A0QH68 · PYRG_MYCA1

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.

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 site20CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site20UTP (UniProtKB | ChEBI)
Binding site21-26ATP (UniProtKB | ChEBI)
Binding site78ATP (UniProtKB | ChEBI)
Binding site78Mg2+ (UniProtKB | ChEBI)
Binding site152Mg2+ (UniProtKB | ChEBI)
Binding site159-161CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site199-204CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site199-204UTP (UniProtKB | ChEBI)
Binding site235CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site235UTP (UniProtKB | ChEBI)
Binding site366L-glutamine (UniProtKB | ChEBI)
Active site393Nucleophile; for glutamine hydrolysis
Binding site394-397L-glutamine (UniProtKB | ChEBI)
Binding site416L-glutamine (UniProtKB | ChEBI)
Binding site477L-glutamine (UniProtKB | ChEBI)
Active site524
Active site526

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
      MAV_3072

Organism names

  • Taxonomic identifier
  • Strain
    • 104
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium avium complex (MAC)

Accessions

  • Primary accession
    A0QH68

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10001394921-583CTP synthase

Interaction

Subunit

Homotetramer.

Structure

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-278Amidoligase domain
Domain303-551Glutamine amidotransferase type-1
Region560-583Disordered

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    583
  • Mass (Da)
    63,142
  • Last updated
    2007-01-09 v1
  • Checksum
    8BCA048A64D906B9
MRKHPQTATKHLFVSGGVASSLGKGLTASSLGQLLTARGLYVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDVGHYERFLDRDLSGSANVTTGQVYSTVIAKERRGEYLGDTVQVIPHITDEIKGRILAMAQPDAQGNRPDVVITEIGGTVGDIESQPFLEAARQVRHDLGRENVFFLHVSLVPYLAPSGELKTKPTQHSVAALRSIGITPDALILRCDRDVPEALKNKIALMCDVDIDGVISTPDAPSIYDIPKVLHREELDAYVVRRLNLPFRDVDWTEWDDLLRRVHEPHETVRIALVGKYVELSDAYLSVTEALRAGGFFHHAKVEMVWVASDDCESASGAAAALGEVHGVLIPGGFGIRGIEGKIGAIHYARTRGLPVLGLCLGLQCIVIEAARAAGLAGANSAEFDPDTPDPVISTMADQVDIVAGAADLGGTMRLGAYPAVLEEDSIVARAYGTTQVSERHRHRYEVNNAYRDKIAESGLRFSGTSPDGHLVEFVEYPPDVHPFIVGTQAHPELKSRPTRPHPLFVAFVGAAMDYKAGELLPVEIPEQSSNGIQHRDSAARPIPEPAARG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000479
EMBL· GenBank· DDBJ
ABK64418.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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