A0A1I5XNZ1 · A0A1I5XNZ1_9PSED

Function

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.

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Activity 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.

Pathway

Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site13CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site13UTP (UniProtKB | ChEBI)
Binding site14-19ATP (UniProtKB | ChEBI)
Binding site71ATP (UniProtKB | ChEBI)
Binding site71Mg2+ (UniProtKB | ChEBI)
Binding site139Mg2+ (UniProtKB | ChEBI)
Binding site146-148CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site186-191CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site186-191UTP (UniProtKB | ChEBI)
Binding site222CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site222UTP (UniProtKB | ChEBI)
Binding site240ATP (UniProtKB | ChEBI)
Binding site351L-glutamine (UniProtKB | ChEBI)
Active site378Nucleophile
Active site378Nucleophile; for glutamine hydrolysis
Binding site379-382L-glutamine (UniProtKB | ChEBI)
Binding site402L-glutamine (UniProtKB | ChEBI)
Binding site469L-glutamine (UniProtKB | ChEBI)
Active site514
Active site516

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular FunctionCTP synthase activity
Molecular Functionmetal ion binding
Biological Process'de novo' CTP biosynthetic process
Biological Processglutamine metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    CTP synthase
  • EC number
  • Alternative names
    • Cytidine 5'-triphosphate synthase
    • Cytidine triphosphate synthetase
      (CTP synthetase
      ; CTPS
      )
    • UTP--ammonia ligase

Gene names

    • Name
      pyrG
    • ORF names
      CDR19_16795
      , N5D41_13380
      , SAMN05216177_111101

Organism names

  • Taxonomic identifier
  • Strains
    • DSM 26169
    • JCM 15604
    • GD03863
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas

Accessions

  • Primary accession
    A0A1I5XNZ1

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-265Amidoligase domain
Domain3-265CTP synthase N-terminal
Domain300-533Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    543
  • Mass (Da)
    59,554
  • Last updated
    2017-04-12 v1
  • Checksum
    A5578F77610E50C4
MTRYIFVTGGVVSSLGKGIASASLAAILEARGLKVTMLKLDPYINVDPGTMSPFQHGEVFVTHDGAETDLDLGHYERFIRTTMTKSNNFTTGRVYEDVLRKERRGDYLGATIQVIPHITDEIKRRIIKGAGDADVALVEIGGTVGDIESQPFLEAIRQLRVEVGAKRAMLMHLTLVPYIATAGETKTKPTQHSVKELRSIGLQPDVLVCRSDHPIDVSSRRKIALFTNVEERAVISLEDVDTIYKIPGVLHAQGLDDFVVERFGLECGGADLSEWDRVVDAKLNPEKEVTIAMVGKYMELLDAYKSLIEAMSHAGIQNRTKVNLRYIDSEDIENQGTALLEGVDAILVPGGFGLRGVEGKIKTVQYARENKIPYLGICLGMQVAVIEYARNVVGWTDANSSEFDMASTHPVVGLITEWQDATGATEQRSESSDLGGTMRLGAQDCQLQAGSLVHDCYGKDVIVERHRHRYEVNNNLLPQLTEAGLKVTGRSGDGALVEVVEAPNHPWFVACQFHPEFTSTPRDGHPLFSGFVNAALAQKAKKV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAOCDH010000014
EMBL· GenBank· DDBJ
MDH0702472.1
EMBL· GenBank· DDBJ
Genomic DNA
NIQV01000010
EMBL· GenBank· DDBJ
PIA70360.1
EMBL· GenBank· DDBJ
Genomic DNA
FOXK01000011
EMBL· GenBank· DDBJ
SFQ33654.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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