A0A842R8I7 · A0A842R8I7_9ARCH

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 site17CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site17UTP (UniProtKB | ChEBI)
Binding site18-23ATP (UniProtKB | ChEBI)
Binding site75ATP (UniProtKB | ChEBI)
Binding site75Mg2+ (UniProtKB | ChEBI)
Binding site145Mg2+ (UniProtKB | ChEBI)
Binding site152-154CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site192-197CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site192-197UTP (UniProtKB | ChEBI)
Binding site228CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site228UTP (UniProtKB | ChEBI)
Binding site246ATP (UniProtKB | ChEBI)
Binding site359L-glutamine (UniProtKB | ChEBI)
Active site386Nucleophile
Active site386Nucleophile; for glutamine hydrolysis
Binding site387-390L-glutamine (UniProtKB | ChEBI)
Binding site410L-glutamine (UniProtKB | ChEBI)
Binding site471L-glutamine (UniProtKB | ChEBI)
Active site516
Active site518

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular FunctionCTP synthase 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
      GF308_04650

Organism names

Accessions

  • Primary accession
    A0A842R8I7

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-271Amidoligase domain
Domain7-271CTP synthase N-terminal
Domain306-535Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    551
  • Mass (Da)
    61,864
  • Last updated
    2021-09-29 v1
  • Checksum
    1F028F31F71C424D
MTHKKTKFVFVVGGVMSGIGKGIVAASIGKNIQVRKGTVDLVKIDPYLNIDAGTMNPIQHGEVYVSDDGGELDVDFGHYARILGLNLKKSQNITTGQIYREVIRKERAGDYLGETVQVIPHIVDEIKRRVRVVADYNSPDLLLIEIGGTVGDIESQPFLEAIRQMILEEKPEDTLLVHTTFVPVPAHLGEPKTKPTQHSVKELRSIGLMPKIIVCRSHNVLDEQTVKKIALFCNVPKEAVFTLPDLDTVYAAPIKLDEQGFGPLILRELKLDLAPPDWSEWLELMDRYINPRGTVHIAMGGKYTQLVDSYISVNEALGHAGAKFRHNVEITWIETEDIEADKRKANLLDDFDGLIVPGGFGYRGTEGKIAMIRYARENNIPFLGLCFGFQLATIEFTRHVVGIKDATSLEFTMADEVESEHLIIDLLPEQKGVKDLGGTMNLGGQTVLIKEGTLAHKLYGKTTIRERHRHRFEVNPEYIEKIEEKGLVFSGQSKDGRCMEILEYPKHPFFIASQFHPEFTSLPWKPNPLFSGFMDAAITRKNARKNIQYKK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WJIK01000027
EMBL· GenBank· DDBJ
MBD3189906.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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