ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q5FNS8 | MSRRTRLIAALDTASRSTAQDWADSLKNDVDAIKLGLEFTYACGLDAVKTVSAGHELFLDLKLHDIPHTVASGLTALAPLRPALTTIHASGGSEMIARSREALESAFPADTKRPKLLAVTVLTSMNAEGLLDIGVNATPQEQVLRLGKLAISAGADGLVCSAHEIAPLRDALGDEPVLVVPGIRPAGSASDDQKRIMTPGQAAQAGADWIVVGRPITKAADPVLAARAIMEELASA | 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): 24596
Sequence Length: 236
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC... |
P43812 | MTSKIIVALDFEKEAEALALVDQIDPSLCRLKVGKEMFTTLGINFVKQLHQRNFDVFLDLKYHDIPNTVARAVRSAADLGVWMVDLHASGGLRMMEDAKKILEPYGKDAPLLIAVTVLTSMEDLDLLQIGINASPMEQVLRLAHLTQRAGLDGVVCSPQEVEILRNACGEDFKLVTPGIRPIGTDFGDQRRVMTPTAAIRAGSDYLVIGRPITQADNPAEVLRSINVSIG | 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): 25192
Sequence Length: 230
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC... |
Q5V216 | MHFFDRLADRIATADSVVSVGLDPDPARLPDSVLDADLPRWQFNRRIIDATHEHAACYKPNAAFYEDPDGWRALEETIAYAHGKNVPVLLDAKRGDIGNTARQYAQILDEDEGPAADAITVNPFLGRDSLEPFLQRADRGVFVLGRTSNPGGEDLQDLELASGEKLYERVVHLADLWNGNGNVGLVVGATNPDELEEIRELVPDIPFLVPGVGAQGGDAEAAVEHGLADGVGLVNSSRGIIFAGEDAATRRDDSGDAFFKAAGQSAKQLKQRLNQFR | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 29996
Sequence Length: 277
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
A4X621 | MESFGARLHRVVGERGPLCVGIDPHPGLLERWGLDDDVRGLERFAGTVVEALGDRVAVVKPQSAFFERFGSRGVAVLESTIRQLRTAGSLVLLDVKRGDIGSTVAAYASAYLDPSSPLHVDAVTVSPYLGVGALAPMFELAAAQGGGVFVLALTSNPEGAAVQRARTADGRTVAQLVIDEISQLNAGARPLGSVGLVVGATIGQTGHELAAVNGPLLAPGLGAQGASAADLRVVFGSSLPAVLPTYSREVLAAGPDVVALRGAADRVLADCRAALTGS | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 28347
Sequence Length: 278
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
P07691 | MTFTASSSSCAITESPVVVALDYHERDKALAFVDKIDPRDCRLKVGKEMFTLFGPQLVRDLQQRGFDVFLDLKFHDIPNTTARAVAAAADLGVWMVNVHASGGARMMAAARDALAPFSKDAPLLIAVTVLTSMETSDLHDLGVTLSPAEHAERLARLTQQCGLDGVVCSAQEAVRFKQAFGAAFKLVTPGIRPAGSEAGDQRRIMTPEQALSAGVDYMVIGRPVTQSVDPAQTLKDINASLKREA | 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): 26328
Sequence Length: 245
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC... |
P14965 | MDARVFQSYSARAEGMKNPIAKELLALMEEKQSNLSVAVDLTKKSEILELVDKIGPYVCVIKTHIDVVEDFDQDMVEKLVALGKKHRFLIFEDRKFADIGNTVKLQYASGVYKIASWAHITNCHTVPGEGIIQGLKEVGLPLGRGLLLLAEMSSKGSLATGSYTEKTLEWFEKHTDFCFGFIAGRRFPNLQSDYITMSPGIGLDVKGDGLGQQYRTPEEVIVNCGSDIIIVGRGVYGAGRNPVVEAKRYREAGWKAYQQRLSQH | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 29362
Sequence Length: 264
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
P13242 | MTKYIFVTGGVVSSLGKGIVAASLGRLLKNRGLNVTIQKFDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDINLNKFSNVTTGKIYSTVLKKERRGDYLGGTVQVIPHITNELKDRVYRAGKETNADVVITEIGGTVGDIESLPFLEAIRQMKSDIGRENVMYIHCTLVPYIKAAGELKTKPTQHSVKELRSLGIQPNIIVVRTEMPISQDMKDKIALFCDIDTKAVIECEDADNLYSIPLELQKQGLDKLVCEHMKLACKEAEMSEWKELVNKVSNLSQTITIGLVGKYVELPDAYISVVESLRHAGYAF... | 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... |
Q8AA75 | MGETKYIFVTGGVASSLGKGIISSSIGKLLQARGYNVTIQKFDPYINIDPGTLNPYEHGECYVTVDGHEADLDLGHYERFLGIQTTKANNITTGRIYKSVIDKERRGDYLGKTIQVIPHITDEIKRNVKLLGNKYKFDFVITEIGGTVGDIESLPYLESIRQLKWELGKNALCVHLTYVPYLAAAGELKTKPTQHSVKELQSVGIQPDVLVLRAEHPLSDGLRKKVAQFCNVDDKAVVQSIDAETIYEVPLLMQAQGLDSTILEKMGLPVGETPGLGPWRKFLERRHAAETKEPINIALVGKYDLQDAYKSIREALSQAG... | 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... |
Q8SQI7 | MKYVIVSGGVISGVGKGIVSSSIGALLKSRGHVVTHFKIDPYLNYNAGRMHPYEHGEVYVLDDGHECDMDFGNYERFNGIKLSGANSIPGGRLLHDIVKCEREGSFLGKTLQINPHIIDEVIRRIRAVADTPVESFGGGQAAVPDVVVVELGGTVGEYESSIYTEALAKFQYVVGKANCAFVSVDYIVELETGEQKTKGIQMGCRNFRRFGLNYDIVICRGRREPNMETRRKISTSCWVKEENVLGLPNLESVYLAPMFLEKHGIVEALNRILGLDDKGMDRRMLDIFSMVGRRHRDGVRIGIVGKYAPEFDSYTSLVNA... | Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen.
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 59338
Sequence Length: 535
Pathway: Pyrimidine metabolism; CTP biosynthesis via... |
Q2NAA7 | MARYIFITGGVVSSLGKGLMAASLGALLQARGYKVRIRKFDPYLNVDPGTMSPYQHGEVYVTDDGAETDLDLGHYERFTGVSARQSDNITSGRVYQDIIAKERRGDYLGATVQVIPHVTDAIKNFALADQDDLDFILCEIGGTVGDIESLPFMEAIRQLRNELEPMQTLSVHVTLVPYIAAAGELKTKPTQHSVRELASLGIKPDVLLCRAEHPLPDGERQKIANFCNVRKEAVIPALDAPSIYSVPLQYHEEGLDAEVLRGFGIVDAPAPDLSAWDDVTDRYFNPEGEVTIGVVGKYVGLQDAYKSLNEALVHGGLANR... | 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... |
A6H0U1 | MNQTKYIFVTGGVTSSLGKGIIAASLAKLLQARGYRTTIQKFDPYINVDPGTLNPYEHGECYVTNDGAETDLDLGHYERFLNVPTSQANNVTTGRIYLSVIEKERRGEFLGKTVQVVPHITNEIKERMQLLGKSGDYDIVITEIGGTVGDIESLPYIESVRQLVWELGENNGIVIHLTLVPFLAAAGELKTKPTQHSVKTLMESGIKADILVCRTEYELSEDLRHKLALFCNVKREAVIQSIDASTIYDVPNLMLEEGLDKVALKKLDLPEKSTPDLKQWNEFLQKHKNPKHEVSIGLVGKYVELQDSYKSILEAFIHAG... | 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... |
Q2S538 | MQTKYIFVTGGVTSSLGKGIFSASLGRLLSDRGLDVTIQKFDPYINVDPGTMNPYEHGEVYVTNDGAETDLDLGHYERFLDQPTSQANNVTTGRVYMEVISKEREGAYLGKTVQVVPHIIDEIKHWMLKLGETGDYDVVITEIGGTVGDIEGQPYLEAIRQLRNELGPRNTMIAHLTLIPHLRAAGELKTKPTQHSVKELLAHGLQPDTIVCRSERSITAEVRRKISLFCNVEEEAVIQMLDAESIYEVPLLLRDEGTGELVVDRFYPKRGDENEKCSDTPDLSDWIGFLKRLKNPEETIPIALVGKYVEHQDAYKSITE... | 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... |
Q5PBQ6 | MSVSDGAATGSVRYSRVLLKVSGEAFVGEKRFGFDPAVVLRLSRDLKNVKESGVELCIVVGGGNIFRGASTSDGFERTSNDYVGMLATVINALALQNALEEMGVECRVLSAMPMTAVCETYVRRRAVRHLEKGRVVICAAGIGSPFFTTDTAAALRGIEMRCDAIFKGTQVDGVYSSDPKKDGSAVRYDRISYHDLLSSNLKIMDAAAISLARENSVPIIVFDLGRDGAFFEAVHGRGLFTTISD | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 26333
Sequence Length: 245
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
|
O66929 | MEEKPKYKRILLKLSGEAFAGEQGYGIDPAFLEYISHEIKNVYDLGVQVAIVIGGGNIFRGFQGKEIGVDRATADYMGMLATVINALALQSALENHVNIPTRVLSAIEMRQVAEPYIRRRAIRHLEKGRIVIFAGGTGNPFFSTDTAAALRAAEIGAEVLIKATKVGGIYDKDPEKYPDAVLIKEISYLEVINMGLKVMDHTALTLCKENEIPIIVLNVKEKGNLRRAVLGEEVGSVVRG | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 26268
Sequence Length: 240
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
|
O28237 | MKVVLSLGGSVLSNESEKIREFAKTIESVAQQNQVFVVVGGGKLAREYIKRARELGASETFCDYIGIAATRLNAMLLISAIPSAAKKVPVDFMEAEELSKLYRVVVMGGTFPGHTTDATAALLAEFIKADVFINATNVDGVYSADPKSDTSAVKYDRLSPQQLVEIVSRSSAKAGTNVVIDLLAAKIIERSKIKTYVILGTPENIMKAVKGEAVGTVIA | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 23398
Sequence Length: 219
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
|
A2BLM0 | MPKGPVVIKVSGKYVNPEKPGLVKRYAQVLHELHSVGYRLVVVVGGGPEARRYIEAARELGLGKSFQDILGIEASRLNARLLIYALHPNAYPEPPRSIWELLEAYSTGLIVVAGGFQPGQSTSGVAALVAEAIGAELLVLATTVDGVYTADPAVDKSAQLIPRLSYEEFRRVVRQSMSPGRYELLDPVAISIVERSNIPVRVVNGSDPENVKRVVLGEELGSLITG | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 24349
Sequence Length: 226
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
|
A8AAG3 | MKTLVLKISGKFVSPYDTPLVEGYAKTLEALRRKYKLAVVVGGGSVARKYIELAPPSKGLKDLIGIEVSRLNALLLSMHTPSAKKVIPKSASEVLELWDGEDILIVGGLQPGQSTNAVALVVAELVGADLVVNATTVDAVYDKPPSQPGAKRIEKIKARELQRLLESFDWKNEPGRYELMDSIALQIAERSKIPIAVIYGGEPERIPSIVEEEAWGTLILP | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 24023
Sequence Length: 221
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
|
Q1IV36 | MSEPKYKRILLKLSGEALAQGEQGFGVDPTRVHEIAAEIAEVHRLGVDIGVVVGGGNFFRGVAEQAKDMDRVSADHMGMLATVMNSLAVQDALEKQNVQCRVMSAIEIFQVAEPFIRRRAMRHLEKGRVVIFAAGTGNPYFSTDTAASLRAAEIKADVIMKATKVDGIYDADPHKVADATMFAQITYMDVLKKGLRVMDATAISLCQENRLPIVVFNLNERGNIQRVVMGEAVGSLVSA | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 26005
Sequence Length: 239
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
|
A4J559 | MSKVFDAKVLAVYMVAPNTYYMEFDAPDIARLAVPGQFVHVRCGETNDPLLRRPISIHMVSRPKGVLALLFRVVGKGTEILSQQKPGDRVNMMGPLGRGFTLPLPGSKVAVAAGGIGAAPLVFLVQELANIKCQVTVYLGARDKRSILCDGQFIQMEAEVVIATDDGSLGFKGTVPELMKRHMDWRKTAMTYVCGPGIMMKEISTMLAEADVPGEVSLEERMGCGVGACLSCAVKISHHGQISNKRACFEGPVFPSWQVVWE | Cofactor: Binds 1 FAD per subunit.
Function: Responsible for channeling the electrons from the oxidation of dihydroorotate from the FMN redox center in the PyrD type B subunit to the ultimate electron acceptor NAD(+).
Sequence Mass (Da): 28456
Sequence Length: 262
Pathway: Pyrimidine metabolism; UMP biosynthesis via de... |
P0DH76 | MQRKQEMMTIVAQKQLAPRIYQLDLQGELVKEMTRPGQFVHIKVPRADLLLRRPISINQIDHSNETCRLIYRVEGAGTEVFATMKAGEQLDILGPLGNGFDITTVAAGQTAFIVGGGIGIPPLYELSKQLNEKGVKVIHFLGYASKEVAYYQQEFMALGETHFATDDGSFGAHGNVGRLLSEALAKGRIPDAVYACGANGMLKAIDSLFPTHPHVYLSLEERMACGIGACYACVCHKKGDTTGAKSVKVCDEGPIFKASEVIL | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Responsible for channeling the electrons from the oxidation of dihydroorotate from the FMN redox center in the PyrD type B subunit to the ultimate electron acceptor NAD(+).
Sequence Mass (Da): 28572
Sequence Length: 263
Pathway: Pyrimidine metabolism; UMP biosyn... |
P58884 | MKIEDCTVEENVQIAKDTYKMKIKGNFVKECRTPGQFVNIRIGDGREHVLRRPISISEIDRGENLVTIIYRIVGEGTKFMANIKKGNEIDVMGPLGRGYDVLSLTKEQTALLVGGGIGVPPLYELAKQFNKRGIKTIIILGFNSKDEVFYEDEFKKFGETYVSTIDGSVGTKGFVTDVIKKLQAENNLVFDKYYSCGPVPMLKALVNAVGEDGYISLENRMACGIGACYACVCKKKKKDDYTRVCYDGPVYLASDVEIE | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Responsible for channeling the electrons from the oxidation of dihydroorotate from the FMN redox center in the PyrD type B subunit to the ultimate electron acceptor NAD(+).
Sequence Mass (Da): 28834
Sequence Length: 259
Pathway: Pyrimidine metabolism; UMP biosyn... |
Q9K9W0 | MRQTERMTITSHQRIADGIYEMKVTGERVKEMTSPGQFVHVKVDDGSELLLRRPLSICHVDEQTSELTLLYRAEGQGTKRLAQKARGETVDILGPLGQGFPLEAIASGETALLIGGGIGVPPLYYLAKRLKAKGCHVINVLGFQSAKDSFYYEQFSQLGTTYVATVDGTAGTKGFVTHVLNQEALSYNVVYSCGPTPMLKAVSERFIGERAFISMEERMGCGIGACFACVCHVTGDEAGTAYRKICTDGPVFPVGEVVL | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Responsible for channeling the electrons from the oxidation of dihydroorotate from the FMN redox center in the PyrD type B subunit to the ultimate electron acceptor NAD(+).
Sequence Mass (Da): 28081
Sequence Length: 259
Pathway: Pyrimidine metabolism; UMP biosyn... |
P56968 | MSQLQEMMTVVSQREVAYNIFEMVLKGTLVDEMDLPGQFLHLAVPNGAMLLRRPISISSWDKRAKTCTILYRIGDETTGTYKLSKLESGAKVDVMGPLGNGFPVAEVTSTDKILIIGGGIGVPPLYELAKQLEKTGCQMTILLGFASENVKILENEFSNLKNVTLKIATDDGSYGTKGHVGMLMNEIDFEVDALYTCGAPAMLKAVAKKYDQLERLYISMESRMACGIGACYACVEHDKEDESHALKVCEDGPVFLGKQLSL | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Responsible for channeling the electrons from the oxidation of dihydroorotate from the FMN redox center in the PyrDB subunit to the ultimate electron acceptor NAD(+).
Sequence Mass (Da): 28660
Sequence Length: 262
Pathway: Pyrimidine metabolism; UMP biosynthesis... |
Q71YI2 | MLQTEMKVIQQTEIADKVYELILTGECVADMSPGQFLMLKPSRSDLLMRRPISICSYDKTAKTCILLYRIEGDGTRDFSKLSEGDTIDVLGPLGKGFDIDQTPAPKTALLIGGGIGVPPMYQLGKELAGKGVQVTFVNGFQSAKDSFYEKEMNAYGTVHIATVDGSLGTQGFVTDITNNFPEEPDVIYSCGPKAMLQAVKASFPETKTYLSLEERMACGIGACYACVCPKADDAKKQFKVCEDGPVFRADEVSL | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Responsible for channeling the electrons from the oxidation of dihydroorotate from the FMN redox center in the PyrD type B subunit to the ultimate electron acceptor NAD(+).
Sequence Mass (Da): 27589
Sequence Length: 254
Pathway: Pyrimidine metabolism; UMP biosyn... |
P58886 | MLPLNVTITQITEESPLVRTFFFDHRFEDMDPGQFVMVWVRGVDEVPMGLSRNNSITVQKVGEATSKLFELKEGDSFGLRGPFGKGFTLPSRGEKVLLIAGGVGAAPLSPYAEAASAAGAEVHTILGARSAGDLLFEWRFEALGDIYASTDDGSKGVKGFVTDVLKGLDVAAYDRIAVCGPEIMMASVFRLLEERKVLEKAEFSLHRYFKCGIGVCGACCIDLSGLRVCKDGPVFSGIQLLGSELGKYSRDASGRRIKI | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Responsible for channeling the electrons from the oxidation of dihydroorotate from the FMN redox center in the PyrD type B subunit to the ultimate electron acceptor NAD(+).
Sequence Mass (Da): 27982
Sequence Length: 259
Pathway: Pyrimidine metabolism; UMP biosyn... |
Q0W8E0 | MRPISATIKEIIDETPTIKTFRLDVDDWLHGKPGQYVMVWIRGVDEVPMTLSYDNAITVQKVGEATEALFKLKAGDSVGIRGPYGNGWEIVGDDILLISGGVGSAPLAPLGEKARRIGVNVTTLAGYRTKEEVHFEDRYRAAGELVVATDDGTYGKKGYVTDLLKSVDLKKFTQIYCCGPEKMMYRVLCALDEAGVAGLSQFSLQRYIKCGIGVCGSCCMDPDGLRVCRDGPVFDGETLLRSEMGKYARDASGRRQQI | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Responsible for channeling the electrons from the oxidation of dihydroorotate from the FMN redox center in the PyrD type B subunit to the ultimate electron acceptor NAD(+).
Sequence Mass (Da): 28246
Sequence Length: 258
Pathway: Pyrimidine metabolism; UMP biosyn... |
P11396 | MFGQTTLGIDSVSSSASRVFRFEVVGMRQNEENDKNKYNIRRSGSVYITVPYNRMSEEMQRIHRLGGKIVKIEPLTRAAG | Function: Rod linker protein, associated with phycocyanin. Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer.
Location Topology:... |
P07124 | MFGQTTLGAGSVSSSASRVFRYEVVGLRQSSETDKNKYNIRNSGSVFITVPYSRMNEEYQRITRLGGKIVKIEQLVSAEA | Function: Rod linker protein, associated with phycocyanin. Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer.
Location Topology:... |
P31966 | MLSQFANGTEAASRVFTYEVQGLRQTEETDNQEYAFRRSGSVFINVPYARMNQEMQRILRLGGKIVSIKPYTGATASDEE | Function: Rod linker protein, associated with phycocyanin. Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer.
Location Topology:... |
P73202 | MLGQSSLVGYSNTQAANRVFVYEVSGLRQTDANENSAHDIRRSGSVFIKVPYARMNDEMRRISRLGGTIVNIRPYQADSNEQN | Function: Rod linker protein, associated with phycocyanin. Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer.
Location Topology:... |
P50035 | MFGQTASGSAALSPSGARVFRYEVVGLRQNEETDRMEFPIRRSGSTFITVPYNRMNEEMQRITRMGGKIVSITPVVAS | Function: Rod linker protein, associated with phycocyanin. Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer.
Location Topology:... |
P14878 | MVYQSRSFQVEVSGLHQNEVTNQNNYPIRSSGSVFITIPFSRFNEELQRINRLGGKIVNIQPLNLQINEN | Function: Rod linker protein, associated with phycocyanin. Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer.
Location Topology:... |
Q0CZH1 | MDPQQRLLLEVVYEALEDAGITLDEIQGSLTSVYCGCFTNDYNAMTTKDLEYYPKYTVTGTGNSILANRISYFYNLHGPSATVDTACSSSLVCFHLGAQSLRDAEADISIVVGSALHFDPNIFITMTDLGMLSTDGRCRHGDAAGSGYVRGEGIAAMVLKRQDRAQADGDHIRAVVRGTGVNHDGRKQGITLPSARAQADLITSTYERAGLEPAETTYVECHGTGTKAGDPRELRAVHEVFCRHRPDTLHVGSVKTNIGHLEGASGIAGLMKATMALEKKIIPPNMHFSTPNPEVDFKNWKLEIPTEPKVWEMGRRTIPR... | Function: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of pyranterreones, a family of antioxidative compounds . The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase pytA that condenses 4 malonyl-CoA units ato the acetyl starter unit by the mo... |
Q0CZH0 | MRFLGIAAVATFSTVVSAYPKSTALYNCVSSVFGPSAPQRIVTPNDTTYLDSRLGETIQFDELPVLLAYAQESKEIAPLIRCAKTAGIKAVPRAGGHSFEAYSALNGTLIIDIAHLNYVNVSDDRQTAVVGAGIRLGALYTALSEHGTSFIGGICPTVGLAGFLGSGGFNMQQRSQGLAVEHVLAAKVVLADGRTVVASPDTNPDLFFAIRGGGGGTYGIVVEFTLSLTSIPRSAMLMLSWNDTASRFPAAKQYLDWAPKQIPEFMSQINVYRDKVQVLGWYYGGTEDELRSLVNASGLLDIGKPAVVIAGGCNTDNARA... | Function: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of pyranterreones, a family of antioxidative compounds . The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase pytA that condenses 4 malonyl-CoA units ato the acetyl starter unit by the mod... |
P46913 | MHRGKGMKFVGDSRIPAEKKPNIPKDYSEYPGKTEAFWPNFLLKEWMVGAVFLIGFLVLTIVHQPPLERMADPTDTGYIPLPDWYFLFLYQLLKYEYAAGSFTVVGAMIMPGLAFGALLLAPFLDRGTERRPWKRPVAVGMMLLAISAAVFLTWQSVATHDWAKAEEQGKITKEADIDTNAEGYKVFKEQGCISCHGDNLQGGAAGPSLVDSGLKPDEIKKIAVEGKGKMPAGVFKGNDKQLEELAKFISETTAK | Function: Component of the menaquinol:cytochrome c reductase complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28162
Sequence Length: 255
Subcellular Location: Cell membrane
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Q8NNK5 | MAKPSAKKVKNRRKVRRTVAGALALTIGLSGAGILATAITPDAQVATAQRDDQALISEGKDLYDVACITCHGVNLQGVEDRGPSLVGVGEGAVYFQVHSGRMPILRNEAQAERKAPRYTEAQTLAIAAYVAANGGGPGLVYNEDGTLAMEELRGENYDGQITSADVARGGDLFRLNCASCHNFTGRGGALSSGKYAPNLDAANEQEIYQAMLTGPQNMPKFSDRQLSADEKKDIIAFIKSTKETPSPGGYSLGSLGPVAEGLFMWVFGILVLVAAAMWIGSRS | Function: Cytochrome c1 subunit of the cytochrome bc1 complex, an essential component of the respiratory electron transport chain required for ATP synthesis. The bc1 complex catalyzes the oxidation of menaquinol and the reduction of cytochrome c in the respiratory chain. The bc1 complex operates through a Q-cycle mecha... |
Q7SIC2 | DTSSLIVEDAPDHVRPYVIRHYSHARAVTVDTQLYRFYVTGPSSGYAFTLMGTNAPHSDALGVLPHIHQKHYENFYCNKGSFQLWAQSGNETQQTRVLSSGDYGSVPRNVTHTFQIQDPDTEMTGVIVPGGFEDLFYYLGTNATDTTHTPYIPSSSDSSSTTGPDSSTISTLQSFDVYAELSFTPRTDTVNGTAPANTVWHTGANALASTAGDPYFIANGWGPKYLNSQYGYQIVAPFVTATQAQDTNYTLSTISMSTTPSTVTVPTWSFPGACAFQVQEGRVVVQIGDYAATELGSGDVAFIPGGVEFKYYSEAYFSKV... | Cofactor: Binds 1 copper ion per subunit.
Function: Performs the first step in the degradation of the flavonoid quercetin by a dioxygenase reaction. The enzyme catalyzes the cleavage of the O-heteroaromatic ring of the flavonol quercetin yielding the depside 2-protocatechuoyl-phloroglucinol carboxylic acid and carbon m... |
P42106 | MKTLCTHSLPKEKMPYLLRSGEGERYLFGRQVATVMANGRSTGDLFEIVLLSGGKGDAFPLHVHKDTHEGILVLDGKLELTLDGERYLLISGDYANIPAGTPHSYRMQSHRTRLVSYTMKGNVAHLYSVIGNPYDHAEHPPYASEEVSNERFAEAAAVADIVFLDEAKPACSAKLAELTELPDGAVPYVLESGEGDRLLTGDQLHRIVAAQKNTDGQFIVVSSEGPKGDRIVDHYHEYHTETFYCLEGQMTMWTDGQEIQLNPGDFLHVPANTVHSYRLDSHYTKMVGVLVPGLFEPFFRTLGDPYEGHIFPCEPQALRF... | Cofactor: Binds 2 Fe(2+) ions per subunit.
Function: Performs the first step in the degradation of the flavonoid quercetin by a dioxygenase reaction. The enzyme catalyzes the cleavage of the O-heteroaromatic ring of the flavonol quercetin yielding the depside 2-protocatechuoyl-phloroglucinol carboxylic acid and carbon ... |
O33472 | MQSLNVNGTLMTYSESGDPHAPTLFLLSGWCQDHRLFKNLAPLLARDFHVICPDWRGHDAKQTDSGDFDSQTLAQDLLAFIDAKGIRDFQMVSTSHGCWVNIDVCEQLGAARLPKTIVIDWLLQPHPGFWQQLAEGQHPTEYVAGRQSFFDEWAETTDNADVLNHLRNEMPWFHGEMWQRACREIEANYRTWGSPLDRMESLPQKPEICHIYSQPLSQDYRQLQLDFAAGHSWFHPRHIPGRTHFPSLENPVAVAQAIREFLQA | Cofactor: None. Contrary to most other dioxygenases, this enzyme does not require a cofactor for catalysis.
Function: Ring-cleaving dioxygenase involved in oxoquinoline degradation and utilization.
Catalytic Activity: 3-hydroxy-1H-quinolin-4-one + O2 = CO + H(+) + N-formylanthranilate
Sequence Mass (Da): 30347
Sequence... |
Q5A6P6 | MPGNREEFDIEKVLKSKKLEAIETSTEKKAPYTVFESTDKLLLIIVLSLVGFWSAISSPIYFPALPTLTKYFNTTPSVMNISVVAYLIFQGIAPTISSNLADTFGRRPVILGSIIVFCAVCIAISQTNVYWLLALLRCFQAAGIAPVFAISSGVAGDICTPANRGGMVGAVSGLQLAGNGIGGLVGAALISGFHTWRAIFIFLAIGGGVTFIFAFLVLAETSRRIVGNGSIRPKNVLNKAVLIYLPHFKNKITNDYSTLQPKGPFDILGPFKIFFQKEVFCTLLPSGMHFAAWTVSLTSLSTELESAKYNYSVMKVGLVY... | Function: MFS antiporter that does not display functional linkage as drug transporter and performs functions that significantly affect biofilm development and virulence. No substrate for transport has been identified yet, but plays an important role in the growth in the host.
Location Topology: Multi-pass membrane prot... |
Q59YT1 | MLSTTQSVTEPTEVTSKKVEDIEKENDEETPYSIFTSYDRLVLIVILSLIGFWSTISSPIYFPALPTLTSYFHTSSSIMNISVVAYLIFQGIAPTISSNLADTFGRRPVILASIIVFCASCVAISQTNVYWLLAVLRCIQAAGIAAVISISSGVAGDVCTRANRGSMVGAVAGLQLVGNGIGGLVGAALISSFNSWRSIFIFLTIGGGVTFILAIFILPETSRKLVGNGSVVPKNILNKSPYIYLPHFKKRMNNDITTIVPATRFDLLGPLKIFFQKNVFCTLLPVGIHFAAWTMVLTSLSTELESRYHYSVMHVGLIYL... | Function: MFS antiporter that does not display functional linkage as drug transporter and performs functions that significantly affect biofilm development and virulence. No substrate for transport has been identified yet, but plays an important role in the growth in the host.
Location Topology: Multi-pass membrane prot... |
Q6FSQ7 | MMEDQQSLHSFISDYDQRSHAVEKYDGPDLSEVDSEDNDKMIKTNEDEAVKEPIYRTRSNQTEPDIANAPPYSRFDAKYKMALVLQCAYTGLFSTMAGAIYYPVLSVIEKQFHITEELVNITVVVYFIFQGIAPTLMGGLADSLGRRPVVLFAVTVYFGACIGLACAQTYAQIVVLRCLQAAGISPVIAINSGIIGDVTTRAERGGYVGYISGFQVLGSAFGALIGAGLSSRWGWRSIFWFLAIGSGVCLVFSIIMLPETKRTIVGNGSVTPRNYLNRAPLLMFPLIRRKLHLDDPEYETLEPRTQLSLLAPLSILKVKE... | Function: Multidrug resistance transporter involved in resistance to the antifungal drugs miconazole, tioconazole, clotrimazole, and ketoconazole; as well as to quinidine . Decreases the intracellular accumulation of clotrimazole in and plays a role in the extrusion of this antifungal from preloaded cells .
Location To... |
P40474 | MAGATSSIIRENDFEDELAESMQSYNRETADKLALTRTESVKPEPEITAPPHSRFSRSFKTVLIAQCAFTGFFSTIAGAIYYPVLSVIERKFDIDEELVNVTVVVYFVFQGLAPTFMGGFADSLGRRPVVLVAIVIYFGACIGLACAQTYAQIIVLRCLQAAGISPVIAINSGIMGDVTTRAERGGYVGYVAGFQVLGSAFGALIGAGLSSRWGWRAIFWFLAIGSGICFLASFLILPETKRNISGNGSVTPKSYLNRAPILVLPTVRKSLHLDNPDYETLELPTQLNLLAPFKILKAYEICILMLVAGLQFAMYTTHLT... | Function: Multidrug resistance transporter involved in resistance and adaptation to quinidine and to the herbicide barban (4-chloro-2-butynyl [3-chlorophenyl] carbamate). Implicated in potassium uptake.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59618
Sequence Length: 542
Subcellular Location: C... |
Q59XM0 | MSHSPNLSPQISNDIIDADTTSLASTETQQNIQHSQIHPIGHHGREQSEEPQNTTKTTTTTTNKIHTTTPSVDPDLGPLRELEQDLSSLESQQEQYLSQKPTSTSIKTNKVPLRERRGLLAQIVLIPEYEDARDYPNKIKYLIVFIIAFASLAGPFGTSVMLPAIDDIVNDLNTNVSTVNVSVGIYLLSLGIFPLWWSSFSERFGRRSVYMVSFTLFVAFSIGTALSPNIAALIVLRVLQGGSSASVQAVGAGTIADLFIPQERGQAMGLYYLGPLAGPFLAPILGGAVSQAWGWRATQWLLMIISACSFVLITFFLPET... | Function: MFS antiporter that does not display functional linkage as drug transporter and performs functions that significantly affect biofilm development and virulence. No substrate for transport has been identified yet, but plays an important role in the growth in the host.
Location Topology: Multi-pass membrane prot... |
P38227 | MQAQGSQSNVGSLRSNCSDNSLPNNHVMMHCDESSGSPHSEHNDYSYEKTNLESTASNSREHRDNQLSRLKSEEYVVPKNQRRGLLPQLAIIPEFKDARDYPPMMKKMIVFLIAFSSMMGPMGTSIIFPAINSITTEFKTSVIMVNVSIGVYLLSLGVFPLWWSSLSELEGRRTTYITSFALLFAFNIGSALAPDINSFIALRMLCGAASASVQSVGAGTVADLYISEDRGKNLSYYYLGPLLAPLLSPIFGSLLVNRWPWRSTQWFMVILSGCNVILLTVLLPETLRKQDSKGAIAQILAERRIQVDNNERGEIQEDYQ... | Function: Multidrug resistance transporter involved in resistance and adaptation to quinidine and to the herbicide barban (4-chloro-2-butynyl [3-chlorophenyl] carbamate).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 77287
Sequence Length: 689
Subcellular Location: Cell membrane
|
E0TW64 | MANKSAEHSHFPWKHIVGFALSIVLTLLALWVAVYTDLSSSAKLWIIFGFAFIQAALQLLMFMHMTESENGGIQVGNTLFGFFGAIVIVLGSIWIFAAHYHHGDHMDGNPPGGAEHSEHSGHNE | Function: Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Major component for energy conversion during vegetative growth.
Catalytic Activity: 2 a quinol + O2 = 2 a quinone + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13601
Sequence Length: 124
Subcellular Loca... |
Q2FI20 | MSTIMKHTVGFIASIVLTLLAVYVTLYTSLTFHAKLTIIFGFAFVQAGLQLLMFMHLTEGKDGRLQTFKVIFALVITLCFVVGTYWVMQGGHSSHL | Function: Catalyzes quinol oxidation with the concomitant reduction of oxygen to water.
Catalytic Activity: 2 a quinol + O2 = 2 a quinone + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 10687
Sequence Length: 96
Subcellular Location: Cell membrane
EC: 1.10.3.-
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P39481 | MNIKRILKVALYTTNASDVGQMYIVLGIVALIIGSVNAALIRDQLSFNNLNAVDYYDAVTLHGIFMIFFVVMPLSTGFANYLVPRMIGAHDLYWPKINALSFWMLVPAVILAAISPLLGAVDLGWYMYAPLSVETTVNYGLGTNLIQIALILSGLSSTLTGVNFVMTITKMKKVPYLKMPLFVWGFFTTAILMIIAMPSLTAGLVFAYLERLWGTPFFDSALGGSPVLWQQLFWFFGHPEVYILILPAMGLVSELLPKMARREIFGYTAIALSSIAIAFLSALGVWMHHMFTAIDNTLVQIVSSATTMAIAIPSGVKVLN... | Cofactor: Binds 1 copper B ion per subunit.
Function: Terminal oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. SoxM forms the functional core of the enzyme complex.
Catalytic Activity: 2 a quinol + O2 = 2 a quinone + 2 H2O
PTM: SoxM is probably a precursor form of subu... |
P57232 | MQLSDFSFDLPKSLISFHPYFIRSTCRLMVMYGHTGMIFHKRFFNIIDEINSGDLIILNNTQVIPARFFGKKESGGKVEVLVEKILGINNILASIKNSKNINIGSKIFFGYKDKIKGSVVDCKNSFFEIFFHDNIDSAIDIINNIGEIPLPPYIKRFRNKLDVDLYQTVYKKKTGSIAAPTAGLHFDLPLLEALHNKGVDIDYITLHIGSGTFQPIRRVQIEEHIMHSESVEVSSSVIQKIKSCKKKGGRIIAVGTSTLRALESAYHSSEWSDSQDFISDTNIFIYPGYKHNIVDALITNFHFPESTLIMLVCSFLGYKN... | 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... |
P44595 | MRVSDFNFDLPDELIARYPKTDRVSCRLLQLNGENGEIFHRTFSDVLDLIDEGDLLIFNNTRVIPARMFGRKASGGKIEVLVERMLDEHRFLAHIRSSKSPKEGAELFLGEDKLGENNGIKAVMKARHGALFEVELSDKSTALLDVLQTIGHMPLPPYIDRPDEEADQECYQTVYSKVPGAVAAPTAGLHFDENLLEKLKAKGVNFEFVTLHVGAGTFQPVRVENIEDHVMHAEYVEVSQEVCNAIIATKKAGKRVIAVGTTSVRSIESAALSAEEFGNPDLIEPYFSDTSIFIYPGKKFRVVDCLITNFHLPESTLIML... | 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... |
Q2SDV0 | MRVDDFDFELPPELIARRPLAERSSSRLLCLDAETGEINHRGFKDLLGMVNPGDLLVFNDTRVIPARLFGQKRSGGKVEVMVERVVSMTEMLAHVRASKAPKPGVEILIEENYVLTMVEREGDLFRLRVSQGGSVSELLERCGHMPLPPYIDREDDLSDRERYQTVYSRQPGAVAAPTAGLHFDEALLLAMSQKGVETAFVTLHVGAGTFQPVRVDVVQDHQMHSEYLEVSADVCERVRQVKAAGGRVVAVGTTAVRALETASRSGSIEPYAGDTSIFIYPGYEFVTVDALVTNFHLPKSTLLMLVSAFAGREHILAAYQ... | 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... |
B8CXG1 | MKVEEFDYELPEELIAQKPLPNRDDSRLMVLHRKTGEIEETVFKNIIKFLEPGDLLVLNDTKVIPARLFGEKIPSGTRIEVLLLKSITEGLWEVLVRPGRRMKKGNRVSFGDGKLVGIVKDYTDFGGRIMQFEYDGDFDKVIEELGEMPLPPYITRKVEDKGRYQTVYARKKGSVAAPTAGLHFTDRLLKKIKEQGIGIIYLTLHVGLGTFRPVRAENVEDHKMHSEYFEVSTDVVNRIKETKEKGKKVIAVGTTVTRALESAAVEKRHLKAMRGWTDIFIYPGYNFKVIDGLITNFHLPKSTLLMLVSAFAGKDMVMSA... | 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... |
B0TF76 | MEVALYDYELPKEAIAQTPVEPRDASRLMVLERRTGAVDHRIFRDLVHILHPGDLLVVNRTRVIPARLFGKKRDSDVTVEIVLLTPMGDDRWEVLVRPGRRLKPGVFVDLGEGRLAAEIVETTDFGGRVVRFHYSGDFDTLIDEIGQMPLPPYIETALPRQEAERYQTVYSQERGSAAAPTAGLHFTPQLLEDLKKRGIEITSVLLHVGLGTFRPVQVDRIEEHKMHSEFFQVDPEAARAIAKAKQEGRRVIAVGTTVARTLETAAGLHNGTVAAGSGWTDIFIYPGYTFQCIDGLITNFHLPRSTLLMLVSAFAGREQV... | 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... |
O25702 | MKEFDLESYDYYLPKELIASYPVLPKEKAKLLVYERRSQKITHTTFEHVLDFFPKNALIVLNDTKVIKARLFGSKHAFLPSKTTEVFFHRFFKNNTALTQIKGKIKVGDKIFFDANYHAEVLELLHNGQRLIAFYDNKTPLNQENILKLLEQYGHMPLPPYIKRADESLDAHEYQSVFAKHMGAVAAPTASLHFSQNTLEKLLKDFKHAFLTLHVGAGTFLSVETKDIREHQIHTEVLRIPKKSQEILQKSQEILCVGTTALRSVEYFKRLENPNQEAFECDIFLHFANPILHVNYLLTNFHLPKSSLLMLVSTMIGLEK... | 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... |
Q01SU0 | MNLSEFDYHLPDELIAQEALADRAASRMLVVHREQGRWEDRCFRDLPEFLRPGDCLVLNDSRVFPARLFGHRSGVHSLAVGKNNPKRHEFLSGAVEVFLLRAVSQDGRDWQALVRPGRKMRTGERIVFDEGLEAEIIARGEFGERTVRFLGSGDLYAAFDRIGHVPLPPYIKRDDSPADRERYQTVFAREKGSVAAPTAGLHFTPEVIERCQAAGADVATVTLHVGLGTFQPLHQEVVEEVKLHTEHYRITADNAGKIGAATRVVAVGTTSVRTLETAARDGVLEGETDIFLYPGVPFRRTGAMLTNFHLPRTSLLVLVS... | 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... |
Q1QVW9 | MSDLPRHSPRRQHAGESAVTAITSPEDTTKAVVIYSGGMDSYTVLHRALRAGFEVHALSFHYGQRHSRELETAHDVCQRLGIAHQVVDIRAIHGLIGNSALTDATQTMPDGDYDADNMAATVVPNRNMILLSLAIGHAVNIGANVCFYGAHGGDHVLYPDCRPEFVERMNDVAAIADFTPVRIAAPYLHASKEEILADGLAMGLDYAQTWTCYLGAERSCGHCGSCRERLAAFAAQGVTDPLVYAGAGASD | 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): 26934
Sequence Length: 2... |
B5EDQ7 | MQKKAVILYSGGLDSTTCLAIAKEQGFAPYALSFSYGQRHQQELEVAKLNARPMGAVDHLLVEFDLRKMGGSALTSDIEVPKEGVGEEIPVTYVPARNTIFLSFALGWAETLDCFDIFIGVNALDYSGYPDCRPEFISAYETMANLATKAGVEGKRLKIHTPLISLTKAEIIQKGLSLGVDYSKTHSCYDPAEDGAACGRCDSCRLRLKGFAEAGVTDPVKYQKL | 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): 24499
Sequence Length: 2... |
Q97D53 | MEISINKEKALVVFSGGQDSTTCLFWAKKRYKEVVAVSFDYNQKHKLELECAKDICKKHGVEHHILDMKLLNQLAPNSLTRADMKVDEDAPKDGPPNTFVDGRNLLFLSFAAVFAKQRGINNIITGVSQSDFSGYPDCRDVFIKSLNVTLNLAMDYQFVLITPLMWIDKAETWKLADDLGVLDIVKNETLTCYNGIKGNGCGECPACKLRKNGYVEFKRLYK | 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): 25054
Sequence Length: 2... |
B2IUR7 | MKAVILLSGGLDSSTILYKAKADGCECHAISFDYQQRHRQELQSALTVAKKAAIAKHQVVNFDLRQWGGSALTDDAIDLPQQRSLDEMSQNIPVTYVPARNTIFLSFALGYAEAIAAERVYIGVNALDYSGYPDCRPDYIEAMQEVFRLGTKQGREGQPIKIVAPLINLKKTEIIQLGNELGVPWELTWSCYAGNDVACGVCDSCRLRLAAFAELGLVDPLVYA | 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): 24632
Sequence Length: 2... |
Q8ETE9 | MTGKKAVVILSGGLDSTTCMGVGKEAGYELYPISFHYGQRHDREIENAKKVASYFNVTEHKVFSLEFLKEIGGSSLTDQSMEVSQEGVGEDVPNTYVPGRNTIFLSIAASYAEAIGAEKIYVGVSAVDYSGYPDCRPEFIEAMQQTIYQGTNANPAMTIEAPLIDLSKGDTVKLGMKLNVPYHLTTSCYLGGEEACGECDSCRLRLQGFEEAGATDPIKYM | 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): 24018
Sequence Length: 2... |
A6LIS9 | MKQQDAALVCFSGGQDSTTCLFWAKKHFSRVEAVCFTYGQKHSLEIEVARKIAADADVPFQLLDVSLISQLDPNCSLTNASIEMDQEKPEDSYPNTFVPGRNMVFLTFAAILARGKGIYHLVTGVSEADYSGYPDCRDTFVRSLNVTLNLAMDEQFVIHTPLMDRDKSEVWELSDELGVFDLVRTQTLTCYNGVMAEGCGHCPACKLRKDGLEKYLKRKEENQK | 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): 25153
Sequence Length: 2... |
Q146Z6 | MIRKDAKRSALVLFSGGQDSATCLAWALERYETVETLGFDYGQRHRVELECREGFRNAVVRAFPAWADRLGEDHMIDLSVLGAISDTAMTREIEIEATANGLPNTFVPGRNLMFMTIAAAIAYRRGLQVLVGGMCETDFSGYPDCRDDTMKALQVALNLGMDTRFLLETPLMWLDKADTWRLAHELGGAELVELVRVETHTCYLGERAELHAWGFGCGECPACRLRKRGYEAYLAGENVTEPV | 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): 27119
Sequence Length: 2... |
O66626 | MKWEISKTFRFEAGHRVWKQNLTYGRGAQFTKEKPVNKCVNLHGHSYVLEVTVGSDTLSEQDMVMDFYHVKNALKGLIEEIDHSFIIDVNDPMYPELKDVAEKYGAMKIFPVEFCPTAEALAKFFYDFLKKRLEEAGLLGEVKVVKVVLWETATSKAEYKEE | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde.
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphat... |
O29809 | MEEEMIIGISTSFSAAHSIPGHKKCGKVHGHNFKVEVEISGKVKENGMVMDFFDLKRIVNEVVAKFDHTLLNEQIEIPTSENICLRIFSELAEKGLNVRRVRVAENEDKWAEIRR | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde.
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphat... |
O31676 | MLSQIYPQAQHPYSFELNKDMHISAAHFIPRESAGACSRVHGHTYTVNITVAGDELDDSGFLVNFSVLKKLVHGNYDHTLLNDHEDFSQDDRYSLPTTEVVAKTIYDNVQAYLDTLENKPTCVQVFVRETPTSYCVYRPKKGGLNG | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde.
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphat... |
Q8K9D8 | MKTIIFKDFQFEAAHYLPYVPKMHKCRRLHGHSFFVRLELKDKINEKNGWIIDYAEIKLAFQPIYDQLDHHFLNDIPGLENPTSEILAKWIWHRLKPKLSILNTIIIKETCTSGCIYQGF | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde.
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphat... |
P65871 | MMSTTLFKDFTFEAAHRLPHVPEGHKCGRLHGHSFMVRLEITGEVDPHTGWIIDFAELKAAFKPTYERLDHHYLNDIPGLENPTSEVLAKWIWDQVKPVVPLLSAVMVKETCTAGCIYRGE | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde.
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphat... |
P44123 | MFKISKEFSFDMAHLLDGHDGKCQNLHGHTYKLQVEISGDLYKSGAKKAMVIDFSDLKSIVKKVILDPMDHAFIYDQTNERESQIATLLQKLNSKTFGVPFRTTAEEIARFIFNRLKHDEQLSISSIRLWETPTSFCEYQE | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde.
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphat... |
B0R9W7 | MRSAQSKRSQSTATGERTLHIGRDRPIRISAGHRLQHHDGKCSRPHGHNYEISVEITGQLTDEGWVVDKGTVTAVVSDWDHRFLLEDGDPLVDAFREAGDGDAVVVLEQPPTAEVMGVVLERKLHDALPETVSAVSVTVAETPALTAGPN | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde.
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphat... |
O25587 | MVIRRLYQFCASHVVRNCSSLKCAQNIHGHNYEVEVFIETNRLDNANMALDFGLMQQEMQVFIESFDHAHHFWDKESLEFQRFIENHCVRYVKCSFNLSAESYALMFLYYLTKILQKSVFSNDEGELKVSSVRVHETKNGYAESFLKDLENPHFKSLVHDHCVSFSQGIQNLWHDKDFFNKIISDEKQCFFHAKPLHQIP | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde.
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphat... |
Q58668 | MMLELNGLHAGLRFSSAHIVFGHPTCGVIHGHSYYVDVKLYGERAGDFKFVCDFKIIKKIVKEICDELDHKLILPKNHEHVYYELRDKTLYFKYENKEYSIPVEDVILLPIPSTTAEDLAIYFANEIADRLKNLGFSNINWIEVSINEGIGQGACYRKYLEVK | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde.
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphat... |
O27296 | MVMMKIVINGIHANLRFSAAHMIPEHESCGCIHGHSYIVDVKVEGKRSGKHGFVADFKDVKDIVRRICSEFDHKLLIPLRNPLINFTSTTRTVKFEIAGKKYSIPEEDCCLMDLESSSAEELSRYFAATLFKELSSKYDISSVEVCVNEGIGQGAIYTISR | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde.
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphat... |
Q9UXZ4 | MKRVVSIKRRIYWTKEFDSSHFLELEYESKCRRLHGHTYRVEVEIEGEPNEHGMIFDFNHLSELIKTLDHKVIVSEKWVRYEEGYVLIEKNDKLLKLPRSEVVVIDKPNVTAEYIAEWISERILENAGENVREIRVRVWEDPRSYAEITLTLKPQGS | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde.
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphat... |
Q6ARX8 | MTENINAGIPLGKQVGHSETYDPSHLFPVARREARKSLGLADDLPFSGPDIWNAYELSWLDSKGKPCVALGEITFPCTSENIIESKSLKLYLNSFNLTRFTSTARVKEIIREDLSRVAGAEVEVKILTPEEFTEVTISAPEGSCIDDLELEEEINAYRPTANYLSTGPEETEEELYTNLLRTNCPVTGQPDWATVIINYRGKAIDQRGLLRYIISFRQHEGFHENCVERIFMDILNRCAPARLTVYARFTRRGGLDINPYRTTHAEHFVNLRLARQ | 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): 31313
Sequence Length: 276
Pathway: tRNA modification; tRNA-queuosine ... |
Q72DG6 | MTTRSTDQTEHLRALGQKTPYPAAGPSTDLLEAFPNRFPDRPYIVSIAFPEFTSLCPVTGQPDFATIVVEYIPDQFCVESKSFKVYMFAFRDHQSFMETITNTILDDMTTKLQPLWCRVKGLFTPRGGTQLHVFAERFKEVEPARAQALRDMVSEWKRENNRHGA | 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): 18924
Sequence Length: 165
Pathway: tRNA modification; tRNA-queuosine ... |
C5BR59 | MSDHADTLLGKDTTYPEHYDPALLQPIPRERSRETMVRGDLPFTGVDIWTAYELSWLDSSGKPHVAVGEFWVPADSSAIIESKSLKYYLNSLNQHRFATREQARQAIAGDLSEAAGGEVQVTLFDIDDYSNVGTLPGTCVDTLDAPVYVYQPDASLLKFVDQPGEQQQLFSHLLKSNCPVTGQPDWATVWVQCSGLTLVPESFLAYVVSFRGHQDFHENCVERIFTDLMAGGKLQDLAVYARYTRRGGLDINPLRFSGAQDPEALEQLVSKRIARQ | 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): 30771
Sequence Length: 276
Pathway: tRNA modification; tRNA-queuosine ... |
Q9WZP8 | MPKAEGRIFDFKGHDAIRTDFLEAIDFDGKDEYIKIETDEFSAVCPFSGLPDIGRVIIEYYPDGGKIVELKSLKYYFVSFRNVGIYQEEATKRIYEDLKNLLKTDRIRVTVIYNIRGGIKTTTQMGSLEGKKSGEVE | 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): 15675
Sequence Length: 137
Pathway: tRNA modification; tRNA-queuosine ... |
B8GTL3 | MSSQPSKDLETFENPQPGRDYTIRIRVPEFTCLCPKTGQPDFATLFLDYVPRARCVELKSLKLYVWAFRDQGAFHEKVTNEILNDLVAATDPNFMRLTAEFNVRGGVYTTVVAEHRHPDWQPPVPVTLP | 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): 14766
Sequence Length: 129
Pathway: tRNA modification; tRNA-queuosine ... |
Q3M4S2 | MSNSSPETVSQPSQEVKYGEREIAEGQLITFPNPRVGRRYDINITLPEFTCKCPFSGYPDFATIYITYVPDERVVELKALKLYINSYRDRYISHEESANQILDDFVAACDPLEATVKADFTPRGNVHTVVEVKHRK | 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): 15548
Sequence Length: 136
Pathway: tRNA modification; tRNA-queuosine ... |
A1WS75 | MNPPESSPLGKASACVDQYDATLLFPIARADQRAELGISGAAPFFGADLWTAFELSWLNQRGKPQVALAHITVPCETPRIVESKSFKLYLNSFSNTRFADAAQVQARIRADVSAAVWRGAASAGSVGVTLLGPDRFAQELMQELDGLSLDRLDVQCTQYQPAPELLSAQHDAAPVSERLTSQLLKSNCPVTGQPDWASVQIAYRGPPIDQEGLLQYLVSFRNHSGFHEQCVERIFMDLWTRCQPIELTVYARYTRRGGLDINPLRTSHPQGLPRNMRTARQ | 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): 31097
Sequence Length: 281
Pathway: tRNA modification; tRNA-queuosine ... |
A5CWU3 | MSSQPNKNLKVFDNPNIERNFIIQINMPEFTCLCPKTGQPDFATLYLEYIADKVCIELKSLKMYIWSYRSKGEFHEAVTNKILDDLIQISNPRFMRLKAIFNVRGGIYTTIIAEYQQKNWTFKTKIDLQYQG | 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): 15541
Sequence Length: 132
Pathway: tRNA modification; tRNA-queuosine ... |
Q9KTK0 | MSKYSDAKELASLTLGKKTEYANQYDPSLLQPVPRSLNRNDLHLSATLPFQGCDIWTLYELSWLNQKGLPQVAIGEVSIPATSANLIESKSFKLYLNSYNQTRFASWDEVQTRLVHDLSACAGETVTVNVKSLNEYTAEPIVTMQGECIDDQDIEIANYEFDDALLQGAAQGEEVSEVLHSHLLKSNCLITNQPDWGSVEIAYHGAKMNREALLRYLVSFREHNEFHEQCVERIFTDIMRYCQPQSLTVYARYTRRGGLDINPFRSSHQSAPNHNQRMARQ | 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): 31969
Sequence Length: 281
Pathway: tRNA modification; tRNA-queuosine ... |
Q87RS6 | MSKYSDAKELAGLTLGKKTEYANQYDASLLQPVPRSLNRDDLELGDTLPFLGHDIWTLYELSWLNSKGLPQVAVGEVYIPATSANLIESKSFKLYLNSYNQTRFASWEEVAERLTQDLSACAGEKVLVEVNPVGHYTNQPIVTMEGECIDDQDIEINSYDFDADLLAGAAGEDQVEEVLHSHLLKSNCLITNQPDWGSVEIRYQGAKIDREKLLRYLVSFREHNEFHEQCVERIFTDLMKYCQPNKLTVFARYTRRGGLDINPYRSTEQDKPAHNHRMARQ | 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): 32113
Sequence Length: 281
Pathway: tRNA modification; tRNA-queuosine ... |
D4GV73 | MDDRVHPEVRRTATEIDTMEIRGAATIADAAARALRTQATESDAADAEAFRAELRATARTLHETRPTAVSLPNALRYVLRDMSSTTVEGLRQSVVDSADEFCARLERAQADLGQVGANRLRDGDTIMTHCHSTDALACVEAAVEQGKHIEAVVKETRPRNQGHITAKRLHELGVPVTLIVDSAARRYLNDVDHVLVGADAVAADGSVINKIGTSGLAVNARERGTPIMVAAQTLKLHPGTMTGHTVDIEMRDTAEVVDDDTLADLGNPTVKNPAFDVTPPRYVDAIVTERGQFPPESIVILMRELFGEGTSEPWAEPSPR... | Function: Catalyzes the isomerization of ribose 1,5-bisphosphate (R15P) to ribulose 1,5-bisphosphate (RuBP), the CO(2) acceptor and substrate for RubisCO. Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and RubisCO.
Catalytic Activity: alpha-D-ribose 1,5-bisphosphate = D-ribulose 1,5-b... |
Q57586 | MVFKMSEMDIIKETYEKIKNMEIRGAGRIGRAAAKALKEYALKISHLNEEEFKNKMREAGNILISARPTAVSLPNVVKYVLKGLNEENPKERVIERADEFINSSLKAIENIGKFGANRIKDGDTILTHCNSEAAISVIKTAYDEGKDIKVFCTETRPRNQGYLTAKTLYDYGIDVTLIVDSAVRYFIKEIDIVVVGADAITANGCLVNKIGTSQIALIANESRVPFLTAAETYKFHPKTIVGELIEIEERSPEEVAVFEDKYKGIKIRNPAFDVTPAKYIDAIITEVGLIPPQGAWYIIEKYFGWLEK | Function: Catalyzes the isomerization of ribose 1,5-bisphosphate (R15P) to ribulose 1,5-bisphosphate (RuBP), the CO(2) acceptor and substrate for RubisCO. Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and RubisCO.
Catalytic Activity: alpha-D-ribose 1,5-bisphosphate = D-ribulose 1,5-b... |
Q5JFM9 | MAVVKEVLEIAEKIKNMEIRGAGKIARSAAYALQLQAEKSKATNVDEFWKEMKQAAKILFETRPTAVSLPNALRYVMHRGKIAYSSGADLEQLRFVIINAAKEFIHNSEKALERIGEFGAKRIEDGDVIMTHCHSKAAISVMKTAWEQGKDIKVIVTETRPKWQGKITAKELASYGIPVIYVVDSAARHYMKMTDKVVMGADSITVNGAVINKIGTALIALTAKEHRVWTMIAAETYKFHPETMLGQLVEIEMRDPTEVIPEDELKTWPKNIEVWNPAFDVTPPEYVDVIITERGIIPPYAAIDILREEFGWALKYTEPW... | Function: Catalyzes the isomerization of ribose 1,5-bisphosphate (R15P) to ribulose 1,5-bisphosphate (RuBP), the CO(2) acceptor and substrate for RubisCO. Only accepts the alpha-anomer of D-ribose 1,5-bisphosphate as substrate, being inactive on the beta-anomer. Displays a strict substrate specificity, since other phos... |
Q6L440 | MKTVIARTSSKLARTPRMNEEIVGFEDVIENLRKKLLSETKGQDVISIHGMPGLGKTTLANRLYSDRSVVSQFDICAQCCVSQVYSYKDLLLSLLRDAIGDESGSRELPDNELADMLRKTLLPRRYLILVDDVWDNSAWDDLRGCFPDVNNRSRIILTTRHHEVAKYASVHSDPLHLRMFYEDESWKLLEKKVFGEQSCSPLLKDVGLRIAKLCGKLPLSIVFVAGTLSEMEKEVECWEQMANNLGGPKLSSFLEDRVIDISRLIRLWISESFIKSSEGRSLEDIAEGYLENLIGRNLVMVTQRADSDGMVKACRLHDVL... | Function: Confers resistance to late blight (Phytophthora infestans) races carrying the avirulence gene Avr1. Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein. That triggers a defense system including the hypers... |
Q9SN35 | MAGYRADDDYDYLFKVVLIGDSGVGKSNLLSRFTRNEFSLESKSTIGVEFATRSLNVNEKVIKAQIWDTAGQERYRAITSAYYRGAVGALLVYDVTRHSTFENVERWLRELRDHTDPNIVVMLVGNKSDLRHLVAVQTEDAKSFAENESLYFMETSALESTNVENAFSEVLTQIYHVVSKKAMEAGEDSGNVPSKGEKIDVDVSAVKKTGCCSN | Function: Intracellular vesicle trafficking and protein transport.
Location Topology: Lipid-anchor
Sequence Mass (Da): 23870
Sequence Length: 214
Subcellular Location: Early endosome membrane
|
Q9LK99 | MAAYRADDDYDFLYKVVLIGDSGVGKSNLLSRFTRNEFSLESKSTIGVEFATRSIHVDEKIVKAQIWDTAGQERYRAITSAYYRGAVGALLVYDVTRHVTFENVERWLKELRDHTEANIVIMLVGNKADLRHLRAVSTEDAKAFAERENTFFMETSALEALNVENAFTEVLSQIYRVASKKALDIGDDHTTLPKGQSINVGSKDDVSEVKKVGCCSS | Function: Intracellular vesicle trafficking and protein transport.
Location Topology: Lipid-anchor
Sequence Mass (Da): 24283
Sequence Length: 217
Subcellular Location: Cell membrane
|
Q1PEX3 | MGTYKAEDDYDYLFKVVLTGDSGVGKSNLLSRFTRNDFSHDSRSTIGVEFATRSIQVDDKIVKAQIWDTAGQERYRAITSAYYRGAVGALLVYDVTRHVTFENVERWLKELRDHTDANTVIMLVGNKADLNHLRAISTEEVKDFAERENTFFMETSALEAINVENAFTEVLTQIYRVVSKKALDAGDDPTTALPKGQMINVGSRDDVSAVKKSGCCAT | Function: Intracellular vesicle trafficking and protein transport.
Location Topology: Lipid-anchor
Sequence Mass (Da): 24337
Sequence Length: 218
Subcellular Location: Cell membrane
|
O04486 | MARRPDEEYDYLFKVVLIGDSGVGKSNLLSRFTRNEFCLESKSTIGVEFATRTLQVEGRTVKAQIWDTAGQERYRAITSAYYRGALGALLVYDVTKPTTFENVSRWLKELRDHADSNIVIMLIGNKTDLKHLRAVATEDAQSYAEKEGLSFIETSALEALNVEKAFQTILSEVYRIISKKSISSDQTTANANIKEGQTIDVAATSESNAKKPCCSSS | Function: Intracellular vesicle trafficking and protein transport.
Location Topology: Lipid-anchor
Sequence Mass (Da): 24108
Sequence Length: 217
Subcellular Location: Endosome membrane
|
Q96283 | MTHRVDQEYDYLFKIVLIGDSGVGKSNILSRFTRNEFCLESKSTIGVEFATRTTQVEGKTIKAQIWDTAGQERYRAITSAYYRGAVGALLVYDITKRQTFDNVLRWLRELRDHADSNIVIMMAGNKSDLNHLRSVAEEDGQSLAEKEGLSFLETSALEATNVEKAFQTILGEIYHIISKKALAAQEAAAANSAIPGQGTTINVDDTSGGAKRACCSS | Function: Intracellular vesicle trafficking and protein transport.
Location Topology: Lipid-anchor
Sequence Mass (Da): 23849
Sequence Length: 217
Subcellular Location: Endosome membrane
|
Q9FJN8 | MTSGGGYGDPSQKIDYVFKVVLIGDSAVGKSQILARYARDEFSLDSKATIGVEFQTRTLVIDHKSVKAQIWDTAGQERYRAVTSAYYRGAVGAMLVYDITRRQTFDHIPRWLEELRAHADKNIVIILIGNKSDLVDQRAIPTEDAKEFAEKEGLFFLETSAFNATNVESAFSTVLTEIFNIVNKKSLAASEDQENGNPGSLAGKKIDIVPGPGQVIPNKSNMCCNS | Function: Intracellular vesicle trafficking and protein transport.
Location Topology: Lipid-anchor
Sequence Mass (Da): 24842
Sequence Length: 226
Subcellular Location: Cell membrane
|
Q9SMQ6 | MAGGGGYGGASGKVDYVFKVVLIGDSAVGKSQLLARFARDEFSMDSKATIGVEFQTRTLSIEQKSIKAQIWDTAGQERYRAVTSAYYRGAVGAMLVYDMTKRETFEHIPRWLEELRAHADKNIVIILIGNKSDLEDQRAVPTEDAKEFAEKEGLFFLETSALNATNVENSFNTLMTQIYNTVNKKNLASEGDSNNPGSLAGKKILIPGSGQEIPAKTSTCCTSS | Function: Regulator of membrane trafficking. May be required for secretion of cell wall components in cells.
Location Topology: Lipid-anchor
Sequence Mass (Da): 24407
Sequence Length: 224
Subcellular Location: Early endosome membrane
|
Q9FE79 | MSKFQSNFNQKIDYVFKVVLIGDSAVGKSQLLARFSRNEFSIESKATIGVEFQTRTLEIDRKTIKAQIWDTAGQERYRAVTSAYYRGAVGAMLVYDITKRQSFDHVARWLEELRGHADKNIVIMLIGNKTDLGTLRAVPTEDAKEFAQRENLFFMETSALDSNNVEPSFLTVLTEIYRIVSKKNLVANEEGESGGDSSLLQGTKIVVAGEETESKGKGCCGTS | Function: Intracellular vesicle trafficking and protein transport.
Location Topology: Lipid-anchor
Sequence Mass (Da): 24839
Sequence Length: 223
Subcellular Location: Cell membrane
|
Q9LH50 | MSNLYGDYNQKIDYVFKVVLIGDSAVGKTQLLARFARNEFSVDSKATIGVEFQTKTLVIDNKTVKAQIWDTAGQERYRAVTSAYYRGAVGAMLVYDMTKRQSFDHMAKWLEELRGHADKNIVIMLIGNKCDLGSLRAVPTEDAQEFAQRENLFFMETSALEATNVETAFLTILTEIYRIISKKSLTADDDDADGNSSLLKGTRIIIPSEQESGKRGGCCGKS | Function: Intracellular vesicle trafficking and protein transport. Plays an important role in the regulation of pollen tube tip growth.
Location Topology: Lipid-anchor
Sequence Mass (Da): 24720
Sequence Length: 222
Subcellular Location: Cytoplasmic vesicle membrane
|
P28187 | MSDDDERGEEYLFKIVIIGDSAVGKSNLLTRYARNEFNPNSKATIGVEFQTQSMLIDGKEVKAQIWDTAGQERFRAVTSAYYRGAVGALVVYDITRSSTFENVGRWLDELNTHSDTTVAKMLIGNKCDLESIRAVSVEEGKSLAESEGLFFMETSALDSTNVKTAFEMVIREIYSNISRKQLNSDSYKEELTVNRVSLVKNENEGTKTFSCCSR | Function: Intracellular vesicle trafficking and protein transport. Binds GTP and GDP and possesses intrinsic GTPase activity.
Location Topology: Lipid-anchor
Sequence Mass (Da): 23981
Sequence Length: 214
Subcellular Location: Golgi apparatus membrane
|
P34142 | MTDTEKSFKVVLLGEGCVGKTSIVFRYIDNIFNDKHLMTQHAGFFQKHINIGGKRICLTIWDTAGQERFHALGPIYYRGSQGALVVYDITDNDSFIKAKNWIKELKTMLGNDISLCIIGNKCDLEKTRVIPLADAEAYAKSVGAIHYSTSAKLNKGIEELFLDLTRRMILNSSGVVIHSNTNTTGQTTNRSERIPIVPDSDSGNKQPGCCSN | Function: Involved in the regulation of phagocytosis.
Location Topology: Lipid-anchor
Sequence Mass (Da): 23490
Sequence Length: 212
Subcellular Location: Cell membrane
|
Q9UL25 | MAAAGGGGGGAAAAGRAYSFKVVLLGEGCVGKTSLVLRYCENKFNDKHITTLQASFLTKKLNIGGKRVNLAIWDTAGQERFHALGPIYYRDSNGAILVYDITDEDSFQKVKNWVKELRKMLGNEICLCIVGNKIDLEKERHVSIQEAESYAESVGAKHYHTSAKQNKGIEELFLDLCKRMIETAQVDERAKGNGSSQPGTARRGVQIIDDEPQAQTSGGGCCSSG | Function: Small GTPase involved in membrane trafficking control . During the mitosis of adherent cells, controls the endosomal trafficking of integrins which is required for the successful completion of cytokinesis . Regulates integrin internalization and recycling, but does not influence the traffic of endosomally tra... |
P35282 | MAAAGGGAAAAAGRAYSFKVVLLGEGCVGKTSLVLRYCENKFNDKHITTLQASFLTKKLNIGGKRVNLAIWDTAGQERFHALGPIYYRDSNGAILVYDVTDEDSFQKVKNWVKELRKMLGNEICLCIVGNKIDLEKERHVSIQEAESYAESVGAKHYHTSAKQNKGIEELFLDLCKRMIETAQVDERAKGNGSSQAGAARRGVQIIDDEPQAQSSGGCCSSG | Function: Small GTPase involved in membrane trafficking control . Regulates integrin internalization and recycling, but does not influence the traffic of endosomally translocated receptors in general . As a result, may regulate cell adhesion and migration . During the mitosis of adherent cells, controls the endosomal t... |
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