A0A1I5DD41 · A0A1I5DD41_9FLAO

  • Protein
    CTP synthase
  • Gene
    pyrG
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.

Type
IDPosition(s)Description
Binding site16CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site16UTP (UniProtKB | ChEBI)
Binding site17-22ATP (UniProtKB | ChEBI)
Binding site57L-glutamine (UniProtKB | ChEBI)
Binding site74ATP (UniProtKB | ChEBI)
Binding site74Mg2+ (UniProtKB | ChEBI)
Binding site144Mg2+ (UniProtKB | ChEBI)
Binding site151-153CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site191-196CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site191-196UTP (UniProtKB | ChEBI)
Binding site227CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site227UTP (UniProtKB | ChEBI)
Binding site245ATP (UniProtKB | ChEBI)
Binding site357L-glutamine (UniProtKB | ChEBI)
Active site384Nucleophile
Active site384Nucleophile; for glutamine hydrolysis
Binding site385-388L-glutamine (UniProtKB | ChEBI)
Binding site408L-glutamine (UniProtKB | ChEBI)
Binding site465L-glutamine (UniProtKB | ChEBI)
Active site510
Active site512

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
      SAMN04487989_107132

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DSM 23925
  • Taxonomic lineage
    Bacteria > Bacteroidota > Flavobacteriia > Flavobacteriales > Flavobacteriaceae > Bizionia

Accessions

  • Primary accession
    A0A1I5DD41

Proteomes

Subcellular Location

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-270Amidoligase domain
Domain6-270CTP synthase N-terminal
Domain305-529Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    544
  • Mass (Da)
    60,718
  • Last updated
    2017-11-22 v1
  • Checksum
    CCBF8372D1973AD1
MTTTTKYIFVTGGVTSSLGKGIIAASLAKLLQAQGYRTTIQKLDPYINVDPGTLNPYEHGECYVTDDGAETDLDLGHYERFLNVPTSQANNVTTGRIYQSVIDKERRGEFLGKTVQVIPHITDEIKERVQKLGNSGDYDIVITEIGGTVGDIESLPYIEAVRQLRWDLGDNNGLVIHLTLVPYLSAAGELKTKPTQHSVKTLMESGVMADILVCRTEHELPMDLRKKLALFCNVREEAVIQSIDASTIYDVPNLMLKQGLDTVVLKKLGLQSHQPNLTRWNEFLKRHKNPKTEVTIGLIGKYVELQDSYKSILEAFIHAGAENEVKVHVEPIHSEYLNADNIHAKLSHLNGILVAPGFGERGIEGKIDAVKYVRENKMPFFGICLGMQMAVIEFARNVLNLKDANSTEMDAKTANPVIGLMESQKDITEKGGTMRLGSWSCNLKPNSIAHKVYKSNTIEERHRHRFEFNNTYKDQIEASGMIATGINPETNLVEIVEVSDHPWFVGVQYHPEYKSTVANPHPLFVAFVKAALKHKNKNKRATMA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FOVN01000007
EMBL· GenBank· DDBJ
SFN96711.1
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.
Help