A0A078RVN0 · A0A078RVN0_BACUN

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 site15CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site15UTP (UniProtKB | ChEBI)
Binding site16-21ATP (UniProtKB | ChEBI)
Binding site56L-glutamine (UniProtKB | ChEBI)
Binding site73ATP (UniProtKB | ChEBI)
Binding site73Mg2+ (UniProtKB | ChEBI)
Binding site143Mg2+ (UniProtKB | ChEBI)
Binding site150-152CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site189-194CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site189-194UTP (UniProtKB | ChEBI)
Binding site225CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site225UTP (UniProtKB | ChEBI)
Binding site243ATP (UniProtKB | ChEBI)
Binding site357L-glutamine (UniProtKB | ChEBI)
Active site384Nucleophile
Active site384Nucleophile; for glutamine hydrolysis
Binding site385-388L-glutamine (UniProtKB | ChEBI)
Binding site408L-glutamine (UniProtKB | ChEBI)
Binding site465L-glutamine (UniProtKB | ChEBI)
Active site510
Active site512

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
      M094_2251

Organism names

Accessions

  • Primary accession
    A0A078RVN0

Proteomes

Subcellular Location

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-268Amidoligase domain
Domain5-268CTP synthase N-terminal
Domain305-529Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    539
  • Mass (Da)
    59,890
  • Last updated
    2014-10-29 v1
  • Checksum
    6B6807AA18FA4DD8
MGETKYIFVTGGVASSLGKGIISSSIGKLLQARGYKVTIQKFDPYINIDPGTLNPYEHGECYVTVDGHEADLDLGHYERFLGIQTTKANNITTGRIYKSVIDKERRGDYLGKTIQVIPHITDEIKRNVKLLGNKYKFDFVITEIGGTVGDIESLPYLESIRQLKWELGKDALCVHLTYVPYLAAAGELKTKPTQHSVKELQSAGIQPDVLVLRTEHELSTTLRKKVALFCNVDENAVVQSIDAPTIYEVPILMQSQGLDVTILKKMGLPVGDTPGLGPWRAFLERRHKAEETAPLHIALVGKYDLQDAYKSIREALSQAGTYNDRKVSVDFVNSEKLTDENVAEALKGMAGGLIGPGFGERGVAGKFVAIKYARTHDIPTFGICLGMQCIAIEFARNVLGYADANSREMDEKTPHNVIDIMEEQKSITNMGGTMRLGAYECVLQKGSKAYEAYGTEHIQERHRHRYEFNNSFKEAYEAAGMKCVGINPESDLVEIVEIPALKWFVGTQFHPEYSSTVLHPHPLFVAFVKAAIENENEKK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JNHN01000179
EMBL· GenBank· DDBJ
KDS48565.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp