H6R103 · H6R103_NOCCG

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.

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 site45ATP (UniProtKB | ChEBI)
Binding site45Mg2+ (UniProtKB | ChEBI)
Binding site119Mg2+ (UniProtKB | ChEBI)
Binding site126-128CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site166-171CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site166-171UTP (UniProtKB | ChEBI)
Binding site202CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site202UTP (UniProtKB | ChEBI)
Binding site220ATP (UniProtKB | ChEBI)
Binding site333L-glutamine (UniProtKB | ChEBI)
Active site360Nucleophile
Active site360Nucleophile; for glutamine hydrolysis
Binding site361-364L-glutamine (UniProtKB | ChEBI)
Binding site383L-glutamine (UniProtKB | ChEBI)
Binding site444L-glutamine (UniProtKB | ChEBI)
Active site491
Active site493

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular FunctionCTP synthase activity
Molecular Functionglutaminase activity
Molecular Functionmetal ion binding
Biological Process'de novo' CTP 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
    • Ordered locus names
      NOCYR_2197

Organism names

Accessions

  • Primary accession
    H6R103

Proteomes

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain1-245CTP synthase N-terminal
Region1-245Amidoligase domain
Domain280-509Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    538
  • Mass (Da)
    58,527
  • Last updated
    2012-04-18 v1
  • Checksum
    FC57470CE3739C56
MLTARGLRVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDVGHYERFLDRDLSRDANVTTGQIYSSVIAKERRGEYLGDTVQVIPHITDEIKARILAMRGPDLQGQEPDVVITEIGGTVGDIESQPFLEAARQIRHDVGRDNVFFLHVSLVPYLAPSGELKTKPTQHSVAALRNIGIQPDALILRCDREVPQSLKSKIALMCDVEVDACISTPDAPSIYDIPKVLHREGLDAYVVRKLGLPFRDVDWTVWGDLLDRVHSPRETVEVALVGKYVDLPDAYLSVTEALRAGGFASRAKVQIRWVQSDDCETPAGAQAALRDVDAVLIPGGFGIRGIEGKVGAIRYARTRGLPLLGLCLGLQCMVIEAARSVGLTDANSAEFEPDTTHPVISTMADQEQAVAGEADLGGTMRLGAYPAVLAKGSVVAQAYGATEVSERHRHRYEVNNAYRDKIAKSGLKFSGTSPDGHLVEFVELPADKHPFFVATQAHPELKSRPTRPHPLFAALIAAALKYKAAERLPVDIPGEELANAGDQAS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FO082843
EMBL· GenBank· DDBJ
CCF62975.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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