNLGEGYDITIVEIGGTVGDIESLPFLEAIRQFKKDVGKENVLYIHVSLLPYIRAAGELKTKPTQHSVKELRSIGIQPDILICRTEMPISDKIREKLALFCDVDKEAVIEARDARTIYEVPLNLEKEGLGKLVTKKLNLPDREPDLDEWRKFVDRVINPLNEVTIGIVGKYVELKDAYLSITEALIHAGAKN... | Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate... |
Q2NH50 | MSKYIVVTGGVVSSIGKGITSASIGRILRSYGVNVTAIKIDPYLNWDSGTLNPYQHGEVYVTDDGMECDLDLGHYERFLDVELSGKANITTGKVYSSVIEKERKGEYLGSCVQIIPHITDEIKLMIRNVAEKTKAEVVMVEVGGTVGDIESQPFIEAVRQLKNEEGHDNCMFVHVTYVPYLKAAKEFKTKPTQHSTKELRGLGINPDMIVCRSELSLDANLKEKIAHFCDVPIEAVINTPDAHSIYEVPLIMYSANVGSYILNRLNIDTATNKADLYEWSQIVEDLKIETPKVKIAVVGKYIELEDAYISIRESLKHAGA... | Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate... |
Q2RFU8 | MPAKFIFVTGGVTSSLGKGITAASLGRLLKSRGLKVAIQKFDPYINIDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDISLTKASNVTAGKVYWSVITKERRGDFLGGTVQVIPHITNEIKARLLRVAEESDPDVVITEIGGTVGDIESLPFLEAIRQMKSDIGRDRVLYIHVTLVPYLRAAGEAKTKPTQHSVKELRSIGIQPDIIVCRTERPFSREMEEKIALFCDIDPDAVIQAWDADSIYEVPLMMQEEGLDSIVVERLKLNCGPAQMDDWRAMVAKLKNITRHLEIALVGKYVTLPDAYLSVVESLRHAGMY... | Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate... |
Q1AW18 | MSGTKYIFVTGGVVSSIGKGTSAAALGMLLKSRGYRVVLQKFDPYINVDPGTMNPYQHGEVFVTEDGAETDLDLGHYERFLDENLGRLSNVTTGSVYWEVISRERRGDYLGATVQVIPHITNEIKARIGRLGREKDVVITEIGGTVGDIESQPFLEAIRQFRNDVGRKNVLYVHVSYVPYIEAAGELKTKPTQHSTQRLREMGISPDILICRADRPIGEEIRRKIALFGDVEVDSVIPAQDAPTLYDIPLSLHGSGLDALVLEKLGLPAPPARLEEWRGLVRRLHGAEREVRVAVIGKYIRLQDAYLSVVEALRHAGGAH... | Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate... |
Q1GF61 | MARFIFITGGVVSSLGKGLASAALGALLQARGYSVRLRKLDPYLNVDPGTMSPFEHGEVFVTDDGAETDLDLGHYERFTGVPARKTDSISSGRIYTNVLEKERRGDYLGKTIQVIPHVTNEIKDFISIGEDEVDFMLCEIGGTVGDIEGLPFFEAIRQFSQDKPRGQCIFMHLTLLPYIKASGELKTKPTQHSVKELRSIGLAPDILVCRSEGPIPVKEREKLALFCNVRADSVIAAQDLKSIYEAPLAYHREGLDQAVLDAFGIAPAPRPTLDTWEDVADRIYNPEGEVKVAIVGKYTQLEDAYKSIAEALTHGGMANR... | Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate... |
O31749 | MEKPKYKRIVLKLSGEALAGEQGNGINPTVIQSIAKQVKEIAELEVEVAVVVGGGNLWRGKTGSDLGMDRATADYMGMLATVMNSLALQDSLETLGIQSRVQTSIEMRQVAEPYIRRKAIRHLEKKRVVIFAAGTGNPYFSTDTTAALRAAEIEADVILMAKNNVDGVYNADPRKDESAVKYESLSYLDVLKDGLEVMDSTASSLCMDNDIPLIVFSIMEEGNIKRAVIGESIGTIVRGK | Function: Catalyzes the reversible phosphorylation of UMP to UDP, with ATP or dATP as the most efficient phosphate donors. Is also able to phosphorylate 5-fluoro-UMP and 6-aza-UMP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 26083
Sequence Length: 240
Pathway: Pyrimidine metabolism; CTP biosynthesis v... |
Q8A5J7 | MAKYKRILLKLSGESLMGEKQYGIDEKRLAEYAAQIKEIHEQGVQIGIVIGGGNIFRGLSGANKGFDRVKGDQMGMLATVINSLALSSALVAAGVKARVLTAVRMEPIGEFYSKWKAIECMENGEIVIMSGGTGNPFFTTDTGSSLRGIEIEADVMLKGTRVDGIYTADPEKDPTATKFSDITYDEVLKRGLKVMDLTATCMCKENNLPIVVFDMDTVGNLKKVISGEEIGTVVHN | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 25549
Sequence Length: 236
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.22
|
Q2L160 | MSSRSYKRVLLKLSGEALMGDDAFGINRSTIVRMTDEIAEVAAMGVELAIVIGGGNIFRGVAPGAQGMDRATADYMGMMATIMNALALQDALKHKGLDTRVQSALNIDQVVEPYIRPKTLRYLEEGKVVIFAAGTGNPFFTTDTAAALRGAEIGAEIVLKATKVDGIYSADPNKDPTATRYARISFDEAIVRRLEVMDATAFALCRDQKLPIKVFSINKSGALKRVVGGEDEGTLVHV | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 25571
Sequence Length: 238
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.22
|
Q89KP5 | MTDPVYRRVVIKLSGEYLAGQQGFGIDQPTVDRVADDLIAARHLGTEVAVVIGGGNIVRGVEVSSRGVSRPTGDTMGMLATMMNCLALEAAIERKGTPARTLSAFVMPEISELFTRTAAHKYLAEGRIVLLGGGTGNPFFTTDTTAVLRAAEIGAQAVLKATNVDGVYSADPKKDPTATRFDRLTHSQAIEGGYKVMDATAFALARETSLPIIVFSIAEPGSIGAILRGIGHGTIVAG | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 24931
Sequence Length: 238
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.22
|
Q8EUG9 | MNKELVILKISGASLKGKNDIIDLDFLREIGRQIKVLSNNYKVAIVLGGGNIWRGNIAKEIGMQRYKADQMGMLATVMNSLALQSLLTNINVKSRIFSTIEMEKIADSYIIRNLEESLNNNEIAILSCGTGRPYFTTDTGVAVSAAELGASYIMMGKNNVDGVYDSDPNKNPNAKFYKHLTYSKAIELGLEVMDITAATICKQSNIKTIVFKMNEKNGILNAFENKSKFTLVSEDEKDLDAFKFGIKNIKNNSEKSSNNWDNKVIDIKTIKEENSLNIDDIFENSIEELQKLKEDDIQKNQKKLNEIIKSFYQDNKE | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 35707
Sequence Length: 317
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.22
|
Q6F0Q9 | MKYKYSTVLLKLSGEALKSENEIYNKEKLEDIAKQIVELAKNGLKLGIVIGGGNIWRGKLGTDIDMPQINADYMGMLATVMNGLALESTIKRLGYDKVNVYSSLPIETVTDDYNFKRARLKMNEGYISIFVGGTGFSYFTTDTNSVIRAIEIGADAVLMAKNGVKGVYDSDPNLNPNAKFYKKLTHREIAENQLRVMDLTAATLAKDAKLPIEVFDMQGQNNIIKVMEGSLESTIIEE | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 26392
Sequence Length: 238
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.22
|
Q600A4 | MDSTILIKLSGESLANKQKSLAIDYELVRQIGSQLKEIQNLGHKILIVIGGGNFWRGTSAAKNGINRNTADYIGMLGTVMNGLALDSVFRDLGIKTRVLSSMSLDPRICEYFVREKAMKYLEDNNVLIFVGGTGRPFFTTDSAATLFASEMGANIILVGKNNVNGIFDSDPKINPNALRYDKITYNQVIEKNLKVMDSTAFSMARDNKIKLLIFDIKEKNSISKLIKRQIKHTEVY | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 26319
Sequence Length: 236
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.22
|
Q8TTQ4 | MLIVLSLGGSILAKNLDSDRFLKYANVLRDISKKHTLLVITGGGEAARNYIGAARAMGADEVTCDYIGIDITRLNARLLIAALGPDGYPEIPTNYLEASKAINSGKVVVMGGVTPGQTTDAVAAILAEYLRADLLTIATSIDGVYSSDPNCDPSAVKYDKISPEKLINIVMAIEMKAGSKSPVDPVAAKIIERCKLDALVMDARDPSLLGEILGEEVAKKSPVSCGTWITARK | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 24664
Sequence Length: 233
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.22
|
Q0W3K6 | MKIVVKVGGSAIVQGLDAQRFKDYADVIKQLAEDHTILIVIGGGTPARDYINVSKQLGANNSILDYIGIGVSRLNARLLISALGDIAYPEPPYDYKDAGLAMYSGKVVVMGGVVPGQTTDAVAAILAEYVHADLLIRTTSVDGVFTADPKLDPKATKIDSMTPQELVDMVTKIEMTAGANNIFDPLGAQIVKRSRIPTVVVNGKQPENLIKAVKGEPIGTIIKE | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 23829
Sequence Length: 224
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.22
|
O69913 | MSSTKAEKSDDGKVSGRFMLKLSGEAFSGGGGLGVDPDVVHAIAREIAAVVRDGAQIAIVIGGGNFFRGAELQVRGMDRARSDYMGMLGTVMNCLALQDFLEKEGVDCRVQTAITMGQVAEPYIPLRAVRHLEKGRVVIFGAGMGMPYFSTDTTAAQRALEIDAEALLMGKNGVDGVYDSDPKTNPDAVKFDALGYGEVITRDLKVADATAVTLCRDNSLPIVVFELLKEGNIARAVKGEKIGTLVGDQGSRD | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 26834
Sequence Length: 253
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.22
|
Q97R83 | MKMANPKYKRILIKLSGEALAGERGVGIDIQTVQTIAKEIQEVHSLGIEIALVIGGGNLWRGEPAAEAGMDRVQADYTGMLGTVMNALVMADSLQQVGVDTRVQTAIAMQQVAEPYVRGRALRHLEKGRIVIFGAGIGSPYFSTDTTAALRAAEIEADAILMAKNGVDGVYNADPKKDKTAVKFEELTHRDVINKGLRIMDSTASTLSMDNDIDLVVFNMNQPGNIKRVVFGENIGTTVSNNIEEKE | Function: Catalyzes the reversible phosphorylation of UMP to UDP, with ATP as the most efficient phosphate donor.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 26703
Sequence Length: 247
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.
Subcellula... |
P80464 | AKSDVAELKPR | Cofactor: Binds 1 Mo-molybdopterin cytosine dinucleotide (Mo-MCD) cofactor per subunit.
Function: Converts (3-methyl-)-quinoline to (3-methyl-)2-oxo-1,2-dihydroquinoline.
Catalytic Activity: A + H2O + quinoline = AH2 + quinolin-2(1H)-one
Sequence Mass (Da): 1213
Sequence Length: 11
Pathway: Xenobiotic degradation; quin... |
Q6VMW0 | MALPNGISSKQELLEAQAHVWNHIYSYINSMSLKCAIQLGIPDAIHKHGNPITLSQLADALNINKAKSHGLFRLMRILVHSGFFDKVKVKVKVEGEDEEEEEDAYSLTPASRLLLRSEPLSVAPFALAMSDPVYTETWHHLSEWFRNDAVAAFDTKYGMTFPEYAVADDRLNVLFNEAMACDAGFVNSILTTECREIFDGLESMVDVGGGTGATAKGIAAAFPGMECTVLDLPNVVGGLKGSENLSFVSGDMFDFIPHADAIFMKFILHDWNDEECVKILKKCKEAISRSNNSCRKIILVEIVMEDEKETHEATETKLFF... | Function: Flavonoid 8-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as pebrellin, aroma compounds which contribute to the flavor of peppermint, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-... |
P0A0J8 | MISFFTKTTDMMTSKKRWTALVVLAVSLFVVTMDMTILIMALPELVRELEPSGTQQLWIVDIYSLVLAGFIIPLSAFADKWGRKKALLTGFALFGLVSLAIFFAESAEFVIAIRFLLGIAGALIMPTTLSMIRVIFENPKERATALAVWSIASSIGAVFGPIIGGALLEQFSWHSAFLINVPFAIIAVVAGLFLLPESKLSKEKSHSWDIPSTILSIAGMIGLVWSIKEFSKEGLADIIPWVVIVLAITMIVIFVKRNLSSSDPMLDVRLFKKRSFSAGTIAAFMTMFAMASVLLLASQWLQVVEELSPFKAGLYLLPMA... | Function: Confers export-mediated resistance against antiseptic and disinfectant compounds such as intercalating dyes, quaternary ammonium salts and diamidines.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55016
Sequence Length: 514
Subcellular Location: Cell membrane
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P14319 | MPYIYLIIAISTEVIGSAFLKSSEGFSKFIPSLGTIISFGICFYFLSKTMQHLPLNITYATWAGLGLVLTTVVSIIIFKEQINLITIVSIVLIIVGVVSLNIFGTSH | Function: Multidrug exporter. Is implicated for the resistance to bacteriocidal quaternary ammonium compounds and ethidium bromide.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11673
Sequence Length: 107
Subcellular Location: Cell membrane
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P0AGC9 | MKGWLFLVIAIVGEVIATSALKSSEGFTKLAPSAVVIIGYGIAFYFLSLVLKSIPVGVAYAVWSGLGVVIITAIAWLLHGQKLDAWGFVGMGLIVSGVVVLNLLSKASAH | Function: Multidrug exporter. Is implicated for the resistance to bacteriocidal quaternary ammonium compounds.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11472
Sequence Length: 110
Subcellular Location: Cell membrane
|
Q96PU8 | MVGEMETKEKPKPTPDYLMQLMNDKKLMSSLPNFCGIFNHLERLLDEEISRVRKDMYNDTLNGSTEKRSAELPDAVGPIVQLQEKLYVPVKEYPDFNFVGRILGPRGLTAKQLEAETGCKIMVRGKGSMRDKKKEEQNRGKPNWEHLNEDLHVLITVEDAQNRAEIKLKRAVEEVKKLLVPAAEGEDSLKKMQLMELAILNGTYRDANIKSPALAFSLAATAQAAPRIITGPAPVLPPAALRTPTPAGPTIMPLIRQIQTAVMPNGTPHPTAAIVPPGPEAGLIYTPYEYPYTLAPATSILEYPIEPSGVLGAVATKVRR... | Function: RNA-binding protein that plays a central role in myelinization . Binds to the 5'-NACUAAY-N(1,20)-UAAY-3' RNA core sequence. Regulates target mRNA stability . In addition, acts by regulating pre-mRNA splicing, mRNA export and protein translation. Required to protect and promote stability of mRNAs such as MBP a... |
Q54II8 | MNPLTLVRETTAWVSGLSKHVKINNEALDKECEDFLNKHKIKAHKEIWADNWFHYCDIDIENKESTFTELTAKYILVLDTLNFCFWPDSEFEYHHLARGLKNALIANPKCFDADQLIKVTSETIHQWFGKDLPNTSERVRLIREVGTVLIEYFNGSIKEMILSANNKASVLVDLVTKYFWGFRDSAIYKGKQVFFYKRAQIFVGDLWGAYQGRGLGKFDDIKQLTMFADYRVPQILEELKVIEYSPELKEMIKNKVEIPVGSEMELEIRAVTVHVVEKMRDYFNKGHCELLALEIDWMLWGRGEAMLDKLPPHHRTLTIF... | Function: Catalyzes the hydrolysis of queuosine 5'-phosphate, releasing the nucleobase queuine (q). Is required for salvage of queuine from exogenous queuosine (Q) that is imported and then converted to queuosine 5'-phosphate intracellularly.
Catalytic Activity: H2O + queuosine 5'-phosphate = D-ribose 5-phosphate + que... |
Q5T6V5 | MDGLLNPRESSKFIAENSRDVFIDSGGVRRVAELLLAKAAGPELRVEGWKALHELNPRAADEAAVNWVFVTDTLNFSFWSEQDEHKCVVRYRGKTYSGYWSLCAAVNRALDEGIPITSASYYATVTLDQVRNILRSDTDVSMPLVEERHRILNETGKILLEKFGGSFLNCVRESENSAQKLMHLVVESFPSYRDVTLFEGKRVSFYKRAQILVADTWSVLEGKGDGCFKDISSITMFADYRLPQVLAHLGALKYSDDLLKKLLKGEMLSYGDRQEVEIRGCSLWCVELIRDCLLELIEQKGEKPNGEINSILLDYYLWDY... | Function: Catalyzes the hydrolysis of queuosine 5'-phosphate, releasing the nucleobase queuine (q). Is required for salvage of queuine from exogenous queuosine (Q) that is imported and then converted to queuosine 5'-phosphate intracellularly. In vitro, can also catalyze the release of the q base directly from Q as subs... |
G3X8U3 | MGPPLSPRESARFVAENSRDVLVDHEGVRRAAELLLPAAAAWRVEQWKSLHELNPRGADEAALGWVFLVDSLNFSFWAEREDSKCAVRYGGTPYTGYWALCAAVNRALDQGIPITSASYYATVSLEQVRDIFRSDTAVPMPLMEERHRILNETGKILLEKFGGSFLNCVQKSGRSAQKLMQLIVENFPSYRDEAEFEGKRIAFYKRAQILVADTWSVLEGKGDGCFEDISSITMFADYRLPQILVYLGALKYSDELLKKLLKGEMLLNGDKQEVEIRGCSIWCVELIRDRLLELLEKGENSPVEINSVLLDYHLWDYARE... | Function: Catalyzes the hydrolysis of queuosine 5'-phosphate, releasing the nucleobase queuine (q). Is required for salvage of queuine from exogenous queuosine (Q) that is imported and then converted to queuosine 5'-phosphate intracellularly.
Catalytic Activity: H2O + queuosine 5'-phosphate = D-ribose 5-phosphate + que... |
A7SNN9 | MSNQVMLPRESGSFIASHSKDVSLCEEGISRASEIVFKSLKSNAYSYKTWKDHELHPKEMSKATVDWIFVLDTLNFSFWVDDGLEPWTIRHKGKDFQGYWALCAGINRAIEEGIHLTSPSYYRNITIDDLKHIFRSETSTEMPLLEERAKNLRETGNILAQTFQNSFAHMILLANKSAKLLLSMVINNFDCFRDDGDFCNQKVSFYKRAQILIADTWACFEGKGFGEFPDIDFLTMFADYKVPQGLYDLGVLQFSEALKQKLVTGQLIPHGDQLEMEIRGNSIWAVEKIYLAVKLKAKKSPEFSNMDSLELAQYLNSVII... | Function: Catalyzes the hydrolysis of queuosine 5'-phosphate, releasing the nucleobase queuine (q). Is required for salvage of queuine from exogenous queuosine (Q) that is imported and then converted to queuosine 5'-phosphate intracellularly.
Catalytic Activity: H2O + queuosine 5'-phosphate = D-ribose 5-phosphate + que... |
Q9HDZ9 | MSRVLQDAEFISLNSNDVKVNKGGCAAVATWIKEKLDSLGPQFAEWQNHELHPKTRDVSTLDWIFLVDILNFSFWSDVDVEDSGKHSKRFSIEYKGKLYTGYWSLCAAINKALDAGIPITSPAFYADEKQCPDTLIASVFDSATVEKIPLLEERIRIMRASGRVLVDSYHGSYCGLLKKCHNQAQRLIKLLLADFPDFRDVSVYKGRECYMLKRAQILVAETWACFQGQNYGRFDDIDSITMFADYRVPQILWQLGCLSYSSDFKKRLLKNELIAHNDPMEIEMRGCSIWAVEKILQNINRKDVNAITIDFFLWDLAKEW... | Function: Catalyzes the hydrolysis of queuosine 5'-phosphate, releasing the nucleobase queuine (q) (By similarity). Is required for salvage of queuine from exogenous queuosine (Q) that is imported and then converted to queuosine 5'-phosphate intracellularly .
Catalytic Activity: H2O + queuosine 5'-phosphate = D-ribose ... |
D1C7A6 | MADPGDRLGVLTTTRRVVEQAQAVWIDHDAVAQIAEAFAARQVTPPTWNRELHWSDGREALANYILVLDAVNFCFWGEPRWRIEYAGAVYDGYWALAASLKRALEQGVPLTDASYLAEITRDDVATIFAGEGEIPLLDERARILRETGSVLAERFAGRFSDAIAAAGRSAVALVDIVTNAFPSFRDVATYRGEQVRFYKRAQILVSDLYGAFDGSDLGAFDDLGELTAFADYKVPQVLHHLGILRYAPALHDRLARREEIPAGSPEEVEIRAATIWGVEELRRALASRGHALDAYQVDWLLWDEGQRLPAGTLPYHRTRT... | Function: Catalyzes the hydrolysis of queuosine 5'-phosphate, releasing the nucleobase queuine (q). Is likely required for salvage of queuine from exogenous queuosine (Q) that is imported and then converted to queuosine 5'-phosphate intracellularly. In vitro, can also catalyze the release of the q base directly from Q ... |
Q817W5 | MDINLFDFHLPEELIAQVPLEDRETSRLMVLDRETGDIEHKHFTDILSYLHEGDCLVLNETKVMPARLHGVKEDTGAHIEVLLLKQEEGDKWETLVKPAKRVKEGTVISFGEGKLKATCTGTADQGGRQLEFSYDGIFYEILDELGEMPLPPYIKETLEDRDRYQTVYAKEIGSAAAPTAGLHFTEELLEKLKQKGVQLAFITLHVGLGTFRPVSADTIEEHHMHAEYYHMSEETAALLNRVKQNGGRIITVGTTSTRTLETIATDHDGKLCAASGWTDIFMYPGYEFKAIDGLITNFHLPKSTLIMLVSAFANRDNVLH... | Function: Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Catalytic Activity: 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxyqueuosine(34) in tRNA + 2 H(+) + L-methionine
Sequence Ma... |
O32054 | MKVDLFDFELPERLIAQVPLEQRDASRLMVLDKHTGELTDSSFKHIISFFNEGDCLVLNNTRVLPARLFGTKEDTGAKVELLLLKQETGDKWETLAKPAKRVKKGTVVTFGDGRLKAICTEELEHGGRKMEFQYDGIFYEVLESLGEMPLPPYIKEQLDDKERYQTVYSKEIGSAAAPTAGLHFTEEILQQLKDKGVQIEFITLHVGLGTFRPVSADEVEEHNMHAEFYQMSEETAAALNKVRENGGRIISVGTTSTRTLETIAGEHDGQFKASSGWTSIFIYPGYEFKAIDGMITNFHLPKSSLIMLVSALAGRENILR... | Function: Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Catalytic Activity: 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxyqueuosine(34) in tRNA + 2 H(+) + L-methionine
Sequence Ma... |
B2IHG4 | MRVDLFDFDLPPERIALRPVEPRDASRLLVVRPDSGDMTDHGMRELPDFLRAGDVLVVNDTRVIPARLHGFRSRGESRAKIEATLHKREGEALWRAFVKPAKKLRVGETICFARQEPGTEVESLEAEVLEKGAEGEVVLGFNRAGAALDAALDLLGEMPLPPYIAGKRAPDSQDSLDYQTLFANRSGAVAAPTASLHFTPRLIAAIEARGVTICKVTLHVGAGTFLPVKAEDTDAHRMHAEWGEVSAEVAAFLNKVHAAGGRIIAAGTTSLRLLESAVDEDGLIQPFQGETSIFMTPGFRFRAVDILLTNFHLPRSTLFM... | Function: Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Catalytic Activity: 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxyqueuosine(34) in tRNA + 2 H(+) + L-methionine
Sequence Ma... |
Q7WMM7 | MPTPLTLADFDYHLPPELIAQSPAAERGGSRLLHLDAASRLHDRRFPDLAGLLRPHDLLVFNDTRVIKARLTGQKATGGKVEVLVERITAPDRALVHVRASKSPGPGMRLRLAEAFEAEVLGREGELFDLRFPAPVLDLLDAHGATPLPPYITHAADATDERRYQTVYAREPGAVAAPTAGLHFDQPMLEQLAAQGVQRAFVTLHVGAGTFQPVRVQNLAEHIMHAEWYTVPEATVAAIARARAHGGRIVAVGTTSVRALESAAAQAQDGPLAAAQGDTRLFITPGYRYRIVDALLTNFHLPQSTLLMLVSALAGVAPIR... | Function: Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Catalytic Activity: 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxyqueuosine(34) in tRNA + 2 H(+) + L-methionine
Sequence Ma... |
O51053 | MKTKEFHFNLSHSLIEQYPSEKRGSSRLIVLDPQLQKIYHKNSVNNILKYINSNIFNNSKARKSRIYAESEMSSNVEFLILDRIDTNLFTALVSKSKKQIIGNFYKFPEGLMDEILSKNSSEVVLKFNNNVGEDYFEKHCFVPLPSYIKRDYDKIDEDRYQTIYSKYVGSTASATAGLHFSRDLFSAFENNNIEYDFITLHVGAGTFLPVRSKKVEEHNMHFETFLIKDFVAVRLQNAKLLGKRILSIVTTTLRALESSYDNNLKKFKTGQQSTNLFIYPGKNYCFKFVDMLFTNFHTPQSTLLMLVSSFAGKDFVFSFY... | Function: Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Catalytic Activity: 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxyqueuosine(34) in tRNA + 2 H(+) + L-methionine
Sequence Ma... |
Q8R620 | MKKLRKRKMSTYLSDYDYFLPEELIGQKPREPRDSAKLMLIDRKNGSVEHKNFYNIIDYLQKGDILVRNATKVIPARIFGHKDTGGVLEILLIKRITLDTWECLLKPAKKLKLGQKLYIGENKELIAELLEIKEDGNRILKFYYEGSFEEILDKLGSMPLPPYITRKLENKDRYQTVYAQRGESVAAPTAGLHFTEELLNKILDKGVEIVDIFLEVGLGTFRPVQTVNVLEHKMHEESFEISEKVAKIINEAKAEGRRIISVGTTATRALESSVDENGKLIAQKKDTGIFIYPGYKFKIVDALITNFHLPKSTLLMLVSA... | Function: Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Catalytic Activity: 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxyqueuosine(34) in tRNA + 2 H(+) + L-methionine
Sequence Ma... |
B9M5N6 | MQLKDFNYHLPPELIAQEPAHRRESARLMTLDRKSGEIGEGVVADIAEYFVAGDLLVINDTKVIPARLLGRKETGGKAEVFLVRRRDEAGQVWQCLIKCSKSPAPGSLILLSEGVTARIVERSEHDTWIVSFSPEEGFLDRLEMIGSMPLPPYIHRPANVIDGERYQTVFARERGAVAAPTAGLHFTESLLQKIRARGVDILPLTLHVGLGTFMPVRVKDLSEHRMHREYYRIPETTAKAVTDRKKAGKRVIALGTTTTRALEHAAAEDGSLDAKEGEADIFIVPGYAFKTVDALITNFHLPESTLLMLVSAFAGRDRLF... | Function: Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Catalytic Activity: 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxyqueuosine(34) in tRNA + 2 H(+) + L-methionine
Sequence Ma... |
Q5KWR3 | MKVDLFDFHLPEELIAQTPLPDRAASRLMVLDKRTGAIRHETFRNIISYLNPGDCLVLNDTRVMPARLYGEKEETGGTVEVLLLKQLDGDRWETLVKPGKRVKPGTKLTFGEGKLEAVCLDTLEHGGRVLEFSYDGLFYEVLAELGEMPLPPYIKEKLDDPERYQTVYAREIGSAAAPTAGLHFTEELLDAIREKGVHIVFITLHVGLGTFRPVQVDDVEKHDMHAEFYQMSEETAETLNRVREQGGRIIAVGTTSTRTLETIAGKHNGRFVAESGWTDIFIYPGYEFKGIDGLVTNFHLPKSTLIMLVSALAGRENILH... | Function: Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Catalytic Activity: 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxyqueuosine(34) in tRNA + 2 H(+) + L-methionine
Sequence Ma... |
A5GEQ5 | MQLNDFDYYLPTELIAQQPAQNRDASRLMTLDRVNGELNETIISEIAALFRDGDLLVINDTRVIPARLLGKKESGGRVEVFLVRRLLEPGEVWQCLIKASKSPKPGSLIILSEGVVARVLERSELDTWAVSFSPVEGFLDRLERIGSMPLPPYIRRSAGDDDRERYQTVFARAKGAVAAPTAGLHFTDALLQKIRQQGVEIAPLTLHVGLGTFMPVRVDDLKDHRMHREYYFIPEATARAVNARKNDGGRVVALGTTTTRALEHAAAGNGSVQPGEGEADIFICPGYTFKVVDALITNFHLPKSTLLMLVSALAGKDRLF... | Function: Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Catalytic Activity: 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxyqueuosine(34) in tRNA + 2 H(+) + L-methionine
Sequence Ma... |
Q7NFD9 | MNAPIDERDFLTDSYDYALPERCIAQQPAEPRDHSRLLVVDGEAHTHRYFYDLPGLLRPGDLLVLNDTRVIPARLFGSKASGGRVEVLLLEPRAPREWLCLVKPARRLAVGARIDFDGVLAARVTELDAETGGRWLRFEGEEDFEAALERVGHTPLPPYLKTGRTRDERYQTLWASRPGAVAAPTAGLHFSGELLARLAERGIERATVTLHVGLGTFRPVQSVSVHTHRMHREWYEIPEATAIAIERTRSRGGRVLAVGTTSARALESAAQPNGLPATGPGRSELFVYPGYRWRVVEGLITNFHLPRSSLLMLVSSLVGR... | Function: Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Catalytic Activity: 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxyqueuosine(34) in tRNA + 2 H(+) + L-methionine
Sequence Ma... |
Q5FR06 | MTDDLAPFDFELPRDHIATEPARPRDSATLLHVRPGLPPDPHVIRDLPDFLREGDLLIANNTAVIRAQLAATRGEAKIGLTLDRILANGSWHALARNSRKLKPQDILHFGDDPVTATVIENEGDGAVSIRFSVEGDEFDAFLERVGALALPPYIERPFGPTKQDDADYRTIFSQYRGAVAAPTAGLHFTPEVLAALDAKGIQRRTLTLHVGAGTFLPVRSTIAEHKMHAEWGEIDAETAAAINETRARGGRIVAVGTTSLRLLESAAREDGTVAPWRGETSIFIKPGYRFKAVDVLMTNFHLPRSTLFMLVCAFSGTETM... | Function: Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Catalytic Activity: 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxyqueuosine(34) in tRNA + 2 H(+) + L-methionine
Sequence Ma... |
A1S7P3 | MRVADFTFDLPDELIARYPMAERTASRLLHLDGSTGALADRQFTDILALIEPGDLMIFNNTRVIPARLFGQKASGGKLEILVERMLDDKRILAHVRSSKSPKPGAEIILDGGFKMTMDARHDALFELSLKDDKTILEVLEAVGHMPLPPYIDRPDEDTDKERYQTVYNERPGAVAAPTAGLHFDESILAALKAKGVDMAFVTLHVGAGTFQPVRVDNVLEHKMHSEWAEVPADVVEKIRATKAAGKRVIAVGTTSVRSLESAAKASEGELEPFCGDTDIFIFPGFEFKVVDAMVTNFHLPESTLIMLVSAFAGFDEVIGA... | Function: Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Catalytic Activity: 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxyqueuosine(34) in tRNA + 2 H(+) + L-methionine
Sequence Ma... |
Q5WG41 | MLEDKAVVVFSGGQDSTTCLFWAKERYRSLHAVIFDYGQRHKEEIQCAVDIANEQGVPYKVFDMGLLNQLTANALTRENISVQAGEAGESPSTFVAGRNHLFLSFAAVYAREMGAKHIITGVCETDFSGYPDCRDVFVKSLNVTLNLAMDEQFVIHTPLMWLNKKETWALADKMGQLEYIRAKTLTCYEGIRGDGCGTCPSCQLRQNGLDLYLREKAGAGQ | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 24592
Sequence Length: 2... |
O67003 | MKKHDGIIVLLSGGMDSATLLWLAKREFKKVYAISFDYGQRHKVELKYAKELAKLAEVEDHFIVQVPFYTSLKGSALIDESVEVPKGEYPENEPPVTTVPMRNLIFLSIASAFADNLEVNYIGIGVHALDTPYPDCRPEFITAAEAAINAGSTFVAKKKERMHVYAPFLGMSKRDIALLGKELGVPFEKTYSCYMGTEPPCGECPTCIQREEALRGIL | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 24238
Sequence Length: 2... |
O29807 | MKAVMLLSGGIDSSTLLYYLLDGGYEVHALTFFYGQKHSKEIESAEKVAKAAKVRHLKVDISTIHDLISYGALTGEEEVPKAFYSEEVQRRTIVPNRNMILLSIAAGYAVKIGAKEVHYAAHLSDYSIYPDCRKEFVKALDTAVYLANIWTPVEVRAPFVDMTKADIVRLGLKLGVPYELTWSCYEGGDRPCLSCGTCLERTEAFLANGVKDPLLSDEEWKNAVKIYEEMRARNEGKSD | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 26726
Sequence Length: 2... |
B9M0M7 | MKKKAVILYSGGLDSTTCMAIAREEGFEPYAMSFDYGQRHSVELATAKANAKTMGASEHLVVSFDLRKVGGSALTADLDVPKEGIGAGIPVTYVPARNTIFLSFALGWAEVLGAFDIFIGVNALDYSGYPDCRPEYIAAFEATANLATRAGVEGTGRFVIHAPLIAMTKAEIIRKGLALGVDYGRTHSCYDPTPEGLACGLCDSCRLRLKGFAEAGVTDPVPYAVRSKK | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 24383
Sequence Length: 2... |
Q74FW9 | MTRKAVVLYSGGLDSTTCLAIARAEGFEPHAMSFSYGQRHSVELELAKRNARPAGAVEHMVVEFDLRKVGGSALTADIAVPKEGVGDDIPVTYVPARNTIFLSFALGWAEVLGAFDIFIGVNALDYSGYPDCRPEYISAFETMANLATRVGVEGTGRFRIHAPLMRLTKAEIIRKGLALGVDYGLTHSCYDPSPAGVACGLCDSCRLRLKGFAEVGVADPVPYVTGGQGLGGGKETP | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 25160
Sequence Length: 2... |
B7K7J4 | MNQPKAVILLSGGLDSATTAAIALASGYEAIALSLFYGQRHHKEIEAAQKIVQVLGIKEHYSLEVNLSQWGGSALTDQSIEVPKAGLNPHLIPITYVPGRNTVFIAIALSLAEAKGAQAIYLGINAIDYSGYPDCRPEYLEAFQKLANLSSKIGVEGKTIQLIAPLVKDSKVDIVRRAVRLGVPIADTWSCYQGEDEPCGLCDSCRIRDRALIEAGYPELATEIGRKLSH | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 24831
Sequence Length: 2... |
Q7NCE2 | MKKALVVFSGGQDSTTCAALACREYDEVHAVTFEYNQRHAIELESARAVGQALGLTGHEFIRLGPLLKGTSPLVSDAPLGQYASAAELPAGVEPTFVPGRNILFLTLAANRAFCLGTGDIVIGVCEADFAGYWDCRQVFVEAMARALGEGIYGDANAIRIHTPLMRLTKAETVKLSVEVLGERFEEVLALSHTCYAGVRGGCGRCHACILRDRGFREAGVPDPIWKFRKEPVSL | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 25272
Sequence Length: 2... |
A9HRF6 | MATSLTPADPLQEAAIVLFSGGQDSATCLAWALSRFGRVETVGFDYGQRHAVELACRARLRDGMAALDPDWATRLGQDHTLALDALGTVSDTALTRDAAITMNENGLPSTFVPGRNLIFLTFAAALAARRGARHIVGGMCETDYSGYPDCRDDTIKAMQVALNLGMASRYVLHTPLMWIDKAETWRMAEGLGGADLVELINRESHSCYLGVRDVMHPWGHGCGTCPACMLRRAGWERYVADGADA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 26507
Sequence Length: 2... |
B7J648 | MPSQPSRELERFSNPHPERDYVVHMDLPEFTCLCPLTGQPDFAHFMLDFIPDQHNVELKSLKLYLWSFRDEGAFHEAMTNRIADDLIGLINPRYLRLLGRWYVRGGITTDVLIEHRQPGWQNPDILGQLPTVRWAQHQPGH | Function: Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Catalytic Activity: 7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH
Sequence Mass (Da): 16512
Sequence Length: 141
Pathway: tRNA modification; tRNA-queuosine ... |
Q0VR70 | MSYLKETPLGRSSEYVDQYMPSLLCPVPRWDAREGLELESATLPFHGSDIWNAYELSWLNEKGKPIVAMCELRVPCTTPNIVESKSLKLYLNSFANTRFQSRDAVRAAIEKDVAQTAGGNIEVLLFSLQESAGFPVWEDRGDCVDNIDLNFEHYEYRPDLLLCDQGPEQTGQLYSHLLRSHCPVTDQPDWATVVVRYTGRAISPASFLRYVVSLRNHQGFHEQIIEQMFVDLMTQCSPRHLTVYGRFTRRGGIDINPFRSNSEQPLPNRRTIRQ | Function: Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Catalytic Activity: 7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH
Sequence Mass (Da): 31403
Sequence Length: 274
Pathway: tRNA modification; tRNA-queuosine ... |
Q0AAV5 | MSTQPSKDLETFPNPRPERDFVLHMRIPEFTCLCPKTGQPDFATIHLDYVPDERCVELKSLKLYMWSFRDQGAFHEAITNEILDDLVRATEPRYMKVTAEFYVRGGIYTTVVAEHRKPGWAPAPKVELA | Function: Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Catalytic Activity: 7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH
Sequence Mass (Da): 14915
Sequence Length: 129
Pathway: tRNA modification; tRNA-queuosine ... |
Q3JAH8 | MPSQPNRELETFANPLPERDYTIRIRIPEFTCLCPKTGQPDFATLQLEYVPDQACVELKSLKLYIWSYRDQGAFHEAVTNQILDDLTAVCKPRFMRLTAEFNVRGGIYTTVAAEYRQPGWDAPKIVRLP | Function: Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Catalytic Activity: 7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH
Sequence Mass (Da): 14866
Sequence Length: 129
Pathway: tRNA modification; tRNA-queuosine ... |
P44068 | MNTELQPKLEKSAVNFQAKPRKQKIRKDPNAPFIREKLELPDGHNKLLLHSCCAPCSGEVMEAILASGIEFTIYFYNPNIHPLKEYLIRKEENIRFAKKFGIPFIDADYDRQNWFDRAKGMEWEPERGIRCTMCFDMRFEKAAEYAHKHGFPVFTSCLGISRWKDMNQINGCGHRAAEKYDDVIYWDYNWRKEGGSQRMIEISKRERFYQQEYCGCVYSLRDSNKWREETGRQKIEIGKLYYSAD | Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
Catalytic Activity: AH2 + epoxyqueuosine(34) in tRNA = A + H2O + queuosine(34) in tRNA
Sequence Mass (Da): 29072
Sequence Length: 245
... |
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