A0A954C075 · A0A954C075_UNCPL

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 site144Mg2+ (UniProtKB | ChEBI)
Binding site151-153CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site191-196CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site191-196UTP (UniProtKB | ChEBI)
Binding site227CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site227UTP (UniProtKB | ChEBI)
Binding site243-245ATP (UniProtKB | ChEBI)
Binding site358L-glutamine (UniProtKB | ChEBI)
Active site385Nucleophile
Active site385Nucleophile; for glutamine hydrolysis
Binding site386-389L-glutamine (UniProtKB | ChEBI)
Binding site409L-glutamine (UniProtKB | ChEBI)
Binding site466L-glutamine (UniProtKB | ChEBI)
Active site511
Active site513

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular FunctionATP binding
Molecular FunctionCTP synthase activity
Molecular Functionidentical protein binding
Molecular Functionmetal ion binding
Biological ProcessCTP 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
      KDB32_10390

Organism names

Accessions

  • Primary accession
    A0A954C075

Proteomes

Subcellular Location

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-271Amidoligase domain
Domain7-271CTP synthase N-terminal
Domain306-530Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    539
  • Mass (Da)
    60,002
  • Last updated
    2023-02-22 v1
  • Checksum
    A65C23A278C51A57
MTKHVTKHIIITGGVVSSLGKGLTTACLGALLEARGLKIRIQKFDPYINVDAGTMNPFQHGEVYVTADGGETDLDLGHYERYTTAPLARNSNITSGRIYRDVIAKERKGAYLGGCVQVVPHITNEIKANIRQWDGPDTDVVLSELGGTAGDIEGAAFLEAFRQFAYEHGRENCIFLHLTLIPFLRASGESKTKPTQQSVGILRQIGIQPDMLVCRTERAITQEMRDKIAMFCNVEKKHVFEERDVENTIYELPLVLRREGVDDAIIQRLGLPAGSADLDAWLEVVHTVTNPKETVDIAVVGKYVELKDAYKSVYESIDHAGIANKVEVKIHRINAEDLTDENVSKRLRGMSGILVPGGFGERGIEGKISAVRFARENKVPYYGLCLGMQIAVIDFARNVAGMDDANSSEFSKETKHPVISLLKDQRDVKNMGGTMRLGAQPCKLIEGTIARKAYGEEIVQERHRHRYEFNNDYRSKLQEKGLVVSGVNPELDLVEIVELKDHPFFVGVQFHPEFQSKPLKPHALFTAFVKASVDYGRKQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAGQRG010000224
EMBL· GenBank· DDBJ
MCA8919477.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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