GCW_01080
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Uniprot: A0A0F6CK76
Description: CTP synthetase EC number: 6.3.4.2 Annotation score: 2 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: ATP + UTP + L-glutamine = ADP + phosphate + CTP + L-glutamate. {ECO:0000256|SAAS:SAAS00037321}. Cofactor: Enzyme regulation: Function [CC]: FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. {ECO:0000256|SAAS:SAAS00037305}. Pathway: PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2. {ECO:0000256|SAAS:SAAS00037318}. Active site: Binding site: Calcium binding: DNA binding: Metal binding: Nucleotide binding: Site: Gene names (primary): pyrG Gene names (synonym): Mass: 61,282 Subunit structure [CC]: SUBUNIT: Homotetramer. {ECO:0000256|SAAS:SAAS00356542}. Gene ontology (GO): ATP binding [GO:0005524]; CTP synthase activity [GO:0003883]; 'de novo' CTP biosynthetic process [GO:0044210]; glutamine metabolic process [GO:0006541] Gene ontology IDs: GO:0003883; GO:0005524; GO:0006541; GO:0044210 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the CTP synthase family. {ECO:0000256|SAAS:SAAS00548960}.; SIMILARITY: Contains glutamine amidotransferase type-1 domain. {ECO:0000256|SAAS:SAAS00037304}. Protein families: CTP synthase family Coiled coil: Domain [FT]: DOMAIN 300 540 Glutamine amidotransferase type-1. {ECO:0000259|PROSITE:PS51273}. Motif: Region: EMBL: CP006916 ProteinModelPortal: MEROPS: EnsemblBacteria KO: AHB99498 UniPathway: K01937 CDD: Gene3D: HAMAP: 3.40.50.300;3.40.50.880 InterPro: PANTHER: IPR029062;IPR004468;IPR017456;IPR017926;IPR027417 PIRSF: PTHR11550 PRINTS: PROSITE: Pfam: PS51273 ProDom: PF06418;PF00117 SMART: SUPFAM: TIGRFAMs: SSF52317;SSF52540 243985-245608(+) >nucleotide sequence AAGGGGTTGATCGTTGCTTCGATTGCAAGTATTTTCAAACACCAAAACTTTAAGATTAAT ATCTTAAAGCTTGATCCCTATCTTAATGTTGATTCGGGAACGATGTCACCATATGAACAT GGTGAGGTGTTTGTTACTTCGGATGGAACAGAGACTGATTTAGATCTTGGTTATTATGAA CGTTTCTTAGTTCAAGATCTAAATGAACGTTCATCAATCACATCAGGTAAAGTTTATTTT AGTGTGATTAATAAAGAACGTAAGGGTGAGTATTTGGGTAAAACGGTCCAATTAATCCCT CACGTTACTAATGAGATTAAAAGACGGATTGCTCTAGCAGCTACTGATGAGAACAATCAA TCTTACGATTTAGTTTTTTGTGAGATCGGTGGGACGATTGGTGATTTAGAATCATTACCT TTTATTGAGGCAATCAAGCAGATCATTCGCGAAAATAATAAGCACGACACGGCTTTTATC CATGTGGTGCCCATCATTAGTTTATCTAACAGCGAACAGAAAACCAAACCATTACAACAC TCTTTAAAAGAGTTAAACAACCTTGGGATTAATCCCGATTTTTTAGTAATTAGATCTAAA GAAAGTTTAGATCTAAAAACCAAGCATAAGATTGCTAGTGCAACCTATCTAAATAAAGAT CATATCTTTAACTCTGTTGATTTAAATAATACTTACTTCTTACCAGATTATTTAAATCAA CAAAAGATCCATGAAAAGATTGCTAACAAATTACAGATCACGATTGATCCAAAGATTAAG TTATCAGCTTGAGATGATCTAGCTAAGAAGATTAATAACCAAGATAACTTAGTAAGAAAG ATCGCGATTATTGGGAAATATACCCAATTTAAAGATGCATATCTCTCTTTAATTGAATCG CTTAATTTAGCTGGTTATCATAACCACGTTAAGTTAGAGATCGATTGAATCGAATCATCA TTATATGATGATGCATCTTTAGAAGAAGTTAATCATAAACTTAAAGATGTTCATGGGGTT ATTGTCCCTGGTGGGTTTGGTTCTAGGGGTGTTGAAGGTAAGATTAAGTTCATTCAGGTT GCTAGAACTAAAAAGATTCCATTCCTTGGGATCTGTTTGGGGATGCAATTAGCTTGTGTT GAGTATGCTAGAAATGTGTTGGGAATGGCTGATGCTAACTCAAGTGAGTTTAATTCACAA ACTACTTATCCGATCTTTAAGATAATGAACCCAGATGATCTTAATTATGGTGGAAGTTTA AGATTGGGTGATTATTTAGTTAGTTTAAAAGATCAAACTTTAGCTAAAGCTATTTATCAA CAAGATAGTATTAAAAGAAGACACCGTCACCGTTATGAGTTTAATAACGATTATTTAAAC CAGTTTAATGACGGTGAATTCATTGTTTCAGGGATCTATCTTCAAGAAAACTTAGTCGAA ACAATCGAACTAAAAAACCATCCGTTTTTTATTGGTTGTCAGTATCACCCAGAGTTTTCA TCAAAGATTACAGCGGCTGAAGCGTTGTTTGATTCACTAGTTAAAAAAATCAAAATGTTA TAA >protein sequence GEVFVTSDGTETDLDLGYYERFLVQDLNERSSITSGKVYFSVINKERKGEYLGKTVQLIP HVTNEIKRRIALAATDENNQSYDLVFCEIGGTIGDLESLPFIEAIKQIIRENNKHDTAFI HVVPIISLSNSEQKTKPLQHSLKELNNLGINPDFLVIRSKESLDLKTKHKIASATYLNKD HIFNSVDLNNTYFLPDYLNQQKIHEKIANKLQITIDPKIKLSAWDDLAKKINNQDNLVRK IAIIGKYTQFKDAYLSLIESLNLAGYHNHVKLEIDWIESSLYDDASLEEVNHKLKDVHGV IVPGGFGSRGVEGKIKFIQVARTKKIPFLGICLGMQLACVEYARNVLGMADANSSEFNSQ TTYPIFKIMNPDDLNYGGSLRLGDYLVSLKDQTLAKAIYQQDSIKRRHRHRYEFNNDYLN QFNDGEFIVSGIYLQENLVETIELKNHPFFIGCQYHPEFSSKITAAEALFDSLVKKIKML |
© Fisunov Lab of Proteomics, 2016.