A0A0M0F768 · A0A0M0F768_CELCE

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.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 site34CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site34UTP (UniProtKB | ChEBI)
Binding site35-40ATP (UniProtKB | ChEBI)
Binding site92ATP (UniProtKB | ChEBI)
Binding site92Mg2+ (UniProtKB | ChEBI)
Binding site161Mg2+ (UniProtKB | ChEBI)
Binding site168-170CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site208-213CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site208-213UTP (UniProtKB | ChEBI)
Binding site244CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site244UTP (UniProtKB | ChEBI)
Binding site262ATP (UniProtKB | ChEBI)
Binding site375L-glutamine (UniProtKB | ChEBI)
Active site402Nucleophile
Active site402Nucleophile; for glutamine hydrolysis
Binding site403-406L-glutamine (UniProtKB | ChEBI)
Binding site426L-glutamine (UniProtKB | ChEBI)
Binding site487L-glutamine (UniProtKB | ChEBI)
Active site534
Active site536

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
      M768_20815

Organism names

Accessions

  • Primary accession
    A0A0M0F768

Proteomes

Subcellular Location

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-20Disordered
Region1-287Amidoligase domain
Domain25-287CTP synthase N-terminal
Domain322-552Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    561
  • Mass (Da)
    60,951
  • Last updated
    2015-11-11 v1
  • Checksum
    B542B7AC7ED99B0D
MADLLNRPSSRLNASGARTEHRTAHVFVTGGVASSLGKGLTASSLGRLLRSRGLRVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDIGHYERFLDVDLEATANVTTGQVYSQVIARERRGEYLGDTVQVIPHITDEIKSRMRAQAGEDVDVIITEIGGTVGDIESQPFLEAARQVRHELGRDDVFFLHVSLVPYIGPSGELKTKPTQHSVAALRSIGIQPDAIVLRADRVVPEPVKRKIALMCDVDNEAVVNAVDAPSIYDIPRVLHSEGLDAYVVRRLGLPFHDVDWDGWSQLLERVHQPAHRVEVALVGKYIDLPDAYLSVTEALRAGGFANDAKVTIRWVASDECQTPEGADDALHGVDAVLVPGGFGVRGIEGKLGALRWARENKVPTLGICLGLQSMVIEYARNVLGIDDASSTEFDPGTSHPVIATMEEQLAIVGGDGDLGGTMRLGSYEAALAPGSVVAKTYGSERVSERHRHRYEVNNSYRKQLEEAGLVISGTSPDSSLVEFVELPADVHPYYVSTQAHPEFKSRPTRSHPLFTGLIGAALENQAD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ATNL01000010
EMBL· GenBank· DDBJ
KON73031.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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