A0A432F018 · A0A432F018_UNCVE

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.

Type
IDPosition(s)Description
Binding site12CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site12UTP (UniProtKB | ChEBI)
Binding site13-18ATP (UniProtKB | ChEBI)
Binding site70ATP (UniProtKB | ChEBI)
Binding site70Mg2+ (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 site405L-glutamine (UniProtKB | ChEBI)
Binding site462L-glutamine (UniProtKB | ChEBI)
Active site507
Active site509

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
      DSZ35_09615

Organism names

Accessions

  • Primary accession
    A0A432F018

Proteomes

Subcellular Location

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-267Amidoligase domain
Domain2-267CTP synthase N-terminal
Domain302-526Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    537
  • Mass (Da)
    59,197
  • Last updated
    2019-05-08 v1
  • Checksum
    ADA852C0E1E9A4A3
MKHIFVTGGVVSSLGKGLTAASIGTLLENRGLKVTLQKFDPYLNVDPGTMSPFQHGEVYVLDDGAETDLDLGHYERFTGTKLTRFNNLTSGQVYQSVLDKERRGDYLGKTVQVIPHVTDEIQNRIREIGDKTGADVVITEIGGTIGDIEGLPFVEAIREFALGAGRGNVLFLHVTFVPFIKAAGELKTKPTQQGVAKLREIGITPDVLVCRCEKSLTKELRQKLSLFCNVPYEAVIEEIDVEHSIYEVPLMLQREGLDDLICERLGLKTKPADMAHWREIIRKLITPRHRVRIGVVGKYVELQDAYKSVYEAVIHGGVANDCGVEIERVDAEDIEENGAANALKGCSGILVPGGFGERGTEGKILAARFARENNIPYLGLCLGMQIATIEFARNVLKLEGAHSAEFDPGTAHPVIALLDEQQNVTDKGGTMRLGSQPCILKPDSLVTRLYGAEEIHERHRHRYEFNNAYREPFEAAGMMFSGTSPDGNLVEIVELTEHPFYVASQFHPEFKSKPNKPHPLFSGFIAAAHACDHAKTV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QOAX01000264
EMBL· GenBank· DDBJ
RTZ64864.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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