A0A926MC78 · A0A926MC78_9PROT

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 site12CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site12UTP (UniProtKB | ChEBI)
Binding site13-18ATP (UniProtKB | ChEBI)
Binding site53L-glutamine (UniProtKB | ChEBI)
Binding site70ATP (UniProtKB | ChEBI)
Binding site70Mg2+ (UniProtKB | ChEBI)
Binding site138Mg2+ (UniProtKB | ChEBI)
Binding site145-147CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site184-189CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site184-189UTP (UniProtKB | ChEBI)
Binding site220CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site220UTP (UniProtKB | ChEBI)
Binding site238ATP (UniProtKB | ChEBI)
Binding site352L-glutamine (UniProtKB | ChEBI)
Active site379Nucleophile
Active site379Nucleophile; for glutamine hydrolysis
Binding site380-383L-glutamine (UniProtKB | ChEBI)
Binding site403L-glutamine (UniProtKB | ChEBI)
Binding site468L-glutamine (UniProtKB | ChEBI)
Active site513
Active site515

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular FunctionCTP synthase activity
Molecular Functionmetal ion binding
Biological ProcessCTP 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
      IDH28_02490

Organism names

Accessions

  • Primary accession
    A0A926MC78

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-263Amidoligase domain
Domain2-261CTP synthase N-terminal
Domain300-532Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    536
  • Mass (Da)
    60,253
  • Last updated
    2023-02-22 v1
  • Checksum
    56D61F17A2EBD5EF
MQYVFITGGVASSLGKGIASASVASLLQQRNFKVRIRKLDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFTNRSAKKTDSTSSGKIYSNVLKKERKGDYLGATIQVIPHVTDEIKLFINSNFEDEDIIIYEIGGTVGDIESLPFLEAIRQIRNDKKITSALIHMTYVPYLSSAGELKTKPTQHSVKELLNSGIQPDIIMCRCEKEINLESLEKISQFCNVKKDSVIPALNAKSIYEVPSIYSHAGLDRVLLEHLGYQASNYPLNLKAWENLTKKINDLKKEVTIGVVGKYTNLKDSYKSLIEALTHGGIENNTIVKINWINAEKINTTELFEELKCVDGILIPGGFGYRGVEGKILAIKYARENNIPFFGICLGMQLSVIEIARNVFGLLDSNSTEFQSSGNPVVSLITEWSNERSIEKRDKTSDKGGTMRLGAYKALLKKGSKVEEIYNTNEIFERHRHRYEVDLNYTKGFNDKGFYFSGMSPDNVLPEVLESTNHKWFIGVQFHPELKSRPLAPHPLFSSFIKHCLK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACWEB010000007
EMBL· GenBank· DDBJ
MBD1147683.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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