SPM_004755

Uniprot: A0A037UQP4
Description: CTP synthetase
EC number: 6.3.4.2
Annotation score: 3 out of 5
Miscellaneous [CC]: MISCELLANEOUS: CTPSs have evolved a hybrid strategy for distinguishing between UTP and CTP. The overlapping regions of the product feedback inhibitory and substrate sites recognize a common feature in both compounds, the triphosphate moiety. To differentiate isosteric substrate and product pyrimidine rings, an additional pocket far from the expected kinase/ligase catalytic site, specifically recognizes the cytosine and ribose portions of the product inhibitor. {ECO:0000256|HAMAP-Rule:MF_01227}.
Protein existence: Inferred from homology
Catalytic activity: CATALYTIC ACTIVITY: ATP + UTP + L-glutamine = ADP + phosphate + CTP + L-glutamate. {ECO:0000256|HAMAP-Rule:MF_01227, ECO:0000256|SAAS:SAAS00037321}.
Cofactor:
Enzyme regulation: ENZYME REGULATION: Allosterically activated by GTP, when glutamine is the substrate; GTP has no effect on the reaction when ammonia is the substrate. The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis. Inhibited by the product CTP, via allosteric rather than competitive inhibition. {ECO:0000256|HAMAP-Rule:MF_01227}.
Function [CC]: 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. {ECO:0000256|HAMAP-Rule:MF_01227}.
Pathway: PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2. {ECO:0000256|HAMAP-Rule:MF_01227, ECO:0000256|SAAS:SAAS00037318}.
Active site: ACT_SITE 381 381 Nucleophile; for glutamine hydrolysis. {ECO:0000256|HAMAP-Rule:MF_01227}.; ACT_SITE 506 506 {ECO:0000256|HAMAP-Rule:MF_01227}.; ACT_SITE 508 508 {ECO:0000256|HAMAP-Rule:MF_01227}.
Binding site: BINDING 13 13 Allosteric inhibitor CTP; alternate. {ECO:0000256|HAMAP-Rule:MF_01227}.; BINDING 13 13 UTP; alternate. {ECO:0000256|HAMAP-Rule:MF_01227}.; BINDING 54 54 L-glutamine. {ECO:0000256|HAMAP-Rule:MF_01227}.; BINDING 71 71 ATP. {ECO:0000256|HAMAP-Rule:MF_01227}.; BINDING 224 224 Allosteric inhibitor CTP; alternate. {ECO:0000256|HAMAP-Rule:MF_01227}.; BINDING 224 224 UTP; alternate. {ECO:0000256|HAMAP-Rule:MF_01227}.; BINDING 242 242 ATP. {ECO:0000256|HAMAP-Rule:MF_01227}.; BINDING 354 354 L-glutamine; via carbonyl oxygen. {ECO:0000256|HAMAP-Rule:MF_01227}.; BINDING 405 405 L-glutamine. {ECO:0000256|HAMAP-Rule:MF_01227}.; BINDING 461 461 L-glutamine; via amide nitrogen. {ECO:0000256|HAMAP-Rule:MF_01227}.
Calcium binding:
DNA binding:
Metal binding: METAL 71 71 Magnesium. {ECO:0000256|HAMAP-Rule:MF_01227}.; METAL 141 141 Magnesium. {ECO:0000256|HAMAP-Rule:MF_01227}.
Nucleotide binding: NP_BIND 14 19 ATP. {ECO:0000256|HAMAP-Rule:MF_01227}.; NP_BIND 148 150 Allosteric inhibitor CTP. {ECO:0000256|HAMAP-Rule:MF_01227}.; NP_BIND 188 193 Allosteric inhibitor CTP; alternate. {ECO:0000256|HAMAP-Rule:MF_01227}.; NP_BIND 188 193 UTP; alternate. {ECO:0000256|HAMAP-Rule:MF_01227}.
Site:
Gene names (primary): pyrG
Gene names (synonym):
Mass: 59,578
Subunit structure [CC]: SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01227, 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|HAMAP-Rule:MF_01227, ECO:0000256|SAAS:SAAS00548960}.; SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. {ECO:0000256|HAMAP-Rule:MF_01227}.
Protein families: CTP synthase family
Coiled coil:
Domain [FT]: DOMAIN 292 531 Glutamine amidotransferase type-1. {ECO:0000259|PROSITE:PS51273}.
Motif:
Region: REGION 1 267 Amidoligase domain. {ECO:0000256|HAMAP-Rule:MF_01227}.; REGION 382 385 L-glutamine binding. {ECO:0000256|HAMAP-Rule:MF_01227}.
EMBL: AGBZ02000004
ProteinModelPortal:
MEROPS:
EnsemblBacteria KO: KAI92050
UniPathway:
CDD:
Gene3D:
HAMAP: 3.40.50.300;3.40.50.880
InterPro: MF_01227
PANTHER: IPR029062;IPR004468;IPR017456;IPR017926;IPR027417
PIRSF: PTHR11550
PRINTS:
PROSITE:
Pfam: PS51273
ProDom: PF06418;PF00117
SMART:
SUPFAM:
TIGRFAMs: SSF52317;SSF52540

19588-21184(+)

>nucleotide sequence
ATGGCAAAATATATTTTTGTAACTGGTGGAGTTGTTAGTGGTTTAGGGAAAGGAATTACA
GCTTCTTCAATTGGTGTTTTATTAAAAGCAAGTGGGTTAAATGTTTTTATGCAAAAATTT
GATCCATATTTAAATGTTGATCCTGGAACAATGAGTCCTTATCAACATGGTGAAGTTTTT
GTAACAGCAGATGGTGCTGAAACAGATTTAGATTTAGGACATTATGAACGTTTTATTGAT
GAAAATTTAACTAAAGAATCAAATATTACTTCAGGACGAATATATAAAAATGTAATTGAA
AAAGAACGTCGTGGCGAATATGAAGGTGGAACAGTTCAAGTTGTTCCACATGTTACAAAT
GAAATTAAAAAGAAAGTTTATCATGCTGCATCAACTTCAAAAGCAGATATTATTATTACT
GAAATTGGGGGGACAGTTGGAGATATTGAATCGTTACCTTTTATTGAAGCAATTCGTCAA
GTTCGAATGGAACAAGGACGAGAAAATGTTATTTATATGCATGTTTCCTTAGTTCCATAT
ATTGCAGCATCAAAAGAATCAAAGACAAAGCCAACCCAACATTCAGTCCGAGAACTATTA
TCACTGGGGATTCAACCAGATATTGTTGTTGCCCGTACTGAACAAGTTCTAGATGATAAC
GTTCTTGAAAAAATTGCTCTATTTTGTAATATTGAAAAAAGTAATGTTTTAGTAGCTACT
GATGTTGCTAGTATTTATGAAGTACCATTAAAAATGTATGAACAAAATGCTCAAATAGTA
ATTAGTAAGTTATTAAATTTAAAAATCACTAAAACTGATATGTCAGAATGAAAACGGTTT
GTTGAAAAAATTAATCAGTCTCAACAAGTAATTGAAATTAAATTAGTTGGAAAATATATT
GAACTTCCAGATGCTTATTTATCAGTTAGTGAATCGTTGCGAATTGCTGGATATGAAAAT
AAGGTTAAAATTAAAATTGATTGAATTAAAGCAGAAGATATTAATAAAAAAAATTATCAA
CAATTATTAAAAAATGCCAAAGGCATTTTAGTTCCTGGTGGTTTTGGTGAACGTGGTTTT
GAAGGGAAAATTTTAGCATGCCAATTTGCTCGTGAAAATAACATTCCGTTTTTTGGAATT
TGTTTTGGAATGCAAGCAGCTGTAATTGAATTTGCCCGTAATGTTTGTCATATTCAAGAT
GCTAATTCTTCAGAATTAACAGAAACAAAAAATGCAATTATTGACATTATTCGTGGAAAA
GATAAAACTGATGCTTTAGGAGGAACATTACGCTTAGGTAATTATAAAACAACTTTTGTT
CCAAACACATTAGCCCATAAATTATATGGCAAAAATGAGGTTTTAGAACGTCATCGCCAT
CGCTATGAAGTTAATAATGATTATCGTGAACAATTAGCGCAAGCAGGGTTAGTATTTAGT
GGCCTTTATGTTGAGAAAAACTTAGTGGAAGTCATTGAAATCCCCAAACATCCTTTTTAC
CTTGCTGCTCAATATCATCCCGAATTTACTTCTCGCCCAAATAAACCGAATCCATTATTT
AATGGTTTTGTGCAAGCAGTAATTAAAAATAAATAA

>protein sequence
MAKYIFVTGGVVSGLGKGITASSIGVLLKASGLNVFMQKFDPYLNVDPGTMSPYQHGEVF
VTADGAETDLDLGHYERFIDENLTKESNITSGRIYKNVIEKERRGEYEGGTVQVVPHVTN
EIKKKVYHAASTSKADIIITEIGGTVGDIESLPFIEAIRQVRMEQGRENVIYMHVSLVPY
IAASKESKTKPTQHSVRELLSLGIQPDIVVARTEQVLDDNVLEKIALFCNIEKSNVLVAT
DVASIYEVPLKMYEQNAQIVISKLLNLKITKTDMSEWKRFVEKINQSQQVIEIKLVGKYI
ELPDAYLSVSESLRIAGYENKVKIKIDWIKAEDINKKNYQQLLKNAKGILVPGGFGERGF
EGKILACQFARENNIPFFGICFGMQAAVIEFARNVCHIQDANSSELTETKNAIIDIIRGK
DKTDALGGTLRLGNYKTTFVPNTLAHKLYGKNEVLERHRHRYEVNNDYREQLAQAGLVFS
GLYVEKNLVEVIEIPKHPFYLAAQYHPEFTSRPNKPNPLFNGFVQAVIKNK