ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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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: 4.1.1.23
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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: 4.1.1.23
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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
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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
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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: 4.1.1.23
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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 | MTKYIFVTGGVVSSLGKGIVAASLGRLLKNRGLNVTIQKFDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDINLNKFSNVTTGKIYSTVLKKERRGDYLGGTVQVIPHITNELKDRVYRAGKETNADVVITEIGGTVGDIESLPFLEAIRQMKSDIGRENVMYIHCTLVPYIKAAGELKTKPTQHSVKELRSLGIQPNIIVVRTEMPISQDMKDKIALFCDIDTKAVIECEDADNLYSIPLELQKQGLDKLVCEHMKLACKEAEMSEWKELVNKVSNLSQTITIGLVGKYVELPDAYISVVESLRHAGYAFDTDVKVKWINAEEVTENNIAELTSGTDGIIVPGGFGDRGVEGKIVATKYARENNIPFLGICLGMQVASIEYARNVLGLKGAHSAEIDPSTQYPIIDLLPEQKDVEDLGGTLRLGLYPCKLEEGTKAFEVYQDEVVYERHRHRYEFNNEFRQQMEEQGFVFSGTSPDGRLVEIIELKDHPWFVASQFHPEFKSRPTRPQPLFKGFIGASVEAANQK | 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
Sequence Mass (Da): 59718
Sequence Length: 535
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
EC: 6.3.4.2
|
Q8AA75 | MGETKYIFVTGGVASSLGKGIISSSIGKLLQARGYNVTIQKFDPYINIDPGTLNPYEHGECYVTVDGHEADLDLGHYERFLGIQTTKANNITTGRIYKSVIDKERRGDYLGKTIQVIPHITDEIKRNVKLLGNKYKFDFVITEIGGTVGDIESLPYLESIRQLKWELGKNALCVHLTYVPYLAAAGELKTKPTQHSVKELQSVGIQPDVLVLRAEHPLSDGLRKKVAQFCNVDDKAVVQSIDAETIYEVPLLMQAQGLDSTILEKMGLPVGETPGLGPWRKFLERRHAAETKEPINIALVGKYDLQDAYKSIREALSQAGTYNDRKVEVHFVNSEKLTDENVAEALKGMAGVMIGPGFGQRGIDGKFVAIKYTRTHDIPTFGICLGMQCIAIEFARNVLGYADADSREMDEKTPHNVIDIMEEQKAITNMGGTMRLGAYECVLQKGSKAYLAYGEEHIQERHRHRYEFNNDYKAQYEAAGMKCVGINPESDLVEIVEIPALKWFIGTQFHPEYSSTVLNPHPLFVAFVKAAIENEKN | 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
Sequence Mass (Da): 59864
Sequence Length: 537
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
EC: 6.3.4.2
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Q8SQI7 | MKYVIVSGGVISGVGKGIVSSSIGALLKSRGHVVTHFKIDPYLNYNAGRMHPYEHGEVYVLDDGHECDMDFGNYERFNGIKLSGANSIPGGRLLHDIVKCEREGSFLGKTLQINPHIIDEVIRRIRAVADTPVESFGGGQAAVPDVVVVELGGTVGEYESSIYTEALAKFQYVVGKANCAFVSVDYIVELETGEQKTKGIQMGCRNFRRFGLNYDIVICRGRREPNMETRRKISTSCWVKEENVLGLPNLESVYLAPMFLEKHGIVEALNRILGLDDKGMDRRMLDIFSMVGRRHRDGVRIGIVGKYAPEFDSYTSLVNALKFSGAHIGVNVEIVWINSESYSVCDFERCDGVVIPGGFGARGISGKIEAIRHARENGVPLLGICLGYQLSVIEMCRNILGMSDAFSEEFQPSGKNLVVRFISDENGVVDKRLRVGGYGVELRDGLVKKLYGGVETVRERHRHRFEVAQEKVRGLLQHGVRFVGFSSGGKKINVFEVESHPFFVGVQFHPEFNARPDRPHPLITGLVSASYERSK | 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 de novo pathway; CTP from UDP: step 2/2.
EC: 6.3.4.2
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Q2NAA7 | MARYIFITGGVVSSLGKGLMAASLGALLQARGYKVRIRKFDPYLNVDPGTMSPYQHGEVYVTDDGAETDLDLGHYERFTGVSARQSDNITSGRVYQDIIAKERRGDYLGATVQVIPHVTDAIKNFALADQDDLDFILCEIGGTVGDIESLPFMEAIRQLRNELEPMQTLSVHVTLVPYIAAAGELKTKPTQHSVRELASLGIKPDVLLCRAEHPLPDGERQKIANFCNVRKEAVIPALDAPSIYSVPLQYHEEGLDAEVLRGFGIVDAPAPDLSAWDDVTDRYFNPEGEVTIGVVGKYVGLQDAYKSLNEALVHGGLANRVKVNIRWIDAEVFEEDDAAIAAKLEPLHGILVPGGFGERGSEGKIASVRFARERKVPFFGICLGMQMACIEGAREAGHALASSTEFGETEEPVVGIITEWMTEEGLEKREAGGDLGGTMRLGAYEAKLDGNSHVSAIYGGATEISERHRHRYEVNAAYRDALEGQGLIFSGMSPDGLLPEIVERPDHPWFVGVQFHPELKSKPFDPHPLFSGFIKAALHQSRLV | 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
Sequence Mass (Da): 59464
Sequence Length: 544
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
EC: 6.3.4.2
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A6H0U1 | MNQTKYIFVTGGVTSSLGKGIIAASLAKLLQARGYRTTIQKFDPYINVDPGTLNPYEHGECYVTNDGAETDLDLGHYERFLNVPTSQANNVTTGRIYLSVIEKERRGEFLGKTVQVVPHITNEIKERMQLLGKSGDYDIVITEIGGTVGDIESLPYIESVRQLVWELGENNGIVIHLTLVPFLAAAGELKTKPTQHSVKTLMESGIKADILVCRTEYELSEDLRHKLALFCNVKREAVIQSIDASTIYDVPNLMLEEGLDKVALKKLDLPEKSTPDLKQWNEFLQKHKNPKHEVSIGLVGKYVELQDSYKSILEAFIHAGATNETKVNVISIHSEFLDVNSADEQLKGLDGILVAPGFGGRGIEGKIETVRYAREKNIPFLGICLGMQMAVIEYSRNVLGYTDANSTEMNQNTSHPVINLMEEQKTITDKGGTMRLGAWKCHLSENTLAHKIYGQSDILERHRHRYEFNSEYLEVLQKAGLKASGVNPETGLVEVIELENHPFFIGVQYHPEYKSTVLAPHPLFVSFIAAAVKHKNK | 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
Sequence Mass (Da): 59920
Sequence Length: 537
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
EC: 6.3.4.2
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Q2S538 | MQTKYIFVTGGVTSSLGKGIFSASLGRLLSDRGLDVTIQKFDPYINVDPGTMNPYEHGEVYVTNDGAETDLDLGHYERFLDQPTSQANNVTTGRVYMEVISKEREGAYLGKTVQVVPHIIDEIKHWMLKLGETGDYDVVITEIGGTVGDIEGQPYLEAIRQLRNELGPRNTMIAHLTLIPHLRAAGELKTKPTQHSVKELLAHGLQPDTIVCRSERSITAEVRRKISLFCNVEEEAVIQMLDAESIYEVPLLLRDEGTGELVVDRFYPKRGDENEKCSDTPDLSDWIGFLKRLKNPEETIPIALVGKYVEHQDAYKSITESFILAGVPDEVQVEVKYVPSEDLSPDTVESQLGDVAGVLVAPGFGDRGVEGKILAAQYAREHDVPFFGICLGLQCAIVEFARHVCGWDGAHSTEFDEDTAYPVIDLMEEQKEISDKGGTMRLGQYDCRIQDGSRAHEIYEADMVQERHRHRYEVNNVLRYKLLEEGMRFSGVNPDTDLVEIMELPDKRWFLGVQFHPEYRTTVGDPHPLFRSFVRACTAYAHEEDLVTSPQPPERKAVPLASVDM | 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
Sequence Mass (Da): 63430
Sequence Length: 565
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
EC: 6.3.4.2
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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
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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
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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
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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
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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
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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
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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 novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Subcellular Location: Cytoplasm
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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 biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
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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 biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
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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 biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
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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 via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Subcellular Location: Cytoplasm
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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 biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
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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 biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
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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 biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
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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: Peripheral membrane protein
Sequence Mass (Da): 9109
Sequence Length: 80
Subcellular Location: Cellular thylakoid membrane
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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: Peripheral membrane protein
Sequence Mass (Da): 8895
Sequence Length: 80
Subcellular Location: Cellular thylakoid membrane
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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: Peripheral membrane protein
Sequence Mass (Da): 9055
Sequence Length: 80
Subcellular Location: Cellular thylakoid membrane
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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: Peripheral membrane protein
Sequence Mass (Da): 9322
Sequence Length: 83
Subcellular Location: Cellular thylakoid membrane
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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: Peripheral membrane protein
Sequence Mass (Da): 8672
Sequence Length: 78
Subcellular Location: Cellular thylakoid membrane
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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: Peripheral membrane protein
Sequence Mass (Da): 8078
Sequence Length: 70
Subcellular Location: Cellular thylakoid membrane
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Q0CZH1 | MDPQQRLLLEVVYEALEDAGITLDEIQGSLTSVYCGCFTNDYNAMTTKDLEYYPKYTVTGTGNSILANRISYFYNLHGPSATVDTACSSSLVCFHLGAQSLRDAEADISIVVGSALHFDPNIFITMTDLGMLSTDGRCRHGDAAGSGYVRGEGIAAMVLKRQDRAQADGDHIRAVVRGTGVNHDGRKQGITLPSARAQADLITSTYERAGLEPAETTYVECHGTGTKAGDPRELRAVHEVFCRHRPDTLHVGSVKTNIGHLEGASGIAGLMKATMALEKKIIPPNMHFSTPNPEVDFKNWKLEIPTEPKVWEMGRRTIPRRASINSFGYGGTNAHAILEEYNSFGSKTTACQQPTVSLPPELAAMVERRPYLLPLTSHSERAGELWAERLAQYLTENEASVADVALSLSTRRTMHRFRSFAVSADMEKVIERIRDPPPGAAWKSKLDTIPRIGFVFTGQGAQWFGMARSLLEQCPLFLQTIRKCDRILQALPSHRPTWSVEAELLKSQQDTMLGRTEYSQPICTAVQLALVDVLAHWGVKPSGVVGHSSGELAATYAAGLLSFENALVAAYYRGVHMGSGAAAPGSMPGAMMAVGMTEAEVTAELEPYRGRIAIAAMNSPSSFTVSGDEDAVVELQQALTDRKVFARRLQVAQACVFVHSLVIKRY | 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 modular PKS of pytA . The acyl chain is then connected to an L-serine through the amide bond by the modular NRPS of pytA . A tetramic acid is formed and released from the PKS-NRPS pytA to give pyranterreone 5 with the help of the thioesterase pytI . Pyranterreone 5 could be methylated by pytC to afford pyranterreone 6 (Probable). Both pyranterreones 5 and 6 are subsequently oxidized by the FAD-linked oxidoreductase pytB and the cytochrome P450 monooxygenase pytD to form the fused gamma-pyrone core, resulting in pyranterreones 7 and 11, respectively . The hydroxy group at C-8 of pyranterreones 7 and 11 are dehydrated by the aspartyl protease pytH to form a delta-7 double bond to give pyranterreones 3 and 1, 2 accordingly . The exo-methylene of pyranterreone 3 could be reduced into a pendant methyl by reductase pytE to provide pyranterreone 4, also known as cordylactam (Probable). Pyranterreone 4 can be reconverted to pyranterreone 3 through pytB-catalyzed dehydrogenation or further oxidized to pyranterreones 9 and 10 (Probable).
Sequence Mass (Da): 72588
Sequence Length: 666
Domain: The N-terminal part acts as a polyketide synthase and includes a ketosynthase (KS) domain that catalyzes repeated decarboxylative condensation to elongate the polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) domain that selects and transfers the extender unit malonyl-CoA; a dehydratase (DH) domain that reduces hydroxyl groups to enoyl groups; an enoylreductase (ER) domain that reduces enoyl groups to alkyl group; a ketoreductase (KR) domain that catalyzes beta-ketoreduction steps; and an acyl-carrier protein (ACP) that serves as the tether of the growing and completed polyketide via its phosphopantetheinyl arm.
Pathway: Secondary metabolite biosynthesis.
EC: 2.3.1.-
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Q0CZH0 | MRFLGIAAVATFSTVVSAYPKSTALYNCVSSVFGPSAPQRIVTPNDTTYLDSRLGETIQFDELPVLLAYAQESKEIAPLIRCAKTAGIKAVPRAGGHSFEAYSALNGTLIIDIAHLNYVNVSDDRQTAVVGAGIRLGALYTALSEHGTSFIGGICPTVGLAGFLGSGGFNMQQRSQGLAVEHVLAAKVVLADGRTVVASPDTNPDLFFAIRGGGGGTYGIVVEFTLSLTSIPRSAMLMLSWNDTASRFPAAKQYLDWAPKQIPEFMSQINVYRDKVQVLGWYYGGTEDELRSLVNASGLLDIGKPAVVIAGGCNTDNARAFGYTTMECLPDGKVDVSILNVVPDPFSKVGNSTQFKWNEVPKSTSMPVADPWQRFHRMSKSFFVLKDNPLTDQTLQSLLDRIASLDAKSQVWGEWHAWNISTPSKGSGNAFAWREKAYAHLEFQIHGAPDDKERQSTYENWLEDLESYLRPTVGGASYSGYLDADISTDPLTSYYGGNVCKLVSVKRKTENDYSSSTVEQLFIDSDVNARKITSRYPIPPPDKSIKTEDITLQDCWVRIYTPPSATSSGSVAVFIHGGGWIMGSPDIEDATCRRICRCSGMTVVSVGYRLAPKFQFPTGLNDCVRATLWTLGHFPVSALVIMGGSAGANLAFGVALKLVDAGLGEKVKGVLALVPATVHPDAVPADKRDQYTAMHENANNTVNTLAAMDCFLDAYAAPPHDKYFSVLLHPRLKDLKKVYLVECGTDTLRDDARLMRDALEEAGVPLMYDAYPGYPHYFWSYPSPVLAEASESFHENMLQALAWLDQE | 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 modular PKS of pytA . The acyl chain is then connected to an L-serine through the amide bond by the modular NRPS of pytA . A tetramic acid is formed and released from the PKS-NRPS pytA to give pyranterreone 5 with the help of the thioesterase pytI . Pyranterreone 5 could be methylated by pytC to afford pyranterreone 6 (Probable). Both pyranterreones 5 and 6 are subsequently oxidized by the FAD-linked oxidoreductase pytB and the cytochrome P450 monooxygenase pytD to form the fused gamma-pyrone core, resulting in pyranterreones 7 and 11, respectively . The hydroxy group at C-8 of pyranterreones 7 and 11 are dehydrated by the aspartyl protease pytH to form a delta-7 double bond to give pyranterreones 3 and 1, 2 accordingly . The exo-methylene of pyranterreone 3 could be reduced into a pendant methyl by reductase pytE to provide pyranterreone 4, also known as cordylactam (Probable). Pyranterreone 4 can be reconverted to pyranterreone 3 through pytB-catalyzed dehydrogenation or further oxidized to pyranterreones 9 and 10 (Probable).
Sequence Mass (Da): 87872
Sequence Length: 807
Pathway: Secondary metabolite biosynthesis.
EC: 1.1.1.-
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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 mechanism that couples electron transfer to generation of the proton gradient that drives ATP synthesis.
PTM: Binds 2 heme c groups covalently per subunit.
Location Topology: Multi-pass membrane protein
Catalytic Activity: a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out)
Sequence Mass (Da): 29867
Sequence Length: 283
Subcellular Location: Cell membrane
EC: 7.1.1.8
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Q7SIC2 | DTSSLIVEDAPDHVRPYVIRHYSHARAVTVDTQLYRFYVTGPSSGYAFTLMGTNAPHSDALGVLPHIHQKHYENFYCNKGSFQLWAQSGNETQQTRVLSSGDYGSVPRNVTHTFQIQDPDTEMTGVIVPGGFEDLFYYLGTNATDTTHTPYIPSSSDSSSTTGPDSSTISTLQSFDVYAELSFTPRTDTVNGTAPANTVWHTGANALASTAGDPYFIANGWGPKYLNSQYGYQIVAPFVTATQAQDTNYTLSTISMSTTPSTVTVPTWSFPGACAFQVQEGRVVVQIGDYAATELGSGDVAFIPGGVEFKYYSEAYFSKVLFVSSGSDGLDQNLVNGGEEWSSVSFPADW | 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 monoxide. This involves the remarkable dioxygenolytic cleavage of two carbon-carbon bonds.
PTM: The N-linked glycan at Asn-191 consists of Man(5)-GlcNAc(2).
Catalytic Activity: O2 + quercetin = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO
Sequence Mass (Da): 37935
Sequence Length: 350
Pathway: Flavonoid metabolism; quercetin degradation.
EC: 1.13.11.24
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P42106 | MKTLCTHSLPKEKMPYLLRSGEGERYLFGRQVATVMANGRSTGDLFEIVLLSGGKGDAFPLHVHKDTHEGILVLDGKLELTLDGERYLLISGDYANIPAGTPHSYRMQSHRTRLVSYTMKGNVAHLYSVIGNPYDHAEHPPYASEEVSNERFAEAAAVADIVFLDEAKPACSAKLAELTELPDGAVPYVLESGEGDRLLTGDQLHRIVAAQKNTDGQFIVVSSEGPKGDRIVDHYHEYHTETFYCLEGQMTMWTDGQEIQLNPGDFLHVPANTVHSYRLDSHYTKMVGVLVPGLFEPFFRTLGDPYEGHIFPCEPQALRFDRILQNIEALDLKVMKP | 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 monoxide. This involves the remarkable dioxygenolytic cleavage of two carbon-carbon bonds.
Catalytic Activity: O2 + quercetin = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO
Sequence Mass (Da): 37600
Sequence Length: 337
Pathway: Flavonoid metabolism; quercetin degradation.
EC: 1.13.11.24
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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 Length: 264
EC: 1.13.11.47
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Q5A6P6 | MPGNREEFDIEKVLKSKKLEAIETSTEKKAPYTVFESTDKLLLIIVLSLVGFWSAISSPIYFPALPTLTKYFNTTPSVMNISVVAYLIFQGIAPTISSNLADTFGRRPVILGSIIVFCAVCIAISQTNVYWLLALLRCFQAAGIAPVFAISSGVAGDICTPANRGGMVGAVSGLQLAGNGIGGLVGAALISGFHTWRAIFIFLAIGGGVTFIFAFLVLAETSRRIVGNGSIRPKNVLNKAVLIYLPHFKNKITNDYSTLQPKGPFDILGPFKIFFQKEVFCTLLPSGMHFAAWTVSLTSLSTELESAKYNYSVMKVGLVYLPQGIACFIGSLIAGRCLNWYYRYRKNLYDKQMNDVPLNDRPPFNLVASRLTLTIVPLAMMVIGLSAFGWCLEYKKPIISIIISTILISFSASVMMSICTTMLVDLYPKQSGASASCVNLMRCWLAALFTGVLDKIISALGLGGTYTLLTGICLLTDLGLVYVLYTANQRFVNYVSPNQTAVNSDAEDY | 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 protein
Sequence Mass (Da): 55432
Sequence Length: 509
Subcellular Location: Cell membrane
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Q59YT1 | MLSTTQSVTEPTEVTSKKVEDIEKENDEETPYSIFTSYDRLVLIVILSLIGFWSTISSPIYFPALPTLTSYFHTSSSIMNISVVAYLIFQGIAPTISSNLADTFGRRPVILASIIVFCASCVAISQTNVYWLLAVLRCIQAAGIAAVISISSGVAGDVCTRANRGSMVGAVAGLQLVGNGIGGLVGAALISSFNSWRSIFIFLTIGGGVTFILAIFILPETSRKLVGNGSVVPKNILNKSPYIYLPHFKKRMNNDITTIVPATRFDLLGPLKIFFQKNVFCTLLPVGIHFAAWTMVLTSLSTELESRYHYSVMHVGLIYLPQGIACIAGSLVVGKSLDWYYRYRKTIYDQEVECLPLDERPQFNIVATRLTLSVVPALLMIIGLVIFGWCIQYKRHIISIIISTILVSFSASVFIAICTTMLVDLYPNNGSGSTSCLNLMRCWLAALGAGVLDSMINAMNVGGTYTVVAGFCILFDLALIYVLHNAKKKFSNSGPTTTKSPPKQ | 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 protein
Sequence Mass (Da): 54897
Sequence Length: 504
Subcellular Location: Cell membrane
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Q6FSQ7 | MMEDQQSLHSFISDYDQRSHAVEKYDGPDLSEVDSEDNDKMIKTNEDEAVKEPIYRTRSNQTEPDIANAPPYSRFDAKYKMALVLQCAYTGLFSTMAGAIYYPVLSVIEKQFHITEELVNITVVVYFIFQGIAPTLMGGLADSLGRRPVVLFAVTVYFGACIGLACAQTYAQIVVLRCLQAAGISPVIAINSGIIGDVTTRAERGGYVGYISGFQVLGSAFGALIGAGLSSRWGWRSIFWFLAIGSGVCLVFSIIMLPETKRTIVGNGSVTPRNYLNRAPLLMFPLIRRKLHLDDPEYETLEPRTQLSLLAPLSILKVKEISILLVTAGIQFATWSTHQTALSTVLSKNYHLSVAKIGLCYLPTGICTLISIVTSGRYLNWSYRRRFAKHKVWLKEQEEILVKENGYSREEVQNIINNDPKYVFNLVQTRLHAAFVTLLLSSSGFVAFGWCIDVKAPLASVLVMSGFASLFSNCILTFSTTLIVDIFPSKTSTATGCLNLFRCLLSALFIGCLSKMATSMTYGGVFTFLGALTALSACPLFYLLKNGREITLKRKRKEDASRAFALSVANEKAEAEGKAEESR | 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 Topology: Multi-pass membrane protein
Sequence Mass (Da): 64364
Sequence Length: 583
Subcellular Location: Cell membrane
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P40474 | MAGATSSIIRENDFEDELAESMQSYNRETADKLALTRTESVKPEPEITAPPHSRFSRSFKTVLIAQCAFTGFFSTIAGAIYYPVLSVIERKFDIDEELVNVTVVVYFVFQGLAPTFMGGFADSLGRRPVVLVAIVIYFGACIGLACAQTYAQIIVLRCLQAAGISPVIAINSGIMGDVTTRAERGGYVGYVAGFQVLGSAFGALIGAGLSSRWGWRAIFWFLAIGSGICFLASFLILPETKRNISGNGSVTPKSYLNRAPILVLPTVRKSLHLDNPDYETLELPTQLNLLAPFKILKAYEICILMLVAGLQFAMYTTHLTALSTALSKQYHLTVAKVGLCYLPSGICTLCSIVIAGRYLNWNYRRRLKYYQNWLGKKRSKLLEEHDNDLNLVQRIIENDPKYTFNIFKARLQPAFVTLLLSSSGFCAYGWCITVKAPLAAVLCMSGFASLFSNCILTFSTTLIVDLFPTKTSTATGCLNLFRCILSAVFIAALSKMVEKMKFGGVFTFLGALTSSSSILLFILLRKGKELAFKRKKQELGVN | 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: Cell membrane
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Q59XM0 | MSHSPNLSPQISNDIIDADTTSLASTETQQNIQHSQIHPIGHHGREQSEEPQNTTKTTTTTTNKIHTTTPSVDPDLGPLRELEQDLSSLESQQEQYLSQKPTSTSIKTNKVPLRERRGLLAQIVLIPEYEDARDYPNKIKYLIVFIIAFASLAGPFGTSVMLPAIDDIVNDLNTNVSTVNVSVGIYLLSLGIFPLWWSSFSERFGRRSVYMVSFTLFVAFSIGTALSPNIAALIVLRVLQGGSSASVQAVGAGTIADLFIPQERGQAMGLYYLGPLAGPFLAPILGGAVSQAWGWRATQWLLMIISACSFVLITFFLPETLRRVDTIQVAKDLMKKSDNNGSQNEKIHDDFAGADNSSVHDIDGNPIPGTELHQVVSNLSRRSSNARSIVTYMEEQENEGPIIDPVMPSISRLTTNRSAYSQRIHQNYVTDELRKTTSNLTQSNHSQYNNNNNNDNDKWSSVKTNCYDLIIRPLHSIILLKHPPVVLVISFSAISFAAIYFFNMAISYEYARSPYNFSSVILGLMYIPNSVTYFMASIIGGKWNDRLLNRYAQKHGELVPESRLSWNIVVAIILYPMACLIFGWTIKYREFWVIPLIGTALFGFASMLVIGATVTYLVDSLPGKGATGVALNNLIRQILAAIATFIVEPLLRAIGAGVLFSIIAGILLVSSLVLLYLKKRGAFFREHYDVMDLYAKL | 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 protein
Sequence Mass (Da): 77198
Sequence Length: 697
Subcellular Location: Cell membrane
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P38227 | MQAQGSQSNVGSLRSNCSDNSLPNNHVMMHCDESSGSPHSEHNDYSYEKTNLESTASNSREHRDNQLSRLKSEEYVVPKNQRRGLLPQLAIIPEFKDARDYPPMMKKMIVFLIAFSSMMGPMGTSIIFPAINSITTEFKTSVIMVNVSIGVYLLSLGVFPLWWSSLSELEGRRTTYITSFALLFAFNIGSALAPDINSFIALRMLCGAASASVQSVGAGTVADLYISEDRGKNLSYYYLGPLLAPLLSPIFGSLLVNRWPWRSTQWFMVILSGCNVILLTVLLPETLRKQDSKGAIAQILAERRIQVDNNERGEIQEDYQRGEDETDRIENQVATLSTEKHNYVGEVRDQDSLDLESHSSPNTYDGRAGETQLQRIYTEASRSLYEYQLDDSGIDATTAQVTRIRSTDPKLARSIRENSLRKLQTNLEEQVKKVLSSNGGEIAPKQVSAVRKVWDTFFVYFIKPLKSLHFLEYPPVALAITFSAISFSTVYFVNMTVEYKYSRPPYNFKPLYIGLLYIPNSVTYFFASIYGGRWVDMLLKRYKEKYGILAPEARISWNVVTSVISFPIALLIFGWCLDKKCHWVTPLIGTALFGYAAMMTIGATLSYLVDSLPGKGATGVALNNLIRQILAATAVFVTTPMLNGMGTGWAFTMLAFIVLGASSVLIILKKHGDYWRENYDLQKLYDKID | 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
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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 Location: Cell membrane
EC: 1.10.3.-
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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 | MNIKRILKVALYTTNASDVGQMYIVLGIVALIIGSVNAALIRDQLSFNNLNAVDYYDAVTLHGIFMIFFVVMPLSTGFANYLVPRMIGAHDLYWPKINALSFWMLVPAVILAAISPLLGAVDLGWYMYAPLSVETTVNYGLGTNLIQIALILSGLSSTLTGVNFVMTITKMKKVPYLKMPLFVWGFFTTAILMIIAMPSLTAGLVFAYLERLWGTPFFDSALGGSPVLWQQLFWFFGHPEVYILILPAMGLVSELLPKMARREIFGYTAIALSSIAIAFLSALGVWMHHMFTAIDNTLVQIVSSATTMAIAIPSGVKVLNWTATLYGGEIRYKTPTILLISFIVMFLLGGITGVFFPLVPIDYALNGTYFVVGHFHYMVYAILYALLGALFYYFPFWSGKWYNDDLGKTGAILLVAGTFLTATGMSIAGILGMPRRYAVIPSPIYDPFQFMASVGAVLTGIGLFILAGVLVHGVFRGRAVNGVDPWDNISVKLQDFFIKPVKLPLSFGKSLDGAFDEEYHGIKFPYYSVLGLFLSFIPLGFMFILIGLIPIGIVLLLAFMGVGLYWGYDQWFKPMQPPPHFYADGGVPVTNSVNNSISPSLGIASMRDARSAVLWFILAEVILFGSFIGGYAFIMSPVTNPLSYVNNIVPAVEVFPLPAIMTAILLSSSIPAHIAYEYFKKGNVKMFRNLGLLTMAMGLTFLGGQIYEFTHYIHFIPQDSAASSFFFATVSLHGFHVIMGLVIWAFMMLRIRKGFIPYAGSVAATYYWHFVDAVWVVVFSTFYLHLIV | 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 subunits I and III.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 87082
Sequence Length: 788
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Cell membrane
EC: 1.10.3.-
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P57232 | MQLSDFSFDLPKSLISFHPYFIRSTCRLMVMYGHTGMIFHKRFFNIIDEINSGDLIILNNTQVIPARFFGKKESGGKVEVLVEKILGINNILASIKNSKNINIGSKIFFGYKDKIKGSVVDCKNSFFEIFFHDNIDSAIDIINNIGEIPLPPYIKRFRNKLDVDLYQTVYKKKTGSIAAPTAGLHFDLPLLEALHNKGVDIDYITLHIGSGTFQPIRRVQIEEHIMHSESVEVSSSVIQKIKSCKKKGGRIIAVGTSTLRALESAYHSSEWSDSQDFISDTNIFIYPGYKHNIVDALITNFHFPESTLIMLVCSFLGYKNTMNAYNTAIVNKYSFFSYGDAMYITHNKLAPYENFII | 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 Mass (Da): 40506
Sequence Length: 357
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.4.99.17
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P44595 | MRVSDFNFDLPDELIARYPKTDRVSCRLLQLNGENGEIFHRTFSDVLDLIDEGDLLIFNNTRVIPARMFGRKASGGKIEVLVERMLDEHRFLAHIRSSKSPKEGAELFLGEDKLGENNGIKAVMKARHGALFEVELSDKSTALLDVLQTIGHMPLPPYIDRPDEEADQECYQTVYSKVPGAVAAPTAGLHFDENLLEKLKAKGVNFEFVTLHVGAGTFQPVRVENIEDHVMHAEYVEVSQEVCNAIIATKKAGKRVIAVGTTSVRSIESAALSAEEFGNPDLIEPYFSDTSIFIYPGKKFRVVDCLITNFHLPESTLIMLVSAFAGYKNTMNAYKHAVKEKYRFFSYGDAMFINKNSNVRGLE | 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 Mass (Da): 40629
Sequence Length: 363
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.4.99.17
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Q2SDV0 | MRVDDFDFELPPELIARRPLAERSSSRLLCLDAETGEINHRGFKDLLGMVNPGDLLVFNDTRVIPARLFGQKRSGGKVEVMVERVVSMTEMLAHVRASKAPKPGVEILIEENYVLTMVEREGDLFRLRVSQGGSVSELLERCGHMPLPPYIDREDDLSDRERYQTVYSRQPGAVAAPTAGLHFDEALLLAMSQKGVETAFVTLHVGAGTFQPVRVDVVQDHQMHSEYLEVSADVCERVRQVKAAGGRVVAVGTTAVRALETASRSGSIEPYAGDTSIFIYPGYEFVTVDALVTNFHLPKSTLLMLVSAFAGREHILAAYQEAIEQRYRFFSYGDAMFLHRRQSGLEDAGAN | 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 Mass (Da): 38947
Sequence Length: 351
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.4.99.17
|
B8CXG1 | MKVEEFDYELPEELIAQKPLPNRDDSRLMVLHRKTGEIEETVFKNIIKFLEPGDLLVLNDTKVIPARLFGEKIPSGTRIEVLLLKSITEGLWEVLVRPGRRMKKGNRVSFGDGKLVGIVKDYTDFGGRIMQFEYDGDFDKVIEELGEMPLPPYITRKVEDKGRYQTVYARKKGSVAAPTAGLHFTDRLLKKIKEQGIGIIYLTLHVGLGTFRPVRAENVEDHKMHSEYFEVSTDVVNRIKETKEKGKKVIAVGTTVTRALESAAVEKRHLKAMRGWTDIFIYPGYNFKVIDGLITNFHLPKSTLLMLVSAFAGKDMVMSAYKLAIKNKYRFFSFGDAMLIL | 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 Mass (Da): 38822
Sequence Length: 341
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.4.99.17
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B0TF76 | MEVALYDYELPKEAIAQTPVEPRDASRLMVLERRTGAVDHRIFRDLVHILHPGDLLVVNRTRVIPARLFGKKRDSDVTVEIVLLTPMGDDRWEVLVRPGRRLKPGVFVDLGEGRLAAEIVETTDFGGRVVRFHYSGDFDTLIDEIGQMPLPPYIETALPRQEAERYQTVYSQERGSAAAPTAGLHFTPQLLEDLKKRGIEITSVLLHVGLGTFRPVQVDRIEEHKMHSEFFQVDPEAARAIAKAKQEGRRVIAVGTTVARTLETAAGLHNGTVAAGSGWTDIFIYPGYTFQCIDGLITNFHLPRSTLLMLVSAFAGREQVLAAYREALEKGYRFFSFGDAMLII | 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 Mass (Da): 38481
Sequence Length: 344
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.4.99.17
|
O25702 | MKEFDLESYDYYLPKELIASYPVLPKEKAKLLVYERRSQKITHTTFEHVLDFFPKNALIVLNDTKVIKARLFGSKHAFLPSKTTEVFFHRFFKNNTALTQIKGKIKVGDKIFFDANYHAEVLELLHNGQRLIAFYDNKTPLNQENILKLLEQYGHMPLPPYIKRADESLDAHEYQSVFAKHMGAVAAPTASLHFSQNTLEKLLKDFKHAFLTLHVGAGTFLSVETKDIREHQIHTEVLRIPKKSQEILQKSQEILCVGTTALRSVEYFKRLENPNQEAFECDIFLHFANPILHVNYLLTNFHLPKSSLLMLVSTMIGLEKTKEIYKTAIEKKYRFYSYGDGMLIL | 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 Mass (Da): 40029
Sequence Length: 345
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.4.99.17
|
Q01SU0 | MNLSEFDYHLPDELIAQEALADRAASRMLVVHREQGRWEDRCFRDLPEFLRPGDCLVLNDSRVFPARLFGHRSGVHSLAVGKNNPKRHEFLSGAVEVFLLRAVSQDGRDWQALVRPGRKMRTGERIVFDEGLEAEIIARGEFGERTVRFLGSGDLYAAFDRIGHVPLPPYIKRDDSPADRERYQTVFAREKGSVAAPTAGLHFTPEVIERCQAAGADVATVTLHVGLGTFQPLHQEVVEEVKLHTEHYRITADNAGKIGAATRVVAVGTTSVRTLETAARDGVLEGETDIFLYPGVPFRRTGAMLTNFHLPRTSLLVLVSAFAGKDLMLAAYRHAVEARYRFYSYGDCMLIV | 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 Mass (Da): 39289
Sequence Length: 352
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.4.99.17
|
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: 251
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
|
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: 225
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
|
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: 222
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
|
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: 224
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
|
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: 221
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
|
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: 224
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
|
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: 243
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
|
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(+) + triphosphate
Sequence Mass (Da): 18719
Sequence Length: 162
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.1.2.50
|
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(+) + triphosphate
Sequence Mass (Da): 13150
Sequence Length: 115
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.1.2.50
|
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(+) + triphosphate
Sequence Mass (Da): 16468
Sequence Length: 146
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.1.2.50
|
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(+) + triphosphate
Sequence Mass (Da): 14273
Sequence Length: 120
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.1.2.50
|
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(+) + triphosphate
Sequence Mass (Da): 13773
Sequence Length: 121
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.1.2.50
|
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(+) + triphosphate
Sequence Mass (Da): 16322
Sequence Length: 141
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.1.2.50
|
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(+) + triphosphate
Sequence Mass (Da): 16234
Sequence Length: 150
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.1.2.50
|
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(+) + triphosphate
Sequence Mass (Da): 23663
Sequence Length: 200
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.1.2.50
|
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(+) + triphosphate
Sequence Mass (Da): 18816
Sequence Length: 163
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.1.2.50
|
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(+) + triphosphate
Sequence Mass (Da): 18062
Sequence Length: 161
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.1.2.50
|
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(+) + triphosphate
Sequence Mass (Da): 18742
Sequence Length: 157
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.1.2.50
|
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 biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.7.1.13
|
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 biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.7.1.13
|
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 biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.7.1.13
|
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 biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.7.1.13
|
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 biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.7.1.13
|
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 biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.7.1.13
|
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 biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.7.1.13
|
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 biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.7.1.13
|
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 biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.7.1.13
|
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 biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.7.1.13
|
D4GV73 | MDDRVHPEVRRTATEIDTMEIRGAATIADAAARALRTQATESDAADAEAFRAELRATARTLHETRPTAVSLPNALRYVLRDMSSTTVEGLRQSVVDSADEFCARLERAQADLGQVGANRLRDGDTIMTHCHSTDALACVEAAVEQGKHIEAVVKETRPRNQGHITAKRLHELGVPVTLIVDSAARRYLNDVDHVLVGADAVAADGSVINKIGTSGLAVNARERGTPIMVAAQTLKLHPGTMTGHTVDIEMRDTAEVVDDDTLADLGNPTVKNPAFDVTPPRYVDAIVTERGQFPPESIVILMRELFGEGTSEPWAEPSPRAEP | 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-bisphosphate
Sequence Mass (Da): 34876
Sequence Length: 323
EC: 5.3.1.29
|
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-bisphosphate
Sequence Mass (Da): 34518
Sequence Length: 308
EC: 5.3.1.29
|
Q5JFM9 | MAVVKEVLEIAEKIKNMEIRGAGKIARSAAYALQLQAEKSKATNVDEFWKEMKQAAKILFETRPTAVSLPNALRYVMHRGKIAYSSGADLEQLRFVIINAAKEFIHNSEKALERIGEFGAKRIEDGDVIMTHCHSKAAISVMKTAWEQGKDIKVIVTETRPKWQGKITAKELASYGIPVIYVVDSAARHYMKMTDKVVMGADSITVNGAVINKIGTALIALTAKEHRVWTMIAAETYKFHPETMLGQLVEIEMRDPTEVIPEDELKTWPKNIEVWNPAFDVTPPEYVDVIITERGIIPPYAAIDILREEFGWALKYTEPWED | 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 phosphorylated sugars such as R5P, ribose, G16P, G6P, G1P, FBP, F6P, and PRPP, are not substrates. 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-bisphosphate
Sequence Mass (Da): 36302
Sequence Length: 322
EC: 5.3.1.29
|
Q6L440 | MKTVIARTSSKLARTPRMNEEIVGFEDVIENLRKKLLSETKGQDVISIHGMPGLGKTTLANRLYSDRSVVSQFDICAQCCVSQVYSYKDLLLSLLRDAIGDESGSRELPDNELADMLRKTLLPRRYLILVDDVWDNSAWDDLRGCFPDVNNRSRIILTTRHHEVAKYASVHSDPLHLRMFYEDESWKLLEKKVFGEQSCSPLLKDVGLRIAKLCGKLPLSIVFVAGTLSEMEKEVECWEQMANNLGGPKLSSFLEDRVIDISRLIRLWISESFIKSSEGRSLEDIAEGYLENLIGRNLVMVTQRADSDGMVKACRLHDVLLDFCKKRAAEENFLLCIKRDQSTKAVISHKQQAHLAFSKMDNLVEWSASSSLVGSVIFKSYDPYFARCPLSSHAFALSHILINFKFLKVLDLEHQVVIDFNPTEHFYLRYLSAHIDQNSIPSSISNLWNLETLILKRTPAGRLNTLLLPSTIWDMVKLRHLHIPNFRAESEDALLENSAKLYDLETLSTTYFSSVEKAELMLRKTPNLRKLICEVQFLEYPNQYHVLNFPVRLEMLKLYRFNNSKVIPFYISAPNLKYLKLSGFYLDSHYLSETADHLKHLEVLKLYRVEFGDHGEWKVSNGMFPQLKILKLNYVCLMKWIVADDAFPNLEQLVLRGCKDLMEIPFCFMDILSLKYIELDNCNKSVVKSAKDIEEAQVEDNQNTNFKLVIIKKMILQFDISHDKEIDNAFKRLASLPGVDSISIDMIEKKLTVGGDMNANEVRLVVGKLIDSGML | 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 hypersensitive response, which restricts the pathogen growth.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 88790
Sequence Length: 775
Subcellular Location: Cytoplasm
|
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 translocated receptors in general (By similarity). As a result, may regulate cell adhesion and migration (By similarity). Involved in neurite growth (By similarity). Following SBF2/MTMT13-mediated activation in response to starvation-induced autophagy, binds to and regulates SNARE protein VAMP8 endolysosomal transport required for SNARE-mediated autophagosome-lysosome fusion . Modulates protein levels of the cargo receptors TMED2 and TMED10, and required for appropriate Golgi localization of TMED10 .
Location Topology: Lipid-anchor
Sequence Mass (Da): 24348
Sequence Length: 225
Subcellular Location: Endoplasmic reticulum membrane
|
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 trafficking of integrins which is required for the successful completion of cytokinesis . Involved in neurite growth (By similarity). Following SBF2/MTMT13-mediated activation in response to starvation-induced autophagy, binds to and regulates SNARE protein VAMP8 endolysosomal transport required for SNARE-mediated autophagosome-lysosome fusion (By similarity). Modulates protein levels of the cargo receptors TMED2 and TMED10, and required for appropriate Golgi localization of TMED10 (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 24106
Sequence Length: 222
Subcellular Location: Endoplasmic reticulum membrane
|
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