M1TR01 · M1TR01_9CORY

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 site21CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site21UTP (UniProtKB | ChEBI)
Binding site22-27ATP (UniProtKB | ChEBI)
Binding site79ATP (UniProtKB | ChEBI)
Binding site79Mg2+ (UniProtKB | ChEBI)
Binding site153Mg2+ (UniProtKB | ChEBI)
Binding site160-162CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site200-205CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site200-205UTP (UniProtKB | ChEBI)
Binding site236CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site236UTP (UniProtKB | ChEBI)
Binding site367L-glutamine (UniProtKB | ChEBI)
Active site394Nucleophile
Active site394Nucleophile; for glutamine hydrolysis
Binding site395-398L-glutamine (UniProtKB | ChEBI)
Binding site417L-glutamine (UniProtKB | ChEBI)
Binding site478L-glutamine (UniProtKB | ChEBI)
Active site526
Active site528

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
    • ORF names
      H924_06535

Organism names

Accessions

  • Primary accession
    M1TR01

Proteomes

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-279Amidoligase domain
Domain11-279CTP synthase N-terminal
Domain314-545Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    554
  • Mass (Da)
    60,622
  • Last updated
    2013-05-01 v1
  • Checksum
    905E05828016F5D4
MTSPRNTRTTKHIFVTGGVVSSLGKGLTAASLGQLLIARGLSVTMQKLDPYLNVDPGTMNPFEHGEVFVTEDGAETDLDLGHYERFLDRNLTLNANVTTGKVYSTVIAKERRGEYLGKTVQVIPHITDEIKARILAMGAPDANGNVPDVVISEVGGTVGDIESQPFLEAARQVRHEIGRDNCFFIHCSLVPYLATSGELKTKPTQHSVSELRGIGILPDALVLRCDREVPQGLKDKIAMMCDVENEGVVSCPDSNSIYNIPDVLYREHLDTFIIRRLGLPFRDVDWTSWHNLIDRVNNPKHEINVGIVGKYIDLPDAYLSVVEAVRAAGYANWTRTNIKWIASDDCETPAGAKRALQNVDAVVIPGGFGIRGIEGKIGAITYARENKVPLLGLCLGLQCTVIEAARQAGLENASSTEFDPEAEQPVIATMEEQKAAVSGEADLGGTMRLGAYPATLREDSLVAELYGTTEVSERHRHRYEVNNAYRGQIEEGSDLIFSGTSPDGQLVEFVEYPKDVHPFLVATQAHPEYKSRPTHAHPLFVGLVKTALELSQRA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP004354
EMBL· GenBank· DDBJ
AGG66751.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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