ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
A0A4P8WAD3 | MASQDGTTELLSQSVNSTCIPGSTYHVDRGRASSASTPPTSPPLSEVDYTPLLESTQEPRHEYTQLAHSLVKAMADYVGHLQEENLPMPSLEPAAQVHGGLKVQGGVAARDTVVKLAQKIVAMTMDPEMKLFISSLQFHFCSSLKVAIDLRVHELDECFRASSRQADALALARYREPHEADTLGFGLAFNTTANFWEVLARDTEGKRSQRFNRAMRAVNINALEVIPRIYPFNRIGGNGLLVDVGGGLGQVARAIMATNQGSRLQRCIVQDVCAADDVLEEVLESNRKLGVELQRHDFFDKQPVTGASIYFFRHIFHDWPDRACVKILKQIVQAMGRDSRLLICDQVVDDEPSIPATLYDIDMWTLFGGKERNRSEWEALFRAADERLYIKKVWTTTEAPTTILEVCLW | Function: O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass . The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine . The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone . The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor . As the NRPS A-domain demonstrates substrate tolerance, pyiS can also use phenylalanine, tyrosine and even para-chlorophenylalanine as amino acid precursor, which leads to the production of novel cytochalasans, including halogenated cytochalasans . Because pyiS lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase pyiC . Reduction by the hydrolyase pyiE leads to 1,5-dihydropyrrolone, which is substrate for dehydration and intra-molecular Diels-Alder cyclization by the Diels-Alderase pyiF to yield the required isoindolone-fused macrocycle . The tailoring cytochrome P450 monooxygenases piyD and piyG catalyze the hydroxylation at C-18 and C-7, respectivily, whereas the short-chain dehydrogenase/reductase pyiH reduces the carbonyl at C-21 in preparation for the transfer of an acetyl group by the acetyltransferase pyiB . These 3 reactions whose order is not clear yet, lead to the production of O-methylpyrichalasin J, a deacetylated pyrichalasin H . Finally, pyiB to converts O-methylpyrichalasin J into the final product pyrichalasin H via acetylation of C-21 .
Sequence Mass (Da): 45694
Sequence Length: 409
Pathway: Mycotoxin biosynthesis.
EC: 2.1.1.-
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A0A4P8WAJ7 | MGFLSAGGLWASLFRARISPIVETDEVLPLTLIDNIAAARNAILSEVIRFDQVLDVVKLRDGLTELIDKRGWRKLGGRLRLRPNGSLEIHVPREFTEERPAFRFTSQAFDIAIEEHALGSQLPKLSDGPSLQPGSTSVDKFNLIPDKPEKLDDYVYSDRPILALHVTSFTNSCIVTLTWSHVVFGARGIKELIAAWSKVLHGEQNVPLLLGTHQDVLAGIGTDGDKTAPFLLDPIKIKGLGLVRIIFGLLWEIWQHPTVETRALHLPKRFVSQLRQKCMEELGAFCREDPAPFISEGDVLEAWCSRFVAQARADEKPALVTNALDIKDRLTAPWSSRGEYLQNTGCCTWTPVQPETLLRSPLGELAYVIRRSIQELATDDQLRAQLRIFRSLGHTKMLPLFGNPNSRVISFSNWTKFNLFEVTNLGPAVISTSPSTRSDASTSPIGRPVYMHCEAAGDSRMLRNCFNVTGKDWDGSYWITAHLYPEDWTKLEEYMRQTQQHISD | Function: Acetyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass . The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine . The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone . The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor . As the NRPS A-domain demonstrates substrate tolerance, pyiS can also use phenylalanine, tyrosine and even para-chlorophenylalanine as amino acid precursor, which leads to the production of novel cytochalasans, including halogenated cytochalasans . Because pyiS lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase pyiC . Reduction by the hydrolyase pyiE leads to 1,5-dihydropyrrolone, which is substrate for dehydration and intra-molecular Diels-Alder cyclization by the Diels-Alderase pyiF to yield the required isoindolone-fused macrocycle . The tailoring cytochrome P450 monooxygenases piyD and piyG catalyze the hydroxylation at C-18 and C-7, respectivily, whereas the short-chain dehydrogenase/reductase pyiH reduces the carbonyl at C-21 in preparation for the transfer of an acetyl group by the acetyltransferase pyiB . These 3 reactions whose order is not clear yet, lead to the production of O-methylpyrichalasin J, a deacetylated pyrichalasin H . Finally, pyiB to converts O-methylpyrichalasin J into the final product pyrichalasin H via acetylation of C-21 .
Sequence Mass (Da): 56597
Sequence Length: 504
Pathway: Mycotoxin biosynthesis.
EC: 2.3.1.-
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A0A4P8W733 | MQTSNYGSLPTSRSAVVLGNDERLRIERHLPLPALRPNEVLVQVKAVAINPCDYKMHQRFPCPGAVDGCDFAGVIVGVGPEVLKFGLGDRVCGAVHGSNPLRPESGSFTDYMTSESEFTLKIPAGLSFEQAVGMGVTGIGTLGMALFRTLQLPGSLDRPATKPRTVLVHGGSSSVGTMAIQLLRLLGHVPIATCSPKNFALARRFGAEEVFDYNSPDCAAAIKAYTKNTLSYILDPFTDAKSVDLCYKAMGRAGGRYCCLEMYPEYVLQRKSIKVGFVMGPLLLGHRLALSQGYERDEDPEMRAFGVEWYKDVQKMLDRGLLKRHPIKLLGDSFEALIEGVEMLQRKEVSGEKLVVALDSEQSKPVLTK | Function: Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass . The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine . The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone . The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor . As the NRPS A-domain demonstrates substrate tolerance, pyiS can also use phenylalanine, tyrosine and even para-chlorophenylalanine as amino acid precursor, which leads to the production of novel cytochalasans, including halogenated cytochalasans . Because pyiS lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase pyiC . Reduction by the hydrolyase pyiE, followed by dehydration and intra-molecular Diels-Alder cyclization by the Diels-Alderase pyiF then yield the required isoindolone-fused macrocycle . The tailoring cytochrome P450 monooxygenases piyD and piyG catalyze the hydroxylation at C-18 and C-7, respectivily, whereas the short-chain dehydrogenase/reductase pyiH reduces the carbonyl at C-21 in preparation for the transfer of an acetyl group by the acetyltransferase pyiB . These 3 reactions whose order is not clear yet, lead to the production of O-methylpyrichalasin J, a deacetylated pyrichalasin H . Finally, pyiB to converts O-methylpyrichalasin J into the final product pyrichalasin H via acetylation of C-21 .
Sequence Mass (Da): 40287
Sequence Length: 369
Pathway: Mycotoxin biosynthesis.
EC: 1.-.-.-
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A0A4P8W744 | MFLSIKRKIIEPYLVIRQSLAPLKLSRWQLTKIMARTAFDGLPSGTLIVLAALSLALLVAVLRIKSQERTRSKEIPGLPVVKRNHLHYLDIVREGRELYPGQPFMAVNKRHSLVVFPPSCFNEIKRLPAHTASAKKFFNTTNYGDWSHVGEESPELIKSVIADLTRSLPARVHTRQDECRDVFDEVVGRRREWKEFPLLMTTFEIITQINACSFVGKTLATNRSWVRSVMMLPVFIHVGVMLLDACPLIVRPFMAYLTFLPSIKNRWDLTRMLAPVLKKDLEEYHEAKDKKEFLRPRAEGKVPFTGFLLSHYKSAQASLKQLISDYIHLSFDSTPNTAAVMFHALCELAIHPEAVEALRQELDEVMVDGKLPPTHLQELRKMDSFLRECFRLHPFGIFTLQRRVEQPVQLSVGPLLPPGTLMAVDGQAIDGSSELWPNPEKFDVYRFYNLRQKLGNENQYHFATTSPDSPGWGDGTQACPGRFFAVNTLKIAMAHFLRNYDIEIKPECLPLKTKPMPSGFFSPDDRAIARIRART | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass . The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine . The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone . The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor . As the NRPS A-domain demonstrates substrate tolerance, pyiS can also use phenylalanine, tyrosine and even para-chlorophenylalanine as amino acid precursor, which leads to the production of novel cytochalasans, including halogenated cytochalasans . Because pyiS lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase pyiC . Reduction by the hydrolyase pyiE leads to 1,5-dihydropyrrolone, which is substrate for dehydration and intra-molecular Diels-Alder cyclization by the Diels-Alderase pyiF to yield the required isoindolone-fused macrocycle . The tailoring cytochrome P450 monooxygenases piyD and piyG catalyze the hydroxylation at C-18 and C-7, respectivily, whereas the short-chain dehydrogenase/reductase pyiH reduces the carbonyl at C-21 in preparation for the transfer of an acetyl group by the acetyltransferase pyiB . These 3 reactions whose order is not clear yet, lead to the production of O-methylpyrichalasin J, a deacetylated pyrichalasin H . Finally, pyiB to converts O-methylpyrichalasin J into the final product pyrichalasin H via acetylation of C-21 .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 61076
Sequence Length: 535
Pathway: Mycotoxin biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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P18542 | MPFGPASRLGVSLFDETPPVEWVPGRSQEEAETIIRAIYRQVLGNAYVMESERLAVPESQFKRGELSVREFVRAVAKSELYRSRFFTSCARYRAIELNFRHLLGRPPLDLEEMRSHSTILDTQGFEAEIDSYIDGDEYQSTFGENIVPYIRGYKTEALQSMVQFTHTFQLVRGASSSSLKGDLSGKAPKLNALVIQSTPTAVISPASAGATFSTPPTGARTRLGVDASAGGKVYRIEVTGYRAKTFNNISKFRRSNQVFLVPYEKLSQEYQRIHQQGGVIASITPV | Function: Rod linker protein, associated with phycoerythrocyanin. 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): 31844
Sequence Length: 286
Subcellular Location: Cellular thylakoid membrane
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P11399 | MSTSVAERLAIKDEVDKKIELRPNWSEDELQIVFKTAYEQVFGRQGLYASQRFATAEALLRNGKISVKQFIELLAKSEFYKECFFYNNSQVRFIELNYKHLLGRAPYDQSEIAFHVDLYAAAGYDAEIESYIYSPEYDNAFGNFVVPYYRGFQSIPGMKTVGFNRIFELYRGRANSDNAQFGGKSARLRSKISMNLANTIVPPTSPIAASTSSARTLVTSPVMGDARMFIVEAIAGTLNTNVAVRRSRQVYTVPYDRLSATYQEIHKRGGKIVKITPAS | Function: Rod linker protein, associated with phycoerythrocyanin. 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): 31492
Sequence Length: 279
Subcellular Location: Cellular thylakoid membrane
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P18543 | MASQTILELWPSSSLEEVQTIIRAVYKQVLGNPHVMESERLVTAESQLCDRSITVREFVRSVAKSDFYRNRYFQSCAPYRFVELNFLHLLGRAPQDQREVSEHIVRTVAEGYDAEIDSYIDSSEYEAAFGENVVPYYRGRSSEANSKQVGFNRIFALDRGPAQIDSAVKSAQLVYAVATNSANAIKASSSTVIGSGTEKRFKILVQGSKFDSPRRISTTEYIVPASKMTPQIQRINRTSGKIVSITEIV | Function: Rod linker protein, associated with phycoerythrin. 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): 27891
Sequence Length: 249
Subcellular Location: Cellular thylakoid membrane
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P31329 | MSSSVAERLAIRDAIGNKVELRQNWSEDDLQKVFRAAYEQIFGRQGIYASQKFTSAEALLRNGKISVRQFVEILAKSEFYKECFFYKNSQVRLIELNYKHLLGRAPYDQSEIADHVDIYAARGYDADIDAYIYSSEYENAFGNSIVPYYRGFQSIPGMKTVGFNRICELYRGRGNSDNAQMGRTNSRLRTKVSLNLPNGILPPTSAGTNFVSAAPTLISSATKGDNRMFVIEAIAGGLNTNVAVRRSRQVYTVSYERLSATYQEIHKRGGKIVKISQV | Function: Rod linker protein, associated with phycoerythrocyanin. 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): 31295
Sequence Length: 278
Subcellular Location: Cellular thylakoid membrane
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P73204 | MTSLVSAQRLGIVAVDEAIPLELRSRSTEEEVDAVILAVYRQVLGNDHLMSQERLTSAESLLRGREISVRDFVRAVALSEVYRQKFFHSNPQNRFIELNYKHLLGRAPYDQSEIAFHTDLYHQGGYEAEINSYIDSVEYTENFGDWVVPYFRGFATQRNQKTVGFSRSFQVYRGYATSDRSQGNGSRSRLTRELARNTASPVYAGSTAESLRGTSAGSRNQMYRLQVIQGAAPGRGTRVRRGKAEYLVSYDNLSAKLQQINRQGDTVTMISLA | 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): 30797
Sequence Length: 273
Domain: The N-terminal PBS-linker domain (residues 19-157 in this experiment) interacts with the C-phycocyanin beta subunit (cpcB).
Subcellular Location: Cellular thylakoid membrane
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Q6LWQ0 | MRHLISMRDIGREEILNILDESERMEAILNEKGHCDFLNGRILATLFYEPSTRTRLSFETAMKRLGGNVIGFTDISNTSVTKGESLADTIKVISGYSDLIAIRHPSEGAARLSSENSKVPVINAGDGSNQHPTQTLLDLYTIKREVGHIENLKIAFIGDLKYGRTVHSLCQALSLFKGVEIKLISPDELKMPREVIEDIAGKIKLSEMADVDIDDVDVVYMTRIQKERFVDVNEYYKVKGIYRLSKEHIGEKNVVIMHPLPRVDEIDSEVDNIPQARYFKQSFYGVPVRMAILKLLFEDSVK | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 34171
Sequence Length: 302
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
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A6UQU0 | MRHLISMRDIGRDDILRILEESEKMEAVLNEKGHSDILNGKILATLFYEPSTRTRLSFETAMKRLGGNVIGFTDISNTSVTKGESLTDTIKVISGYSDLIVIRHPSEGAARLSSEVSGVPVINAGDGSNQHPTQTLLDLYTIKREVGKIDGLKIAFIGDLKYGRTVHSLCQALSLFKNVELRLISPDELKIPREVLEYIDGKVLLSETSEINIEDVDVVYMTRIQKERFIDLNEYQKVKGTYRLLKEHVLEKNLIIMHPLPRVDEIDSKVDSLNQAKYFKQSFYGVPVRMAILSLLSKDLQK | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 34119
Sequence Length: 302
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
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O66990 | MLKLIVKNGYVIDPSQNLEGEFDILVENGKIKKIDKNILVPEAEIIDAKGLIVCPGFIDIHVHLRDPGQTYKEDIESGSRCAVAGGFTTIVCMPNTNPPIDNTTVVNYILQKSKSVGLCRVLPTGTITKGRKGKEIADFYSLKEAGCVAFTDDGSPVMDSSVMRKALELASQLGVPIMDHCEDDKLAYGVINEGEVSALLGLSSRAPEAEEIQIARDGILAQRTGGHVHIQHVSTKLSLEIIEFFKEKGVKITCEVNPNHLLFTEREVLNSGANARVNPPLRKKEDRLALIEGVKRGIIDCFATDHAPHQTFEKELVEFAMPGIIGLQTALPSALELYRKGIISLKKLIEMFTINPARIIGVDLGTLKLGSPADITIFDPNKEWILNEETNLSKSRNTPLWGKVLKGKVIYTIKDGKMVYKD | Cofactor: Binds 1 Zn(2+) ion per subunit . Fully functional with a mononuclear metal center. Does not require a second metal for activity, although the conservation of the second metal-binding site during evolution leaves open the possibility that a second ion might bind in vivo .
Function: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Catalytic Activity: (S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate
Sequence Mass (Da): 46380
Sequence Length: 422
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
EC: 3.5.2.3
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O04904 | MIKTLVSPYSGFGSQKLKFDRSSEKVKTRAVRMELTITQPDDWHLHLRDGDLLHAVVPHSASNFKRAIVMPNLKPPVTSTAAAIIYRKFIMKALPSESSFDPLMTLYLTDKTLPEEIRLARESGVVYAVKLYPAGATTNSQDGVTDLFGKCLPVLEEMVKQNMPLLVHGEVTDPSIDVFDREKIFIETVLQPLIQRLPQLKVVMEHITTMDAVNFVESCKEGSVGATVTPQHLLLNRNALFQGGLQPHNYCLPVLKREIHREAIVKAVTSGSKKFFLGTDSAPHERSRKESSCGCAGIYSAPIALSLYAKVFDEAGALDKLEAFTSFNGPDFYGLPRNSSKITLKKSPWKVPDVFNFPFGEIVPMFAGETLQWQPLK | Cofactor: Binds 2 Zn(2+) ions per subunit.
Catalytic Activity: (S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate
Sequence Mass (Da): 41950
Sequence Length: 377
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
Subcellular Location: Mitochondrion
EC: 3.5.2.3
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O28034 | MIRGKVFYKGEFVEAGIEVENGRIKRIGKLVEGKEVKGVILPAGIDVHVHLRDFAEKRKETIETGTLSALHGGICLVVDQPNTKPPVDDAETYFRRMGKAEKSVYVDYALNLALTNSNHGKIGSIMRKISERYFVPAVGEVFIQHDSEDLQIDYETLSSVYKRFEGVVFTIHAEDPAYVARGSPNFVFRRREAEVLAVERLVELGKFHFCHISTKDSAKEILNSNSTYEVTPHHMLLSVEDYGRLGNLVNVNPPLREREDVEWLFRNFHRIDVLASDHAPHTLEDKEAGASGFPGVETMYPLFVNLASKGYISFKTLVEKIASNPARIFGFKGYGEIEVGNYANFAVFDLKKVDEIRAERLHSKCGWTPFEGFEAVFPDKVYLRGKELLENEMKAGNVLKKRV | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Catalytic Activity: (S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate
Sequence Mass (Da): 45559
Sequence Length: 403
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
EC: 3.5.2.3
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Q92SC7 | MQDLVIRRPDDWHLHLRDGGMLRGVIADTSRHFARAIIMPNLVPPVVTSADAAAYRERILAAIPAGDRFEPLMTLYLTEGTDPGDVEAGFRSGLVKAVKLYPAGATTNSSSGVRDIDKAMPVLERMAEIGLPLCVHGEVTTAEVDIFDREAVFIETVLDPLRRRLPDLRITMEHVTTKDGVDYIREHAANLAGSITTHHLIINRNAILVGGIKPHYYCLPVAKREAHRLALRQAAISGDVRFFLGTDSAPHVDPLKECACGCAGIYTSINTLSCLAHVFEEEGALDRLEAFTSLNGPAWYGLPANEETITLRKQEEPVSYPARIETEAGPVTVFDPMFPLHWAVTQA | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Catalytic Activity: (S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate
Sequence Mass (Da): 38106
Sequence Length: 347
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
EC: 3.5.2.3
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Q7UNR2 | MVVGQRERKRRCIRGEPLMNDTTWVLDGGRLIDPANGIDRIARLVLHEGKVHSIDTPDGDVPPDAGRLDVTGKIVAPGLVDLATELREPGSEEDETIQTGSNAALAGGYTTVLCCSSTKPLMDSAASVQLVRQIAQRVDGVRVLPIACLSKGRQAEQMAELGILAAAGAAGFSDTPRPMPNDALLKRALDYCRMFDLPIFDRPEVPELADGGVMHDGQIGLILGLKGLPTEAEDLAVARDVRLAEATKGRLHVGPVSTMGSIDMIGRVKSRGIHISASVCPHNLFGSDELLRSYDSRYKVHPPMRSPSHVEALRNAVAEGVIDAIESGHMPRAQEKKANDLDLAPFGASALETTLAAIATDLVETKILPWSRAIECLSTAPARIAGVKGGTLSVGANADVTVIDPLNAWSVEAKEFRSRCHSSPMTGRTLTARVTHTLVGGRLKFELHPTVASAAS | Function: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Catalytic Activity: (S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate
Sequence Mass (Da): 48514
Sequence Length: 456
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
EC: 3.5.2.3
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Q1AVY7 | MSTRSGSAAELAIRGAHVVDPSSGLDGVTDVVVRGGRVAAVGRGRPAARELDASGLFLFPGFVDLHAHWRTPGREDEEDLESGSSAAAAGGFTGVVMMPNTDPVLDRPALVSGLVRRAERESRVRAFVAAALHAGLAGERLTEMRLLKEAGALCVSDDGLGTQSAGVLRNGMLYARSAGLPVILHCEDRTLATGAVHEGAAAALAGVPGTPASAEDVATAAALVLAAETGARVHITHVSTALSAALVGFFRGRAAVTADTTPHHTTLTDELVFALDGLFRVNPPLRPGSDREGVVGALRDGILDFVATDHAPHAPEEKELPLEEAAPGFLGHETAFAALYTGLVLEGRLSLGRLVEAMSCGPGRWVGGLGSLSPGSPADLALVDLGEEWTVSRRTLASRSSNSPYLGRRLRGRVVGTMVGGEMVYDRMGARLGVRT | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Catalytic Activity: (S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate
Sequence Mass (Da): 45111
Sequence Length: 436
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
EC: 3.5.2.3
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Q9UX05 | MMILWIMGKAYLSKEIRDVCINFDRRIKEIKSICKPDIALPKGTLILPGAIDLHTHIRGLKLAYKEDVVSGTSEASYGGITLIGDMPNSVPFVNTMETITAKLREFEYYSRVDYFVYSGVTKDLKKVDKFPIAGYKIFPEDLEKEETLEVLKSMKLKILHPEVPLALRGNRKLRLNIWYEIGALYYVKGYQNVHITHATNIRTVRLAKELGFTVDITPHHLLVDREKECLTKVNPPIRDTNERLWLLQAINEVDTVVSDHAPHASFEKQQPYEICPPGIAALSFTVPFILTLVSKGIISIDRAVELISTNPARILNIPYGEIKENNYANFTIIQFKDWRYSTKYSKVIETPLDGFPLRASIYMTIIQGKVGSLEGEVFPVKGINPFGENK | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Catalytic Activity: (S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate
Sequence Mass (Da): 44333
Sequence Length: 390
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
EC: 3.5.2.3
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Q8Y667 | MNRLAVEIPGLSLKNPIMPASGCFGFGQEYSKYYDLNELGAIMAKAVTPEPRLGNPTPRVAETASGMLNAIGLQNPGLEHVLAHELPFLEQFETPIIANVAGATEDDYVQVCARIGESKAVKAIELNISCPNVKHGGIAFGTDPEVAHRLTKAVKNVASVPVYVKLSPNVADIVSIAQAIEAAGADGLTMINTLLGMRIDLKTRKPIIANGTGGLSGPAIKPVAIRMIHQVRAVSNIPIIGMGGVQTVDDVLEFLIAGADAVAVGTMNFTDPFICPKLISELPKRMDALGISSLQDLKKERTNQ | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate
Sequence Mass (Da): 32181
Sequence Length: 304
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.1.14
|
Q8EUY2 | MKNNNRLKINLPGFELKNPIMPASGCFGFGKEFSELYDLSRLGAIIIKAATKNEKFGNPTPRVAETSSGMLNAIGLQNPGVDHIINHELKELEKYDVPIIANVAGDDIDDYVYVAKRISQAKNVVALELNISCPNVKNGGIQFGTDCNVAYNLTKKVKKVSSKPVYVKLSPNVSDIVGMAKAIEEAKADGLSLINTLIGMALDPKSGKPILANKTGGLSGPAIKPVAIRMIYQVSQAVNIPIIGMGGISNVQDVIDFISAGASAVAIGTANFINPYICVEIIDQLESKLDELNVNHIWDLKGRSYR | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate
Sequence Mass (Da): 32909
Sequence Length: 306
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.1.14
|
C6BW12 | MDVSIDFAGLKLKNPILTASGTFGFGLEFQRYGDLESLGGIVVKGLSLKPREGNPMPRIAETPCGMLNAIGIQNPGVEEFINKKLPKLPWKTLPVLANLYATDAEEFGELAGVLAGEEGVAALEVNVSCPNVKEGGIAFGQDPKQITKVAEAVKKNAGNKPIIIKLSPNVTDITVCAKAAEDGGADALSLINTLSGMAVDIERRTPRLANVIGGLSGPAVKPVALRCVYQTVNAVKIPVMGLGGITTAEDAAEFLLVGAKAVQIGTGNFLSPDTAFRIAEELPKVLERVKAESLDEFIGSLKLPK | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate
Sequence Mass (Da): 31986
Sequence Length: 305
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.1.14
|
Q8TT55 | MPAGRKWSYPMYNLTGLELKNPTILAAGVLGTTGASLCRVAREGGAGAVVTKSIGPAPKTGHSNPSMIKLDCGFLNAMGLPNPSYPGFLQELEFAKNNSAVPVIASIFGGAPSEFAEVAEGLLPAKPDALELNVSCPHAEGYGAAVGSNPCLVEAVTAAVKDVVNVPVWVKLTPNVADITCIGNAAESGGADAVVAINTVKGMAIDIESGYPVLGNRSGGLSGKAVKPVAVKCVYDLYTALEIPVIGVGGVSSWEDAVELMMAGAAAVQVGSAVYDRVDIFSEIGAGIEAFLERKGYSDIQKIIGLSHEMV | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate
Sequence Mass (Da): 31847
Sequence Length: 311
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.1.14
|
Q0W8E1 | MKITCNAGGLTLKNPTILAAGVLGTTGASLKRIASMGAGAVVTKSIGTEPKPGHHNPSMIRLEEGYINAMGLPNPSFGEFRQELEIARESGVPVIASIFGATPEEFTAVANGLPGADAYELNVSCPHAKGYGMQCGTDPELVRSITKAVKAAVKVPVWVKLTPNVTDIRPIGLAAQEGGADAVVAINTLKAMAIDINTGWPILGNRSGGLSGPAVKPVAIKCVYDLYEVLDIPVIGVGGVSNWADAIEFMMAGACAVEIGSAVYEDIGTFASVSMGISNYLDRKNMKLDEIIGLAHRVVKQ | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate
Sequence Mass (Da): 31301
Sequence Length: 301
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.1.14
|
Q58070 | MGECMLKTNICGIEFKNPVFLASGIMGETGSALKRIAKGGAGAVTTKSIGLNPNPGHKNPTIVEVYGGFLNAMGLPNPGVDEYLEEIEKVRDELNRMDVRIIGSIYGKDEEEFAEVAKKMERYVDIIELNISCPHAKGYGATIGQNPDLSYDVCKAVKKAVKIPVFAKLTPNVTDIIEIAQAVVDAGVDGLVAINTVRGMAIDIRAKKPILANKFGGLSGKAIKSIGIKVVWDLYENFDVPIIGVGGIMSGEDAIEYMMAGASAVQIGSGVYYRGYDIFKKVCDEIISFLKEENLTLEEIVGMAHE | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate
Sequence Mass (Da): 32940
Sequence Length: 306
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.1.14
|
Q8TXU6 | MRPVEVLGKRWAHPIACASGALAAHRPGMENAVLRGAAAIFTKTVTESPREGHPGPVFVDYLDEGYALNAMGLPNPGPDRMVVEIEEFRDEFDVPVYASVAADGPEGFKRLARAFSGVADGLELNVSCPHAGKGYGAELGSDPEAVAEITEAAVRAFDGPVSVKLTPNVDRETLLEVAAAAIDAGAEALTAVNTLGPGLRIDLRTASPVLGAGVGGLSGPALKPIALRVVADLALEFGEEVEIIGVGGIRNGEDVVEFLFAGAKAVQVATAAREKDFGDIAMETSHILKELGYDGPEEAIGAALPEYRERLRRLGWCQ | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate
Sequence Mass (Da): 33274
Sequence Length: 318
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.1.14
|
O27281 | MFFMLETSICNIELRNPTILAAGVMGSMASSLNRIYRGGAGAVVTKSFSLRPNPGYRNPTTVEVTGGVINAIGLSNPGVEAFREELKLVDEEVPLIASVYGASPEEFASAAASVEEYADMIELNVSCPHAMAGCGASIGQDPELTFRVVSAVKDAVDVPISTKLTPNVTDIVEIAGSAEEAGSDALTLINSLGPGMKIDIKTARPILSNAFGGMSGPAIKPVAVRCVYDVYRSVDIPIMGVGGVRDFQDAVEFLFAGARAVQVGTAIMYDGPEVFMKICRGLEAFMMAEGFSSVDEMVGLAHD | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate
Sequence Mass (Da): 31829
Sequence Length: 303
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.1.14
|
B2A2U4 | MADLKVNFAGIPMKNPVASASGTFGFGFEYQSVISPHELGALVVKGLTLSPKRGNQGTRLHETASGLLNSIGLENPGIDNFINEILPDLRQCDATTLINISGGNDEEYVEITQKLNNCQGIAGLEVNISCPNIREGGLVYGVDPELTYRLVSKVRQSTSFPVIVKLSPNVTDITEIAKACERAGADGLSLINTVAGMAIDIDQKEPVFDNISAGLSGPAIKPIALKAVYQVSQAVDLPVMGMGGIYNYQDAIEFILAGATSVALGTVNFAEPTAAKSIIQGIDNYLEREGYLSVNDIRGLAWK | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate
Sequence Mass (Da): 32174
Sequence Length: 303
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.1.14
|
Q5WVN0 | MYSLLRPLLFRLDAEKAHSLTLSLLHYLPGFYFRKMAGQPVHAMGLVFPHQVGLAAGLDKNGEHLDALAKLGFSFIELGTVTPKGQTGNPKPRLFRIAEANAIINRMGFNNSGVDVLVENVKSANYKGILGINIGKNKETNLNQAADDYLYCFRKVYDHASYVTINISSPNTPDLRQLQQGDYFAELLAQLQKEQIKLADQYGRHVPLVVKVSPDETDETLKQMTDIILQYGIEGIIATNTTCSREMVKNLPCSEEQGGLSGRPLMELSTRCLRLLKQYVGNDVTLIGVGGIDSLESAKDKINAGASLLQVYSGLVYKGPELIHDIVSGLNAV | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 36579
Sequence Length: 333
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Subcellular Location: Cell membrane
EC: 1.3.5.2
|
Q6AE78 | MYRTLFSLVLSRFDPERAHRLAFAAIRALPVIGLGSLLRRFTAPDPSLAVEALGLRFDSPFGIAAGFDKDGEGVIGLGALGFGHVEVGTITARPQPGNDKPRLFRLLPDRAVINRMGFNNHGAGAAANRLLRVRRARRRPVLGVNISKSRAVAVEDATADYLISARALAPVADYLVVNVSSPNTPGLRGLQEREALAPLLSAVKAASGKKPLLVKIAPDLTDEQIVAVARLAVELGLAGIIATNTTIARDGLSSDPAVVEAAGAGGLSGAPLAARSLEVLTLIRANVPPSLCVISVGGVETAQDVQRRLDAGATLVQGYTAFLYRGPLWARQITRGLSALRSR | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 36075
Sequence Length: 343
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Subcellular Location: Cell membrane
EC: 1.3.5.2
|
B7KZJ5 | MIDALFPLARPLLHGLDAETAHDLTIRGLSLLPPRRPPADDASLAVEMFGQSFPNPVGLAAGFDKGARVADALLGLGFGFVEVGGVVPQPQPGNPRPRVFRLPRDRAVINRFGLNSEGLDAVADRLKARAGREGIVGVNIGANKESADRLADYVACTARLAPHVAFITVNVSSPNTPGLRDLQGEAFLDDLLARVVAARDASGSSAAVLLKIAPDIALEGLDAMTATALRRGIQGLVVSNTTIARPSSLVESSVAKETGGLSGRPLFGLSTRLLAETYLRVGDRIPLIGVGGIDSAEAAWAKIRAGARLVQLYSALVYEGPGLVGTIKRGLSQRLRAEGLTSLAPVVGRDAAALARDA | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37272
Sequence Length: 358
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Subcellular Location: Cell membrane
EC: 1.3.5.2
|
Q609J2 | MIYENLLRPLLFRLDPETAHELSLSALRLAAKLGPANPLKQSLPTSPRTVMGLEFPNPIGLAAGLDKNGDCIDGLAALGFGFLEIGTVTPRPQPGNPRPRLFRVPEAGALVNRMGFNNSGVAHLIARVRQTRYRGILGINIGKNLTTPVERALDDYREGLKAVYPYAHYVTLNVSSPNTPGLRSLQFGALLDELLDGLMGEREELTAQHGKRVPLALKVAPDMDSREIKALAGAVVRHGVDAVIATNTTASRDGVEGLEHADEAGGLSGKPLFLRSTEVVARLADALQGRAPIIACGGVFSGADAVAKFEAGASLVQVYTGFIYRGPALLAEIGRVVAAL | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 36078
Sequence Length: 340
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Subcellular Location: Cell membrane
EC: 1.3.5.2
|
B3DX48 | MIYKSFLRPILFSLEPEYAHNLCLGLLSHPFYPFFHKLLASFQKDLPLLPKELWGMQFPNPVGLAAGFDKNGVGLRAWESFGFGFVEIGTVTPLPQEGNPAPRLCRLPKEGALWNSLGFPSQGAQRVAERLKKVFLSGRPKIPVGINIGKNRHTPLEETIEDYKKCFSYFKDLGDFFVVNVSSPNTPGLKSLQQKRFLELLFDRLNPLNSSPRKPLLVKIAPDIELKNLAGILEVLLRNESVGIVIANTLPAKGPGGKEGGLSGKPLRELSLGLIRFVKKETAGRLPIIGVGGIFSSKDAFEKMEAGADLIEIFTGFVYNGPSFPANLCRELERLRKTPQCSAIFLQD | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38519
Sequence Length: 348
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Subcellular Location: Cell membrane
EC: 1.3.5.2
|
A2SHQ5 | MPLIPYALTRPFLFGLDAEHAHELTLASIARLQNTPLQCLWQQPRIDDPVTLAGVRFPNRIGLAAGLDKNGRCIDGFGAMGFGFIEVGTVTPKGQPGNPKPRIFRLPQAEALINRLGFNNDGLDAFLANVRRAGFRQGGGVLGLNIGKNAATPIEDAVDDYLLGLEGVYPHADYVTVNISSPNTQNLRSLQSDAALDALLGRLQERRQQLIARHGRSVPMFVKIAPDLDEAQVDVIAATLKKNAVDGVIATNTTLSRDAVRGQAHATEVGGLSGRPVFEASNRVVGQLRAALGAGYPIIGVGGVMSGADARAKRDVGADVVQIYTGLIYRGPALVSEAARALKG | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 36495
Sequence Length: 344
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Subcellular Location: Cell membrane
EC: 1.3.5.2
|
A7IBC2 | MDLYGVLKPLFRFMTPEQAHHLSIRVLKSGLVPDLSGGPDDPVLATRVWGLDFPNPVGLAAGFDKHCEVADALFRFGFGFVEAGTVTPRPQPGNPLPRLFRLDEDEAVINRFGFNSEGLAPFVFRLGQRRASGKHGIVGANVGKNKESEDALEDYGAGVSATCRLADYLVCNISSPNTPGLRALQARAEMETLLAHVISVRNASMPDPAARTPLLVKVAPDLDDAALADVAEASLATGVDGIIMGNTTLSRPASLQSKFKDETGGLSGKPLLALSTERLGALYRLVGGRLPIIGVGGIASGADAYAKVRAGASLVQIYSALVFHGPGLVTRIKTDLAARLKADGFASIADAVGVDVR | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37534
Sequence Length: 357
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Subcellular Location: Cell membrane
EC: 1.3.5.2
|
Q9PAE7 | MYSLFRPLLFTCDTERAHDISLCTLDIAYHSGALPLLTRHPRPLPTTAFGLNFPNPVGLAAGLDKNGTHIDALFALGFGFIEIGTTTPRPQPGNPKPRLFRLTQQQAVINRMGFNNLGVDALVRNVAGARQRNGPLGINIGKNKDTPNEQASNDYRYCLERVYALADYVTINLSSPNTAGLRALQEEQTLRRLIGELREAQETLAAKHGRHVPMLIKMAPDLSDSDIDAAARVLNEMSVDGVIATNTTVTRPLLRQHRLASETGGLSGAPLLGQSTLVLRRLRTHLPETIALIGVGGICCGADAVAKMAAGANLVQCYTGLIFKGPQLVGECVEAIRRRREASSSGRASTQ | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37890
Sequence Length: 351
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Subcellular Location: Cell membrane
EC: 1.3.5.2
|
P28272 | MTASLTTKFLNNTYENPFMNASGVHCMTTQELDELANSKAGAFITKSATTLEREGNPEPRYISVPLGSINSMGLPNEGIDYYLSYVLNRQKNYPDAPAIFFSVAGMSIDENLNLLRKIQDSEFNGITELNLSCPNVPGKPQVAYDFDLTKETLEKVFAFFKKPLGVKLPPYFDFAHFDIMAKILNEFPLAYVNSINSIGNGLFIDVEKESVVVKPKNGFGGIGGEYVKPTALANVRAFYTRLRPEIKVIGTGGIKSGKDAFEHLLCGASMLQIGTELQKEGVKIFERIEKELKDIMEAKGYTSIDQFRGKLNSI | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with fumarate as the electron acceptor. Molecular oxygen can replace fumarate in vitro. Does not use oxaloacetate or NAD or NADP as electron acceptors.
Catalytic Activity: (S)-dihydroorotate + fumarate = orotate + succinate
Sequence Mass (Da): 34801
Sequence Length: 314
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway.
Subcellular Location: Cytoplasm
EC: 1.3.98.1
|
A2BJ25 | MNSYALDLADVLVEAGAIRFGEFRLSSGSTSPIYIDMRIVPSKPQLFRRVLGMLAEKLNDVREVDVVVGVATAGIIWATGLALLSEKPLAYVRPKRKEHGLQRVVEGIVEGRRVLVVDDVATTGSSLASAVESLREAGAEPVAAMVIVDREQGAVERLADYGVKLYSLATLREIIHAMVVKGYLDPAEATRLINLLYGESL | Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 21776
Sequence Length: 201
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
EC: 2.4.2.10
|
Q74J27 | MHKDQIISQLIKEKIITISPDKPFTYASGMLSPIYTDLRLTVSYPDLRDMIASDLSNLIAAEFPQATIIGGVATAGIPHAALVAEKLHLPMIYVRPKPKDHGKGRQIEGRFSENDQIVLIDDLITTGGSVLNAVKATEKDGGKVAGVASIFTYYLPDAKENFKEANVKYTPLLSYPELLKKENESGHITSDQYDILKTWHEDPWAWGKKFNS | Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 23543
Sequence Length: 212
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
EC: 2.4.2.10
|
Q5WX86 | MNHTKSSFIKLALECQVLKFGEFTLKSGRISPYFFNAGLFYHGNSIRQLGQFYAKTLLEQEISFEHLFGPAYKGIPLATATAVALAELGRDITVTFNRKEVKTHGEGGQLIGSPLTGRTVIIDDVITAGTAFRESQTLIKENGGILRGVIIALDRCERGLTEKSTLSEIREQGIEVYSIINLFDLIEFLKNDNQYEQVQKLESYHELYGAY | Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 23634
Sequence Length: 211
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
EC: 2.4.2.10
|
Q9KVD5 | MKAYQREFIEFALEKQVLKFGEFTLKSGRKSPYFFNAGLFNTGRDLARLGRFYAAALVDSGIEFDVLFGPAYKGIPIATTTAVALADHHDVDTPYCFNRKEAKNHGEGGNLVGSKLEGRVMLVDDVITAGTAIRESMELIQANKADLAGVLVAIDRQEKGKGELSAIQEVERDFGCAVISIVSLTDLITYLEQQGNNTEHLEAVKAYRAQYGI | Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 23402
Sequence Length: 213
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
EC: 2.4.2.10
|
Q9PGZ3 | MSHYRQRFLQLALDSNALCFGEFTLKSGRISPYFFNAGHFNSGAKTAALAQCYADAIDAANMNFDLVFGPAYKGIPLATALACEYARRERDLLLAFNRKEVKNHGEGGTLIGAPLNGRKILIIDDVITAGTAIREVLRIIRNAGGTPTGIAVALNRQEIASETNRQSSVQALMAETGIPVVAIATLSDLLAFVEENASLAKFYEPLLAYKTHYGTEASD | Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 23675
Sequence Length: 219
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
EC: 2.4.2.10
|
P13298 | MPIMLEDYQKNFLELAIECQALRFGSFKLKSGRESPYFFNLGLFNTGKLLSNLATAYAIAIIQSDLKFDVIFGPAYKGIPLAAIVCVKLAEIGGSKFQNIQYAFNRKEAKDHGEGGIIVGSALENKRILIIDDVMTAGTAINEAFEIISNAKGQVVGSIIALDRQEVVSTDDKEGLSATQTVSKKYGIPVLSIVSLIHIITYLEGRITAEEKSKIEQYLQTYGASA | Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 24664
Sequence Length: 226
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
EC: 2.4.2.10
|
Q2GG43 | MFTNPIICALDTHDINHALLLTKMLYGRVSMVKLGLEFFTAYGLSGVQAIADCGVPIFLDLKLHDIPNTVSKAISVIASLNVAMLTIHVSGGREMMIRAMDSISGSVTKLVGVTVLTSMDDSDLKEIGVNESPVQQVMLLSKLAREVGLYGIVCSAFEAKEVRNRYTEKDLKLIVPGIRFDSDCNDQKRVKSPKDAMLAGANYLVIGRPITMSSDPVQTVEDILLSISKCI | 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): 25120
Sequence Length: 231
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
Q834E3 | MHDRPIIALDFPTQKEVAVFLEKFPKEEALFVKVGMELFYAEGPAIVRWLKEQGHDVFLDLKLHDIPNTVEKAMTNLAKLGVAITNVHAAGGVRMMQAAKEGLIKGTQPGAKVPELIAVTQLTSTSEEEMHHDQLINVPLETSVIHYAKCAEKAGLDGVVCSALEARGIQEATKQTFICLTPGIRPAGSAVGDQQRVVTPQHAREIGSTYIVVGRPITQAENPYEAYQEIKKDWSEK | 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): 26036
Sequence Length: 237
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
Q2J838 | MSAGRRSSGGRSAAAPRFTPPRGRAPLAVALDAPDAATALRWAAAVAPTVAVLKIGLELFYREGPAIVTALRAAGVLAGAGGAAVAAGGTGSAPELFLDLKLHDIPATVAGGMRSITPLGPRFVTVHAAGGAAMIRAAIEAAPDVEVAVVTVLTSLDVAALSAIGLAGPPSDAVRRLAVLAVEAGARTLVCSPREVRMVRMELGSNVTLITPGVRPAGSETGDQARTATPEAALVGGSDLVVVGRPITGAPDPGVAARAIAAGLSAAGRAADLL | 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): 26909
Sequence Length: 274
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
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Q7UIA4 | MMTFATQLNAAILRTGSVTCVGLDPRLEQLPKPLRDSVSEKRKDSVAAAYTQFCCEIIDAVAGLVPCVKPQAAFFEQLGPAGMVSLGEVISHANQAGLIVITDGKRNDIGSTATAYADAYLGSAEPDRSPWGSDALTVSPYLGRDSLEPFVEVCDRRAAGIFVLVKTSNPGGGYLQDLSVDGKTIYQSVAELVTELNKSRLDADGYGPVGAVVGATYPEQLVELRKAMPHSILLVPGFGAQGGSADDVRAAMDANGAGAVVNSSRHIVFAHKREEFSVAADESNWQDAVRAATIQMNEQLKG | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 31904
Sequence Length: 302
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
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Q6NCY0 | MAPVDIPDRDRLIVALDLPDLRVAEAMVDRLGDSVGFYKIGYQLAYAGGLPLARALVGAGKKVFVDLKLHDIGNTVARGVESLSHLGASFLTVHAYPQTMKAAVEARGSSKVKILAVTVLTSYDDRDLADAGYRFGVRDLVEARARQAQAIGVDGLVCSPEEAAHLRSIVGPEMDLVTPGIRPAGAAAGDQKRIMTPAKAIAAGASYLVVGRPVLDAPDPKAAADAIVAEIAAARGS | 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): 24690
Sequence Length: 237
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
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Q2RNS7 | MPMAQMTQNPVFVAIDTTVVGDATTLAARLHDEVGGIKLGLEFFARNGHKGVKEVCRAGALPLFLDLKFHDIPNTVAGAVRAVMPLAPALLNVHACGGRAMMIAAREAAQSEALALGIAPPKMIAVTVLTSMDDDDLGGTGVAGGVLDQVRRLAALTRDAGLDGVVCSAREARVLRADLGDDFLLVTPGVRPLWSTTNDQKRVVTPQEAMAEGADVLVIGRPITGATDPAQAARLIAGEIVGWDVGI | 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): 25673
Sequence Length: 247
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
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A7NS27 | MNFFESLDTAAWRNQSRLCVGLDPEPARMPDCLPKDAEGIYTFCAAIMDATVDLVCAYKPNVAFFEAHGAAGWSALERLVKRRPGPPLILDAKRGDIGSTAEAYARSVFTTLGADAVTLSPYLGSDALEPFLRHADRGCFILCKTSNPGSGDLQDARLADGRPLYLAVAEMARDCWNMRGNVGLVVGATHPAALADIRRACPDMLILAPGVGAQGGDLEATVRAAAAGDDPRLIVNVSRTVLYADRGANFAAAARTAARQLRDAINAALRAV | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 28846
Sequence Length: 272
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
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A5UPS3 | MTFRETVCATARRNRSWLCIGLDPEPMRMPVHLPADAEGVYAFCAAIMDATSDLVCAFKPNIAFFEAFGAAGWSALERLIRLRPGPPIILDAKRGDIGSTAEAYARAAFEVLDADAVTVNPYLGGDALEPFLRHSQRGCFILCKTSNPGSHDLQDMRLADGRPLYLAVAEMARDRWNMHGNTGLVVGATHPTAITEVRRACPDMLLLVPGIGAQGGDLDTTVRAAAAVDEPLMMINVSRTVLYADRGTNFAAAARTTALRLRDAINAALMAR | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 29331
Sequence Length: 272
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
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Q9UX10 | MLKSRVILAMDKPLSYQVLKEMENELYGIKVGLPLVLDLGVDKTRELLIGLDVEEIIVDFKLADIGYIMKSIVERLSFANSFIAHSFIGVKGSLDELKRYLDANSKNLYLVAVMSHEGWSTLFADYIKNVIREISPKGIVVGGTKLDHITQYRRDFEKMTIVSPGMGSQGGSYGDAVCAGADYEIIGRSIYNAGNPLTALRTINKIIEDKVMKCKGAIFRKK | 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): 24701
Sequence Length: 222
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
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Q9NRF8 | MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDINLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAVQEWVMNQAKVPVDGNKEEPQICVIELGGTIGDIEGMPFVEAFRQFQFKAKRENFCNIHVSLVPQLSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQVICIHDVSSTYRVPVLLEEQSIVKYFKERLHLPIGDSASNLLFKWRNMADRYERLQKICSIALVGKYTKLRDCYASVFKALEHSALAINHKLNLMYIDSIDLEKITETEDPVKFHEAWQKLCKADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGVCLGMQLAVIEFARNCLNLKDADSTEFRPNAPVPLVIDMPEHNPGNLGGTMRLGIRRTVFKTENSILRKLYGDVPFIEERHRHRFEVNPNLIKQFEQNDLSFVGQDVDGDRMEIIELANHPYFVGVQFHPEFSSRPMKPSPPYLGLLLAATGNLNAYLQQGCKLSSSDRYSDASDDSFSEPRIAELEIS | Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Constitutes the rate-limiting enzyme in the synthesis of cytosine nucleotides.
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 65678
Sequence Length: 586
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
EC: 6.3.4.2
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Q5U2N0 | MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDINLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAIQDWVMNQAKVSVDGNKEDPQICVIELGGTIGDIEGMAFVEAFRQFQFKAKRENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQVICIHDVSSIYRVPLLLEEQGVVKYFQERLDLPINDCSNNLLFKWKTMADRYERLQKICSIALVGKYTKLRDCYASVFKALEHSALAINHKLNLMYIDSIDLEPVTKAEDPVKFHEAWQKLCLADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGICLGMQLAVIEFARNCLNLKDANSTEFDPNTPVPLVIDMPEHNPGDLGGTMRLGLRRTVFTTENSILKKLYGDVPYIEERHRHRYEVNPNLINQFENKDLCFVGEDVDGKRMEIIELTGHPYFIGVQFHPEFSSRPMKPSPPYLGLLLAATGTLNTHLQQMSKLSYSDIYSDASDDSFSEAKFAELDIN | Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Constitutes the rate-limiting enzyme in the synthesis of cytosine nucleotides (By similarity).
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 65674
Sequence Length: 586
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
EC: 6.3.4.2
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Q72BL2 | MKTKFIFITGGVLSSLGKGLAAASVGALLKARGLKVTIQKLDPYINVDPGTMNPFQHGEVYVTDDGAETDLDLGHYERYLAEPMSQKNNYTSGSIYHRVITKERRGDYLGGTVQVIPHVTDEIKNAVLSLAEDDPDVALIEIGGTVGDIEGLPFLEAIRQLRGDLGKDRCLYIHLTLVPYLRAAGEHKTKPTQHSVKELRSIGIQPDIILCRCEEAITADLKRKIALFCNVDQDAVFSAVDVKNIYEVPLRFYEEGFDQKIAIMLRLPAKNPNLEPWETLVDTCAHPQGRVTIGIVGKYVDLKEAYKSLHEALVHGGVANKVAVDLKYVNSEEITEENVAEALKGLDGILVPGGFGYRGVEGKILTIRYARENRVPFFGICLGMQCAVIEFARNVMGLEDANSEEFNELSKNKVIYLMTEWFDHRRQAVERRDSSSDKGGTMRLGSYPCVVVPDTKAHDAYGVKHIDERHRHRFEFNKAYFDAMAQSGMVFSGLSPDGELVEIVELPDHPWFLGCQFHPEFKSNPMQPHPLFREFIRAAKTHPAGKR | 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): 61071
Sequence Length: 547
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
EC: 6.3.4.2
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Q54V77 | MKYIVVTGGVLSGIGKGIIASSTAMILKSMGLRVTSIKIDPYLNIDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDVNLGKDNNITTGKIYNLVIEKERKGQYLGKTVQVVPHITEEIQNWIERVAHLPVDGDKGTPDVCVIELGGTVGDIESMPFTEALRQFQFRVGVENFCLMHVSLVPVLGVVGEQKTKPSQQSIRELRSLGLSPDFCLCRSTQPLTEETKKKISLFCHVAPDNVIGVHDVSNIYRVPILLNQQNLPNLVLRRLQLNPKVDLSKTSPSESTPYWMASWKGLADRMDKITNESLNPIRIAMVGKYTGLTDAYLSVIKALDHASMAIERKMVIDWVEASNLETQNSSTAEYKKSWEMLRGAHGILVPGGFGDRGIEGMILTANYARTSGKPFLGICLGLQIAVIEYARNVMGWENANSEEFSASGSGKNVVVFMPEVSKTHMGGTMRLGSRDTIFTDVDNKISKLYNVDKVGQAVEERHRHRYEVNPEVVDEIHAKGLHFVGKDTTGVRMEIVELKDHDYYVACQFHPEFKSRPQRPSPPFIGLLNASLERLKKM | 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): 63238
Sequence Length: 569
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
EC: 6.3.4.2
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Q9VUL1 | MKYILVTGGVISGVGKGVIASSFGTLLKSCGLDVTSIKIDPYINIDAGTFSPYEHGEVYVLDDGAEVDLDLGNYERFLDVTLHRDNNITTGKIYKLVIEKERTGEYLGKTVQVVPHITDAIQEWVERVAQTPVQGSSKPQVCIVELGGTIGDIEGMPFVEAFRQFQFRVKRENFCLAHVSLVPLPKATGEPKTKPTQSSVRELRGCGLSPDLIVCRSEKPIGLEVKEKISNFCHVGPDQVICIHDLNSIYHVPLLMEQNGVIEYLNERLQLNIDMSKRTKCLQQWRDLARRTETVRREVCIAVVGKYTKFTDSYASVVKALQHAALAVNRKLELVFIESCLLEEETLHSEPSKYHKEWQKLCDSHGILVPGGFGSRGMEGKIRACQWARENQKPLLGICLGLQAAVIEFARNKLGLKDANTTEIDPNTANALVIDMPEHHTGQLGGTMRLGKRITVFSDGPSVIRQLYGNPKSVQERHRHRYEVNPKYVHLLEEQGMRFVGTDVDKTRMEIIELSGHPYFVATQYHPEYLSRPLKPSPPFLGLILASVDRLNQYIQRGCRLSPRQLSDASSDEEDSVVGLAGATKSLSSLKIPITPTNGISKSCNGSISTSDSEGACGGVDPTNGHK | Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Constitutes the rate-limiting enzyme in the synthesis of cytosine nucleotides.
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 69448
Sequence Length: 627
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.2
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Q6MD01 | MQTKYIFITGGVCSSLGKGLTSAAIGLLLEKKGLRVSMLKLDPYLNVDPGTMSPFQHGEVYVTDDGAETDLDLGHYYRYTNSFLSKASNATSGQIYNTVIKRERHGDYLGKTVQVIPHITNEIKQRIVNCGKQQENIDVVLVEIGGTAGDIESLPFLEAIRQFTYDHRNNCLNIHLTYVPYLKAAGEVKTKPSQHSVQVLRGIGIFPDIIVCRCEVNLSDEVKDKISLFCNVNRRAVIEEKDVEHSIYEVPLDLHKQGIDALICELLHLPNPSINLSEWEKILETIKNPKGTVTVGIVGKYVQHQDAYKSVFESLTHGALAAGYKLQIKRFEADKLPLDDNQLAKTIEGCDGYLVPGGFGERGWLGKIHTAKLCREKKIPYFGICLGMQVMAVEFARHVVGLNEANSTEFDPDTIHPVISLLSEQRGLQDLGGTMRLGAYICDLKLHTKAYQAYKSSQISERHRHRYEFNNTYKEQMEKAGFVVAGTLKGENLCEIAEVKDHPWMIGVQFHPEFKSKPTDPHPLFRDFIQAMIIYHKSQHGK | 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): 60873
Sequence Length: 542
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
EC: 6.3.4.2
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Q52NW7 | MEICTKGSRKHLTSRASEPSYNVPENQYVLYVVSSTLSIVKQLVKVAESKKSRFSGAIEKLNERLDSLKDYRIINRDLVVKDLERLKKRFDTEVINAELSEQLAKINVNLSRSYSEKGYLRLEKATGSENEWWAKIKPSQNDDWQQFEPDGYTIFSSRDHYASLFKSYSDYEIEAKIPLPLRRGKAVVLYPEYISRICVLPESRSIQREQENFTKLRDKGIALSKKDWQAKLTTDELAEQEKERATINKRLGYFATEHEKVGIVHKALEPKLKPFQQIEKEWRQCKVKSKSTFPNSMTFVQNPAYQAVHSGFKKLKEQIGLADEDILLSLEKIEAIGLVNMPLLYERWCLLQIIKVLTQAFRYQPEDNWKRKLIANIQGNEEQISIQFFNPSVSRAITLQYEPFLANGKRPDFVLDVEAITKSGNQISKRLVVDAKYYSAAYLKQRGGIGGVIHELYNGKDYSECQENSVFVLHPVLDAVEKVVSPQEWAKDSYLGELSMFDWEPAHHQRQATNYGAVCANPMKSQRYLDEIQRMLGMFLQYGIEDNTSFRGASDDTHAVNFCVSCGSEKVVDVTKSMSSNNQKRWYRCNECTHFTVYTHCGTCNTRLIKNGEYWTYLSLMPMSSINIKCPNCESPV | Function: Catalyzes the hydrolysis of pyrethroids pesticides. Hydrolyzes cis-permethrin at approximately equal rate to trans-permethrin.
Catalytic Activity: (-)-trans-permethrin + H2O = (1S,3R)-3-(2,2-dichlorovinyl)-2,2-dimethylcyclopropanecarboxylate + (3-phenoxyphenyl)methanol + H(+)
Sequence Mass (Da): 73427
Sequence Length: 637
EC: 3.1.1.88
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C0LA90 | MTVTDIILIHGALNRGACYDAVVPLLEARGYRVHAPDLTGHTPGDGGHLSVVDMEHYTRPVADILARAEGQSILLGHSLGGASISWLAQHHPDKVAGLIYLTAVLTAPGITPETFVLPGEPNRGTPHALDLIQPVDEGRGLQADFSRLERLREVFMGDYPGEGMPPAEQFIQTQSTVPFGTPNPMEGRALEIPRLYIEALDDVVIPIAVQRQMQKEFPGPVAVVSLPASHAPYYSMPERLAEAIADFADAPAEYRQTATKAGPDRPAGADGGRADRADLP | Function: Catalyzes the hydrolysis of pyrethroids pesticides. Catalyzes the hydrolysis of cypermethrin to equimolar amounts of cyano-3-phenoxybenzyl alcohol and 2,2-dimethyl-3-(2,2-dichlorovinyl)-cyclopropanecarboxylic acid. Hydrolyzes cis-permethrin at approximately equal rate to trans-permethrin.
Catalytic Activity: (-)-trans-permethrin + H2O = (1S,3R)-3-(2,2-dichlorovinyl)-2,2-dimethylcyclopropanecarboxylate + (3-phenoxyphenyl)methanol + H(+)
Sequence Mass (Da): 30012
Sequence Length: 280
EC: 3.1.1.88
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Q6FCH3 | MAETNSPRYSRILLKLSGEALSGNKDMGIDAQVLDQMSLSIAHLVGLGVQVGIVVGGGNLYRGSQLQKDGLVGRVTGDQMGMLATVMNGLAMRDALVRRNIKTRLMSALSIGTVVEPYSSRDAIRYLSQGEVCVFVAGTGNPFFTTDTAACLRGIEIEANLILKATKVDGVYNKDPSKYDDAVKYDNLTFDQVLDEKLGVMDLTAICLCRDHNVPLQVFDMNKPGALLSVIMGEKEGTHVTK | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 26103
Sequence Length: 242
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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Q9YF40 | MESVVVKISGSLVHPPRLDYLTRLRDVLWGLVDGGFRVAVVVGGGGLARSYIDVLRRAGVSEALLDEMGIESSRLNASLLAKLLYPRSQPYPLASLREVLEVFMTGLIPVSGGFQPGQSTNAVAAVIAEALGARTLLNCLKGVEGVYSDEPSTPGARLLRRLTYRQLEDILVKVSSQRAGSYTLWDMVALSVARRSGLRIVFFDCSDPANIWGALKGEKGSIVEG | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 24202
Sequence Length: 225
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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Q8UFM1 | MMSSKPIYKRVLLKASGEALMGDQGFGIDVAVADRIASDIAEARAMGVEVGVVVGGGNIFRGVAVASKGGDRVTGDHMGMLATVINALALATSLRKLSIDTVVLSAIAMPEICESFSQRAALHHLAQGRVVIFAGGTGNPFFTTDSAAALRAAEMGAEAIFKGTQVDGIYSADPKKDPTATRFDELTHSEVLGKGLAVMDIAAVALARENHIPIIVFSIHEKGGFAQILTGGGRKTIVHDK | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 25057
Sequence Length: 241
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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Q0RBL9 | MAKYRRVVVKLSGRAIAGSAEFGFDSNALEHLAREIIAVRQSGVEVAIVVGGGNLFRGNQSDRWGIDRVEADNIGMLGTVINSLLLRGKLTALGEDNLRVMTAVPVPAVAEPYIRLRAVHLLEKGATVILACGNGQPFLTTDYPAVQRALELGADAVLAAKDGVDGVYDSDPKINPEAQRFSRLSYDEVISRGLRVMDQSAFILARDFGIPLHIFDIEQQGAMTAICRGEHRGTVIDTTGGKAGSAALASSAETVV | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 27257
Sequence Length: 256
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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Q2J528 | MTRYRRVVVKLSGRAIAGSAEFGFDSNALEHLAREIIAVRQSGVEVAIVVGGGNLFRGNQSDRWGIDRVEADNIGMLSTVINSLLLRGKLTALGEDNLRVMTAVPVPAVAEPYIRLRAVHLLEKGATVILACGNGQPFLTTDYPAVQRALELNADAVLAAKDGVDGVYDSDPKINPGARLFSHLSYDEVISRGLRVMDQSAFILARDFGMPLHIFDIEQRGAMTAICRGEHRGTVISSSPEKSEEFGNEVLASPAESTA | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 27903
Sequence Length: 259
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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Q14JD0 | MSNDSSECSQKLPKLKRILLKLSGESLSADQGFGINVESAQPIINQIKTLTNFGVELALVVGGGNILRGGRANFGNKIRRATADSMGMIATMINALALRDMLISEGVDAEVFSAKGVDGLLKVASAHEFNQELAKGRVLIFAGGTGNPFVTTDTTASLRAVEIGADALLKATTVNGVYDKDPNKYSDAKRFDKVTFSEVVSKELNVMDLGAFTQCRDFGIPIYVFDLTQPNALVDAVLDSKYGTWVTLD | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 26659
Sequence Length: 249
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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A5WGF1 | MSDKNPQYSRILLKLSGEALAGGLGMGIDTSVLDKMSLAIAHLCGLGVQVGIVVGGGNLYRGSQLQKEGLVGRVTGDQMGMLATVMNGLAMRDALERRNINTRLMSALPIGEVTESYSSRNAIRYLKNGDVCIFVAGTGNPFFTTDTAACLRGIEIEAGVILKATKVDGVYDKDPSEHADAKKYDALTFDEVLEQKLGVMDLTAIALCREHNVPLQVFDMNKPNSLLNVIMGENEGTRVFH | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 25937
Sequence Length: 241
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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Q8ZTP3 | MALVIKLSGRVFEDEELVFKYAGVIRNLSGKVAVVTGGGEVARRYIAIAKRGGASNTFQDLLGIYASRLNALLLISLLKDAYPRVPANIEEFLEAWSGHRIVVTGGFQPGQSTATVAALVAEAVGASALLNAANIDAVYSDDPRRNPNAQRLRELKYDEFEKIIRSSSLPGGYELMDVWSISILKRNCITTYVFDGRRPDHVVAAARGENPGSKITC | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 23542
Sequence Length: 217
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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Q8U122 | MRIVFDIGGSVLVPENPDIDFIKEIAYQLTKVSEDHEVAVVVGGGKLARKYIEVAEKFNSSETFKDFIGIQITRANAMLLIAALREKAYPVVVEDFWEAWKAVQLKKIPVMGGTHPGHTTDAVAALLAEFLKADLLVVITNVDGVYTADPKKDPTAKKIKKMKPEELLEIVGKGIEKAGSSSVIDPLAAKIIARSGIKTIVIGKEDAKDLFRVIKGDHNGTTIEP | Function: Catalyzes the reversible phosphorylation of UMP to UDP, with ATP as the most efficient phosphate donor.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 24491
Sequence Length: 225
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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K7QVW7 | MTTPQIDERAMEAGAAALQETIVDPGPLDVTALAVAAALAAGLHSAADDPAAALDKCIVLDELTEFAEKLVVHDRPGGIGTTVEYVEVYEDASGVRLGTATGNAVVLKMEPHMWQFHQSVSELADGSFEAVGVIDCTAMLRRMTQVLRVTGRSGRYAGKSGFMTLAISDPNQRPPHYSVQVVLC | Function: Involved in the biosynthesis of the spirotetramate antibiotics pyrroindomycins. Catalyzes the intramolecular cyclization forming the spiro-conjugate moiety in pyrroindomycins, via an exo-selective [4+2] cycloaddition reaction.
Catalytic Activity: 4-[(1R,2R,4aS,5S,8aR)-2-[(2R,3R,5E,7E)-3-ethyl-2-hydroxy-5,7-dimethylnona-5,7-dien-1-yl]-5-hydroxy-1-methyl-1,2,4a,5,6,7,8,8a-octahydronaphthalene-1-carbonyl]-2-methylidene-5-oxo-2,5-dihydro-1H-pyrrol-3-olate = (1S,3R,6R,8R,9R,11R,14S,15S,19R,20R)-8-ethyl-9,15-dihydroxy-3,4,6,20-tetramethyl-21,23-dioxo-24-azapentacyclo[20.2.1.0(1,6).0(11,20).0(14,19)]pentacosa-4,12,22(25)-trien-25-olate
Sequence Mass (Da): 19481
Sequence Length: 184
Domain: The N-terminal 10-AA residues are absolutely required for enzymatic activity.
Pathway: Antibiotic biosynthesis.
EC: 5.-.-.-
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P68004 | YPAKPEAPGEDASPEELSRYYASLRHYLNLVTRQRY | Function: This gut peptide inhibits exocrine pancreatic secretion, has a vasoconstrictory action and inhibitis jejunal and colonic mobility.
PTM: The peptide YY form is cleaved at Pro-2 by the prolyl endopeptidase FAP (seprase) activity (in vitro) to generate peptide YY(3-36).
Sequence Mass (Da): 4242
Sequence Length: 36
Subcellular Location: Secreted
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P10082 | MVFVRRPWPALTTVLLALLVCLGALVDAYPIKPEAPREDASPEELNRYYASLRHYLNLVTRQRYGKRDGPDTLLSKTFFPDGEDRPVRSRSEGPDLW | Function: This gut peptide inhibits exocrine pancreatic secretion, has a vasoconstrictory action and inhibitis jejunal and colonic mobility.
PTM: The peptide YY form is cleaved at Pro-30 by the prolyl endopeptidase FAP (seprase) activity (in vitro) to generate peptide YY(3-36).
Sequence Mass (Da): 11145
Sequence Length: 97
Subcellular Location: Secreted
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P07257 | MLSAARLQFAQGSVRRLTVSARDAPTKISTLAVKVHGGSRYATKDGVAHLLNRFNFQNTNTRSALKLVRESELLGGTFKSTLDREYITLKATFLKDDLPYYVNALADVLYKTAFKPHELTESVLPAARYDYAVAEQCPVKSAEDQLYAITFRKGLGNPLLYDGVERVSLQDIKDFADKVYTKENLEVSGENVVEADLKRFVDESLLSTLPAGKSLVSKSEPKFFLGEENRVRFIGDSVAAIGIPVNKASLAQYEVLANYLTSALSELSGLISSAKLDKFTDGGLFTLFVRDQDSAVVSSNIKKIVADLKKGKDLSPAINYTKLKNAVQNESVSSPIELNFDAVKDFKLGKFNYVAVGDVSNLPYLDEL | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40478
Sequence Length: 368
Subcellular Location: Mitochondrion inner membrane
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Q0WWE3 | MADDEVVDPKKYLEESCKPKCVKPLLEYQACVKRIQGDDSGHKHCTGQYFDYWQCIDKCVAPKLFAKLK | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 7983
Sequence Length: 69
Subcellular Location: Mitochondrion inner membrane
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Q9SJV7 | MPEEDVVDQKRYFEESCKPKCVKPLLEYQACVKRIQDDESGHKHCTGQYFDYWHCVDKCVSV | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 7372
Sequence Length: 62
Subcellular Location: Mitochondrion inner membrane
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Q1ZXP3 | MQTSECKVKGPIQEGCASGCEKSWSAYQACSGRVAKLEHDEKANCLGQFLEHVQCIDKCVGPKLFAQLK | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 7547
Sequence Length: 69
Subcellular Location: Mitochondrion inner membrane
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P07919 | MGLEDEQKMLTESGDPEEEEEEEEELVDPLTTVREQCEQLEKCVKARERLELCDERVSSRSHTEEDCTEELFDFLHARDHCVAHKLFNNLK | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 10739
Sequence Length: 91
Subcellular Location: Mitochondrion inner membrane
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P99028 | MGLEDERKMLTGSGDPKEEEEEELVDPLTTVREHCEQLEKCVKARERLELCDNRVSSRSQTEEDCTEELFDFLHARDHCVAHKLFKNLK | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 10435
Sequence Length: 89
Subcellular Location: Mitochondrion inner membrane
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V5IM94 | MGFWDAVTDLIDAATPWATVEAEAPADTPAETAPASESTEETTAETKAEESAPAAEEPEEEAEEEEEEEEDEDEIVDPKETLEEECRNSKECAPAKHHYDECAARVTGAGADNKEDCVEEFFHLVHCATQCAAPKLWNTLK | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15443
Sequence Length: 141
Subcellular Location: Mitochondrion inner membrane
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Q5M9I5 | MGLEDERKMLTGSGDPKEEEEEELVDPLTTVREHCEQLEKCVKARERLESCDRRVSSRSQTEEDCTEELFDFLHARDHCVAHKLFKSLK | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 10424
Sequence Length: 89
Subcellular Location: Mitochondrion inner membrane
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O42932 | MSFWKNLFTSAFTPISAEADELIKEDRKQFEENTPSKKNFETQSPDEPSPKTTDSTGARDANLSLKTQEPIVSADDAKGAQGKGADEKEEKKETIQPPEEVKTEPPQPEEKEGKEAKEPEEPPKEEAEEPQEGGEEEEEEEEEEEITDPLEKMTQECMDAPDCKEVKHHFEECTARVTKKVEQGDKSEDCIEEFFHLYHCARDCADPKVFKVLV | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 24308
Sequence Length: 214
Subcellular Location: Mitochondrion inner membrane
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P48504 | MSDEEVVDPKATLEVSCKPKCVRQLKEYQACTKRVEGDESGHKHCTGQYFDYWHCIDKCVAAKLFDHLK | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 7977
Sequence Length: 69
Domain: Lacks the acidic domain of other UQCRH.
Subcellular Location: Mitochondrion inner membrane
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P00127 | MGMLELVGEYWEQLKITVVPVVAAAEDDDNEQHEEKAAEGEEKEEENGDEDEDEDEDEDDDDDDDEDEEEEEEVTDQLEDLREHFKNTEEGKALVHHYEECAERVKIQQQQPGYADLEHKEDCVEEFFHLQHYLDTATAPRLFDKLK | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17257
Sequence Length: 147
Subcellular Location: Mitochondrion inner membrane
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Q9SUU5 | MASLLKAFIDPKKNFLARMHMKAISTRLRRYGLRYDDLYDQYYSMDIKEAMNRLPREVVDARNQRLKRAMDLSMKHEYLPKDLQAVQTPFRGYLQDMLALVERESKEREALGALPLYQRTLP | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14527
Sequence Length: 122
Subcellular Location: Mitochondrion inner membrane
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F4JWS8 | MASFLQRLVDPRKNFLARMHMKSVSNRLRRYGLRYDDLYDPLYDLDIKEALNRLPREIVDARNQRLMRAMDLSMKHEYLPDNLQAVQTPFRSYLQDMLALVKRERAEREALGALPLYQRTIP | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14596
Sequence Length: 122
Subcellular Location: Mitochondrion inner membrane
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P00129 | MAGRPAVSASSRWLEGIRKWYYNAAGFNKLGLMRDDTIHENDDVKEAIRRLPENLYNDRVFRIKRALDLSMRQQILPKEQWTKYEEDKSYLEPYLKEVIRERKEREEWAKK | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13476
Sequence Length: 111
Subcellular Location: Mitochondrion inner membrane
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A0A1S4CL59 | MFRAIPFTATVHPYAITAPRLVVKMSAIATKNTRVESLEVKPPAHPTYDLKEVMKLALSEDAGNLGDVTCKATIPLDMESDAHFLAKEDGIIAGIALAEMIFAEVDPSLKVEWYVNDGDKVHKGLKFGKVQGNAYNIVIAERVVLNFMQRMSGIATLTKEMADAAHPAYILETRKTAPGLRLVDKWAVLIGGGKNHRMGLFDMVMIKDNHISAAGGVGKALKSVDQYLEQNKLQIGVEVETRTIEEVREVLDYASQTKTSLTRIMLDNMVVPLSNGDIDVSMLKEAVELINGRFDTEASGNVTLETVHKIGQTGVTYISSGALTHSVKALDISLKIDTELALEVGRRTKRA | Function: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN) (Probable) . Involved in the catabolism of quinolinic acid (QA) (Probable).
Catalytic Activity: CO2 + diphosphate + nicotinate beta-D-ribonucleotide = 5-phospho-alpha-D-ribose 1-diphosphate + 2 H(+) + quinolinate
Sequence Mass (Da): 38330
Sequence Length: 351
Pathway: Alkaloid biosynthesis; nicotine biosynthesis.
Subcellular Location: Mitochondrion
EC: 2.4.2.19
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P54163 | MFNNSFWIFFAIIHFIIVLLFYKGFGKMGLFVWIGFATVCANLQVVKTVELFGLTATLGNVMYGTIFFATDVLNEKYGPAEARKAVWLGFSTLLTLTFVMQGVLLFEPASSDISQTALETIFGFLPRVALGSLLAFIFSQTLDVYVYSAIRRIFPSDRLLWLRNGGSTAVSQLFDTFIFTAVAFLGIYPADVWLHIFISTYLIKFAVSLISLPYAYAAKKMIPNDERSS | Function: Involved in the import of queuosine (Q) precursors, required for Q precursor salvage.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25671
Sequence Length: 229
Subcellular Location: Cell membrane
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P37619 | MNVFSQTQRYKALFWLSLFHLLVITSSNYLVQLPVSILGFHTTWGAFSFPFIFLATDLTVRIFGAPLARRIIFAVMIPALLISYVISSLFYMGSWQGFGALAHFNLFVARIATASFMAYALGQILDVHVFNRLRQSRRWWLAPTASTLFGNVSDTLAFFFIAFWRSPDAFMAEHWMEIALVDYCFKVLISIVFFLPMYGVLLNMLLKRLADKSEINALQAS | Function: Involved in the import of queuosine (Q) precursors, required for Q precursor salvage. Transports 7-cyano-7-deazaguanine (preQ(0)) and 7-aminomethyl-7-deazaguanine (preQ(1)), with a preference for preQ(0).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25269
Sequence Length: 221
Subcellular Location: Cell inner membrane
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P44908 | MKLTSPIFNDQQKRRAIIWLSFFHIFIIAASNYFVQIPFEITLKLTALGAANDFSFHSTWGTLTFPFIFLATDLTVRIFGAEDARKIIFVVMFPALIVSYVISVLFSESKFQGFESLTHFDLFVFRIAIASFAAYVVGQLLDVIVFNRLRQLKTWWVAPTSSMTFGSMADTFVFFSIAFYQSADPFMAEHWAQLGFVDYLFKLFIGIILFVPAYGVVLNVILRKLQMLVTERVPA | Function: Involved in the import of queuosine (Q) precursors, required for Q precursor salvage.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26889
Sequence Length: 235
Subcellular Location: Cell inner membrane
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Q56XY2 | MVFGQVVIGPPGSGKTTYCNGMSQFLSLMGRKVAIVNLDPANDALPYECGVNIEELIKLEDVMSEHSLGPNGGLVYCMEYLEKNIDWLESKLKPLLKDHYILFDFPGQVELFFIHDSTKNVLTKLIKSLNLRLTAVQLIDSHLCCDPGNYVSSLLLSLSTMLHMELPHVNVLSKIDLIGSYGKLAFNLDFYTDVQDLSYLEHHLSQDPRSAKYRKLTKELCSVIEDYSLVNFTTLDIQDKESVGDLVKLIDKSNGYIFAGIDASVVEYSKIAIGQTDWDYNRVAAVQEKYMEDEEIQD | Function: Small GTPase that is essential for the correct formation of the tangential divisions in early embryos. Associates with microtubule during mitosis and may function in the positioning of the division plane. May participate in the patterning of the early embryo at the octant-dermatogen transition . Is crucial for normal development of the plant .
Sequence Mass (Da): 33565
Sequence Length: 298
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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Q8W586 | MDPMESSSEQDIVEESQKLVDSLDKLRVSAASSSSNFKKKPIIIIVVGMAGSGKTSFLHRLVCHTFDSKSHGYVVNLDPAVMSLPFGANIDIRDTVKYKEVMKQYNLGPNGGILTSLNLFATKFDEVVSVIEKRADQLDYVLVDTPGQIEIFTWSASGAIITEAFASTFPTVVTYVVDTPRSSSPITFMSNMLYACSILYKTRLPLVLAFNKTDVADHKFALEWMEDFEVFQAAIQSDNSYTATLANSLSLSLYEFYRNIRSVGVSAISGAGMDGFFKAIEASAEEYMETYKADLDMRKADKERLEEERKKHEMEKLRKDMESSQGGTVVLNTGLKDRDATEKMMLEEDDEDFQVEDEEDSDDAIDEDDEDDETKHYYL | Function: Small GTPase that is essential for the correct formation of the tangential divisions in early embryos. Associates with microtubule during mitosis and may function in the positioning of the division plane. May participate in the patterning of the early embryo at the octant-dermatogen transition.
Sequence Mass (Da): 42551
Sequence Length: 379
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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Q9AYU1 | MAGKLMRAVQYDGYGGGAAGLKHVEVPIPSPGKGEVLIKLEAISLNQLDWKLQNGMVRPFLPRKFPFIPATDVAGEVVRIGQDVKNFKPGDKVVAMLGSFGGGGLAEYGVASEKLTVHRPPEVSAAESSGLPIAGLTAHMALTQHIGLNLDKSGPHKNILITAASGGVGQYAVQLAKLGNTHVTATCGSRNFDLVKSLGADEVIDYKTPEGAALKSPSGKKYDAVIHCASPLPWSVFKPNLSKHGKVIDITPGPRVMLTSAMTKLTCSKKRLVTLLVVIKGEHLSYLVELMREGKLKTVIDSKFSLSKAEEAWAKSIDGHATGKIVVEP | Function: NADPH-dependent single-electron reducing quinone reductase . Involved in haustorium initiation in parasitic plants through redox cycling of exogenous haustorium-inducing factors . Can use 9,10-phenanthrenequinone (PAQ), 1,2-naphthoquinone, 5-hydroxy-1,4-naphthoquinone (juglone) and 2,6-dimethoxy-p-benzoquinone (DMBQ) as substrates, but has no activity with menadione, diamide, 2,3-dimethoxy-5-methyl-1,4-benzoquinone or 1,4-naphthoquinone .
Catalytic Activity: 2 a quinone + H(+) + NADPH = 2 a 1,4-benzosemiquinone + NADP(+)
Sequence Mass (Da): 34872
Sequence Length: 329
Subcellular Location: Plastid
EC: 1.6.5.5
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Q9AYU0 | MATKVYIVYYSTYGHVERLAQEIKKGAESVGNVEVKLWQVPEILSDEVLGKMWAPPKSDVPVITPDELVEADGIIFGFPTRFGMMAAQFKAFFDSTGGLWKTQALAGKPAGIFFSTGTQGGGQETTALTAITQLTHHGMIYVPIGYTFGADMFNMEKIKGGSPYGAGTFAGADGSRQPSDIELKQAFHQGMYIAGITKKIKQTSA | Cofactor: Binds 1 FMN per monomer.
Function: NAD(P)H:quinone oxidoreductase reducing quinones by a two-electron transfer mechanism . Can use either NADPH or NADH as electron donor (Ref.2). Can use menadione, 5-hydroxy-1,4-naphthoquinone (juglone) and 2,6-dimethoxy-p-benzoquinone (DMBQ) as substrates (Ref.2). Mitigates the toxicity of exogenous quinones in the rhizosphere (Ref.2).
Catalytic Activity: a quinone + H(+) + NADH = a quinol + NAD(+)
Sequence Mass (Da): 22100
Sequence Length: 205
EC: 1.6.5.2
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P0DOV3 | MEDRQLTNADNENGRKCACGGAAPFFVGLVVALVFGWWAFPEMLYSQKEQPIRFSHKVHVNDAGMECKQCHSLREDGSFAGLPSTASCAECHSDVLGSDPEEARFVAEYVKSGKEVKWLVYQYQPDNVFFSHAAHSLDGCNQCHQFSERELCNLCHLDVADSDKAPTHYENKLTGYSKQTMKMWQCERCHANENHLGVTNSSNACFVCHK | Cofactor: Binds 6 heme c groups covalently per subunit.
Function: Component of the respiratory Qrc complex, that catalyzes the reduction of the menaquinone pool using electrons transferred from the reduced periplasmic cytochrome c3, and which is probably involved in sulfate respiration. Is likely essential for growth on H(2) or formate since the periplasmic hydrogenases and/or formate dehydrogenases act as primary electron donors for the Qrc complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23605
Sequence Length: 210
Subcellular Location: Cell inner membrane
EC: 1.97.-.-
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Q72E84 | MALDRRGFLKFIGGATAGILATPVVWKGLDDVSIWSQNWSWIPRNIKGANSYVPTVSKLCPTGIGVRVRLVDGRPVRVIGNPEHPLSKGGVSSIAAAEVQMLYSPARMKRPLKRSPDGAYVMISWEEAEAMLLDGLKAAKGGDALACISGDDNGTINELLSAFVQQSGSKSFFLMPGEAQPAAKAWDLMGGEGQIGYDIEKSDFVLAIGANVLEAWGTAIRNRHAFGASHPHGAEPTAQFVYAGPVLNNTATGADDWLPIRPGTESAFALGLAHLLIKAGASSSAPDFDAFRSLAASFSPEKVAAQTGVDAKALTALAQALAKAKHPLVIVGSEFSQGAGAAPVMAGIALNMLLGSVNRDGGLRALPVARKVVPAGMDRKAMLQQDLTLWASAIASGKAKAPKAMLVYEANPVYALPQGSAFKDTLAKVPFKVAFTSFLDETAMQCDLVIPVSMGLERLDDVCTPYGCGEVVYSLATPVTAPLFDTKPAGDALIALGGKLGLDLGVASFEDMLKAKAAAHGADFDKLAEGTAFTSRATVGANLSFRPDVLSKALDVKAPALPLALAPVMKLNMGTSKTAIPPFNTKTIRRWEVQGKEGYVMLNGATARKLGLAQHDRVVLSNPTGKVTVRVNIFEGVMNDTVAMPLGFGHTAFDEFSKGKGENVMHLLAPSTEPVTGLAVWTGAGVNIAKA | Cofactor: There is no molybdenum or tungsten pterin cofactor present in the Qrc complex, despite the similarity of QrcB to molybdopterin-containing oxidoreductases.
Function: Component of the respiratory Qrc complex, that catalyzes the reduction of the menaquinone pool using electrons transferred from the reduced periplasmic cytochrome c3, and which is probably involved in sulfate respiration. Is likely essential for growth on H(2) or formate since the periplasmic hydrogenases and/or formate dehydrogenases act as primary electron donors for the Qrc complex. The function of the QrcB subunit is unknown; in the absence of a catalytic site, it may provide a structural scaffold for the other subunits.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Sequence Mass (Da): 72355
Sequence Length: 691
Subcellular Location: Periplasm
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Q72E85 | MSSFKEFKIKWGMVIDLDKCTGCGACMVACQAENNIAPQPDASNKLKSLNWLVVYELNNGKPFPEHDVAYLPRPCMQCGKPSCVSVCPVVATDKNEEGGIVSQVYPRCIGCRYCMASCPYHARYFNWFDPTWPEGMDKTLTPDVSVRPRGVVEKCTFCHHRFMQAKDKARVEGRDPSALRDGDYVTSCTEACPNGAIIFGDFNNPEHRVHELHKSKYAFRLLERLGTDPQVYYLSRREWVRRLGDNYLEHEKVKG | Cofactor: Binds 3 [4Fe-4S] cluster per subunit.
Function: Component of the respiratory Qrc complex, that catalyzes the reduction of the menaquinone pool using electrons transferred from the reduced periplasmic cytochrome c3, and which is probably involved in sulfate respiration. Is likely essential for growth on H(2) or formate since the periplasmic hydrogenases and/or formate dehydrogenases act as primary electron donors for the Qrc complex. QrcC is an electron-transferring subunit; its cubane iron sulfur clusters form a pathway for electron transfer between the hemes of QrcA and the membrane quinone pool.
Sequence Mass (Da): 29043
Sequence Length: 255
Subcellular Location: Periplasm
EC: 1.97.-.-
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Q72E86 | MDKNYNLPVDAELFPEGCERCSLSKFMMWMAFVFVFFGWGLYAAYRVLAEGLGVTGLDDYFGFGLWITFDLAVIALGAGAFFSGLLRYILNIDPLKNIINLAVIIGFLCYSGAMLVLVLDIGQPLRAWFGYWHANVHSMLTEVIFCITCYCLVLIIEYVPLILENRQLNKNKLVHAVAHNFHVMMPLFAGIGAFLSTFHQGSLGGMYGVLFGRPYIYREGFFIWPWTFFLYVLSAVGSGPVFTVLVCTLMEKMTGRKLVSWEVKSLMGKIAGTMLMVYLIFKFADTYAWAYDLLPRQGLTFDQMFTSGWIYGKWMLWAELFYCGLVPAIILIVPALRNNPVLFYSAAILDCIGITINRYVMTVQALAIPVMPFDSWESYLPNWAEWGASVMIVAYAALVLSLSYRYLPIFPQEAELNRK | Function: Component of the respiratory Qrc complex, that catalyzes the reduction of the menaquinone pool using electrons transferred from the reduced periplasmic cytochrome c3, and which is probably involved in sulfate respiration. Is likely essential for growth on H(2) or formate since the periplasmic hydrogenases and/or formate dehydrogenases act as primary electron donors for the Qrc complex. The QrcD subunit anchors the protein complex to the membrane and likely interacts with the quinone pool.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47537
Sequence Length: 419
Subcellular Location: Cell inner membrane
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C3ZQF9 | MMLGNMTFTQTILHELLRQHNMTKNEFIERFGLPPLVYVPELSPGAKTVTLVFYVIIFLAALLGNTLVVVVVWKNKVMRTTMNIFICSLAASDLLITIVCIPVTLMQNMLQNWIMGDFMCKLVPFIQTIAVASSILTLTGIAIERYYAIIHPLKVKYLLSKTRAGIILALVWVVSVGVATPMLFVHKAEEIHDFLYEQRFVTCQEKWWGQTQQTSYTIFNLVVLFIIPLLTMTSLYIRIAHRLWVQQPVGVTGNFAHGNSVRRKRQAVKMLVVVVLLFAVCWLPYHTVTVMNELTGLRLEEKSAKLLIAIVQLIAFSNSFNNPVVYAILNENFKKNFMTMLRCRVNRVSPQQVTPNTLQTPLEQSTRSCRLPAGAPNQQI | Function: Receptor for QRFP-like peptide. The activity of this receptor is mediated by G proteins which activate a phosphatidyl-inositol-calcium second messenger system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43187
Sequence Length: 380
Subcellular Location: Cell membrane
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Q96P65 | MQALNITPEQFSRLLRDHNLTREQFIALYRLRPLVYTPELPGRAKLALVLTGVLIFALALFGNALVFYVVTRSKAMRTVTNIFICSLALSDLLITFFCIPVTMLQNISDNWLGGAFICKMVPFVQSTAVVTEILTMTCIAVERHQGLVHPFKMKWQYTNRRAFTMLGVVWLVAVIVGSPMWHVQQLEIKYDFLYEKEHICCLEEWTSPVHQKIYTTFILVILFLLPLMVMLILYSKIGYELWIKKRVGDGSVLRTIHGKEMSKIARKKKRAVIMMVTVVALFAVCWAPFHVVHMMIEYSNFEKEYDDVTIKMIFAIVQIIGFSNSICNPIVYAFMNENFKKNVLSAVCYCIVNKTFSPAQRHGNSGITMMRKKAKFSLRENPVEETKGEAFSDGNIEVKLCEQTEEKKKLKRHLALFRSELAENSPLDSGH | Function: Receptor for the orexigenic neuropeptide QRFP. The activity of this receptor is mediated by G proteins that modulate adenylate cyclase activity and intracellular calcium levels.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49488
Sequence Length: 431
Subcellular Location: Cell membrane
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P83861 | MQALNITAEQFSRLLSAHNLTREQFIHRYGLRPLVYTPELPARAKLAFALAGALIFALALFGNSLVIYVVTRSKAMRTVTNIFICSLALSDLLIAFFCIPVTMLQNISDKWLGGAFICKMVPFVQSTAVVTEILTMTCIAVERHQGLIHPFKMKWQYTTRRAFTILGVVWLAAIIVGSPMWHVQRLEIKYDFLYEKEHVCCLEEWASPMHQRIYTTFILVILFLLPLVVMLVLYSKIGYELWIKKRVGDSSALQTIHGKEMSKIARKKKRAVVMMVTVVALFAACWAPFHVVHMMVEYSNFEKEYDDVTIKMVFAVAQTIGFFNSICNPFVYAFMNENFKKNFLSAVCYCIVRETFSPGQKPGNSGISMMQKRAKLSRSQRPVAEAKGDLFSDANVDVKLCEQPGEKRQLKRQLAFFSSELSENSTFGSGHEL | Function: Receptor for the orexigenic neuropeptide QRFP. The activity of this receptor is mediated by G proteins that modulate adenylate cyclase activity and intracellular calcium levels (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49245
Sequence Length: 433
Subcellular Location: Cell membrane
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