A0A2W6TXC4 · A0A2W6TXC4_ACTSX

  • 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.
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 site27CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site27UTP (UniProtKB | ChEBI)
Binding site28-33ATP (UniProtKB | ChEBI)
Binding site85ATP (UniProtKB | ChEBI)
Binding site85Mg2+ (UniProtKB | ChEBI)
Binding site159Mg2+ (UniProtKB | ChEBI)
Binding site166-168CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site206-211CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site206-211UTP (UniProtKB | ChEBI)
Binding site242CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site242UTP (UniProtKB | ChEBI)
Binding site258-260ATP (UniProtKB | ChEBI)
Binding site373L-glutamine (UniProtKB | ChEBI)
Active site400Nucleophile
Active site400Nucleophile; for glutamine hydrolysis
Binding site401-404L-glutamine (UniProtKB | ChEBI)
Binding site424L-glutamine (UniProtKB | ChEBI)
Binding site485L-glutamine (UniProtKB | ChEBI)
Active site532
Active site534

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
      DI576_15280

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • S2_006_000_R1_54
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Actinomycetales > Actinomycetaceae > Actinomyces

Accessions

  • Primary accession
    A0A2W6TXC4

Proteomes

Subcellular Location

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-285Amidoligase domain
Domain17-285CTP synthase N-terminal
Domain320-551Glutamine amidotransferase
Region562-590Disordered

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    590
  • Mass (Da)
    63,508
  • Last updated
    2018-09-12 v1
  • Checksum
    4B3E0B1A90C9CE4E
MSPNRTRPSGSPPDAPRHIFVTGGVVSSLGKGLTASSLGRLLRARGLDVVMQKLDPYINVDPGTMNPFQHGEVFVTEDGAETDLDIGHYERFLDVDLTGAANATTGQVYSAVIAKERRGEYLGDTVQVIPHVTDEIKRVMRAQAAPGAGGGAPDVIITEIGGTVGDIESQPFLEAARQVRADLGRENVAFVHVSLIPFLSAAGELKTKPTQHSVAALRSIGIQPDALVLRTDRPLPEGVKSKVALMCDVDASAVIECKDAASIYEVPPTLHREGLDAFLVQRLALPFRDVDWTEWNGLLDRVHNPRYRVEVALVGKYVDLHDAYLSVSEAIRHGGFAGNARVDIRWVASDACETRQGAQRALAGVDAVVVPGGFGVRGIEGKLGALRWAREHRVPTLGLCLGLQCMVIEAARNLLALPAASSTEMEPETPDPVVTTMDSQRQFVTGGGDLGGTMRLGACPAVLAPGSIVAEAYGATEVSERHRHRFEVNNAYRERLASVGLRVTGTSPDGHLVELVELDRELHPYYVGTQAHPELKSRPTRAHPLFTGLIRAGLERRRDLYASHRLDGPRTGEAGNDREQGGRGSEPRSA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QFPC01000377
EMBL· GenBank· DDBJ
PZU28537.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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