ACL_RS06905

Uniprot: A9NE27
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 383 383 Nucleophile; for glutamine hydrolysis. {ECO:0000256|HAMAP-Rule:MF_01227}.; ACT_SITE 507 507 {ECO:0000256|HAMAP-Rule:MF_01227}.; ACT_SITE 509 509 {ECO:0000256|HAMAP-Rule:MF_01227}.
Binding site: BINDING 14 14 Allosteric inhibitor CTP; alternate. {ECO:0000256|HAMAP-Rule:MF_01227}.; BINDING 14 14 UTP; alternate. {ECO:0000256|HAMAP-Rule:MF_01227}.; BINDING 72 72 ATP. {ECO:0000256|HAMAP-Rule:MF_01227}.; BINDING 225 225 Allosteric inhibitor CTP; alternate. {ECO:0000256|HAMAP-Rule:MF_01227}.; BINDING 225 225 UTP; alternate. {ECO:0000256|HAMAP-Rule:MF_01227}.; BINDING 243 243 ATP. {ECO:0000256|HAMAP-Rule:MF_01227}.; BINDING 356 356 L-glutamine; via carbonyl oxygen. {ECO:0000256|HAMAP-Rule:MF_01227}.; BINDING 407 407 L-glutamine. {ECO:0000256|HAMAP-Rule:MF_01227}.; BINDING 462 462 L-glutamine; via amide nitrogen. {ECO:0000256|HAMAP-Rule:MF_01227}.
Calcium binding:
DNA binding:
Metal binding: METAL 72 72 Magnesium. {ECO:0000256|HAMAP-Rule:MF_01227}.; METAL 142 142 Magnesium. {ECO:0000256|HAMAP-Rule:MF_01227}.
Nucleotide binding: NP_BIND 15 20 ATP. {ECO:0000256|HAMAP-Rule:MF_01227}.; NP_BIND 149 151 Allosteric inhibitor CTP. {ECO:0000256|HAMAP-Rule:MF_01227}.; NP_BIND 189 194 Allosteric inhibitor CTP; alternate. {ECO:0000256|HAMAP-Rule:MF_01227}.; NP_BIND 189 194 UTP; alternate. {ECO:0000256|HAMAP-Rule:MF_01227}.
Site:
Gene names (primary): pyrG
Gene names (synonym):
Mass: 60,780
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 294 534 Glutamine amidotransferase type-1. {ECO:0000259|PROSITE:PS51273}.
Motif:
Region: REGION 1 268 Amidoligase domain. {ECO:0000256|HAMAP-Rule:MF_01227}.; REGION 384 387 L-glutamine binding. {ECO:0000256|HAMAP-Rule:MF_01227}.
EMBL: CP000896
ProteinModelPortal: A9NE27
MEROPS: C26.964
EnsemblBacteria KO: ABX81987
UniPathway: K01937
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

1455955-1457566(-)

>nucleotide sequence
TTATTGCTTAATTTTGTTATTTTTAAGAGACATTTCTATAAATCTTCTAAATAACGGGTG
TGGGCGTAGTGGTCTTGATAAAAACTCAGGGTGATATTGTACGCCTACAAACCAAACATG
GTTTTTAAGTTCAATAATTTCCACTAAATTTCGCTCAGGATTTATACCACTAAATATAAA
ATTATTATCGTTAAATAACGCCTTATATTGATTGTTAAATTCATAACGATGTCTATGACG
TTCCTTAATTAGAGCATGCCCATAAGACTTAGATGCAACAGTATTTGGTTCAATCTTACA
ATCATATAAACCTAATCTTAATGTACCACCTAAATCAGTGCCTGGTGCTTCTAGTGTATG
GATAAGTGGCATAGATGTATTCGGATCAATTTCTGTGGTTTCAGCTTCTTTATAACCTAA
TACATTTCTAGCATATTCAATGGTTGCTAGTTGCATACCATAACATATACCAAAGAAGGG
TATGTTATGTTCTCTAGCATACTGAATCGCTAATAGTTTACCTGAGGTTGCTCTTTTACC
AAATCCACCAGGTACTAAAATACCATCACAAGACTCTAAGGTATCTTCATAGTTATCATT
GGTTAGCTTTTCAGCATTTAACCATTTAATTTTAACTTCACAGCGGTGATAAAATCCTGC
GTGTTTTAGTGATTCTGATACAGATAAATATGCATCTTGTAGTGTCACATACTTACCAAC
TAAACCAATCGTAATACGGTGTTGTGGGGTTTTAATACGTTCAATTAAATCTTCCCAAGA
AGACATATCTGGTATAACTTCATTATCTATTTGGAAATGCTTTAAGATATAGTCATCAAT
TTTTTGTTTTCTAAAATTTAAAATAGATTCATATATAACGTTAACATCAAGAGATTCAAA
CACTGCTTCTTTATCAACATCACAAAATAACGCAATCTTTTCCTTTACATCACTACTAAT
ATTTACTTCACTTCTTAATATAATAATATCTGGTTGAATACCAAGTGATCTTAACTCTTT
AACAGAGTGTTGGGTTGGTTTTGTTTTGATCTCATTAGATGCTTTTAAAAAAGGTACTAG
AGTATTATGTATATAAAGCGTGTTTTTATAGCCAAAATCACGTCTTGCTTGACGAATTGC
TTCTAAGTATGGAAGAGATTCAATATCGCCTACTGTGCCGCCAGTTTCAGTGATAATAAC
GTCTGCACCGGATATTTGTGCTGCTTCTTTTAACTTTAATTTGATTTCATCTGTAACATG
AGGAATAACTTGTACAGTTGCACCTAAATAATCCCCTCTACGTTCTTTATTAATAACGTT
TTGATATATCTTACCTGTTGTAATCGAGGATTCCTTTGTCAAATTAATATCAATAAAACG
TTCATAATGCCCTAAATCTAAGTCTGTTTCTGCACCATCATCTGTAACAAAAACCTCTCC
ATGTTGAAAAGGACTCATGGTACCTGGATCCACATTAATATAAGGATCAAACTTTTGGGT
AAACACCTTTAACCCTCTAGATTTTAAAATTTGACCGATTGCAGATGCTGATATACCTTT
ACCTAAAGATGATACAACGCCGCCTGTAACAAATATAAATTTTGTAGCCAT

>protein sequence
MATKFIFVTGGVVSSLGKGISASAIGQILKSRGLKVFTQKFDPYINVDPGTMSPFQHGEV
FVTDDGAETDLDLGHYERFIDINLTKESSITTGKIYQNVINKERRGDYLGATVQVIPHVT
DEIKLKLKEAAQISGADVIITETGGTVGDIESLPYLEAIRQARRDFGYKNTLYIHNTLVP
FLKASNEIKTKPTQHSVKELRSLGIQPDIIILRSEVNISSDVKEKIALFCDVDKEAVFES
LDVNVIYESILNFRKQKIDDYILKHFQIDNEVIPDMSSWEDLIERIKTPQHRITIGLVGK
YVTLQDAYLSVSESLKHAGFYHRCEVKIKWLNAEKLTNDNYEDTLESCDGILVPGGFGKR
ATSGKLLAIQYAREHNIPFFGICYGMQLATIEYARNVLGYKEAETTEIDPNTSMPLIHTL
EAPGTDLGGTLRLGLYDCKIEPNTVASKSYGHALIKERHRHRYEFNNQYKALFNDNNFIF
SGINPERNLVEIIELKNHVWFVGVQYHPEFLSRPLRPHPLFRRFIEMSLKNNKIKQ