A0A1R4GSK1 · A0A1R4GSK1_9GAMM

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 site140Mg2+ (UniProtKB | ChEBI)
Binding site147-149CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site187-192CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site187-192UTP (UniProtKB | ChEBI)
Binding site223CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site223UTP (UniProtKB | ChEBI)
Binding site241ATP (UniProtKB | ChEBI)
Binding site354L-glutamine (UniProtKB | ChEBI)
Active site381Nucleophile
Active site381Nucleophile; for glutamine hydrolysis
Binding site382-385L-glutamine (UniProtKB | ChEBI)
Binding site404L-glutamine (UniProtKB | ChEBI)
Binding site471L-glutamine (UniProtKB | ChEBI)
Active site516
Active site518

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular FunctionATP binding
Molecular FunctionCTP synthase activity
Molecular Functionglutaminase activity
Molecular Functionidentical protein binding
Molecular Functionmetal ion binding
Biological Process'de novo' CTP biosynthetic process
Biological Processglutamine metabolic process
Biological Processpyrimidine nucleobase biosynthetic 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
      A1232T_01153

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Psychrobacter_piechaudii
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Moraxellales > Moraxellaceae > Psychrobacter

Accessions

  • Primary accession
    A0A1R4GSK1

Proteomes

Subcellular Location

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-266Amidoligase domain
Domain3-265CTP synthase N-terminal
Domain301-535Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    542
  • Mass (Da)
    60,368
  • Last updated
    2017-04-12 v1
  • Checksum
    DB286D3F624884D6
MTKFIFVTGGVVSSLGKGITAASLAAVLEARGLKVTMTKMDPYINVDPGTMSPFQHGEVFVTEDGAETDLDLGYYERFLRHSKMSKTNNFTSGRIYQTVLNKERRGDYLGGTVQVIPHITDEIKHRIHASGEGHDIAIIEIGGTVGDIESLPFMEAVRQMQVELGRNRAMLMHLTLVPYISSAGETKTKPTQHSVKELRSIGLQPDVLICRSEHAIGEDNRRKIALFTNVEERAVILCEDADSIYQIPRTLHEQDLDDIILERFGIEAPEADLSDWDKVVDRLLNAEGKVTVAIVGKYVELPDAYKSINEALLHAGITHKTKVEIDYVDAEALETDDSLVQQLEQADAILVPGGFGERGKLGKMRAITYARENNIPFLGICLGMQLAVIEFATNKLGLRADSTEFDRQAEEPIIGLITEWLDEKGELQVRNDDSDLGGTMRLGSQKAELVEGSKLHQIYGSKIITERHRHRYEMNNRYIEPLEEAGMSISGYSAKQHLVESVEIADHPWFIGVQFHPEFTSSPRTGHPLFASFIEAAIKNQK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FUGE01000123
EMBL· GenBank· DDBJ
SJM71166.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp