A0AAJ2QKR5 · A0AAJ2QKR5_9ACTN

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 site19CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site19UTP (UniProtKB | ChEBI)
Binding site20-25ATP (UniProtKB | ChEBI)
Binding site77ATP (UniProtKB | ChEBI)
Binding site77Mg2+ (UniProtKB | ChEBI)
Binding site146Mg2+ (UniProtKB | ChEBI)
Binding site153-155CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site193-198CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site193-198UTP (UniProtKB | ChEBI)
Binding site229CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site229UTP (UniProtKB | ChEBI)
Binding site247ATP (UniProtKB | ChEBI)
Binding site360L-glutamine (UniProtKB | ChEBI)
Active site387Nucleophile
Active site387Nucleophile; for glutamine hydrolysis
Binding site388-391L-glutamine (UniProtKB | ChEBI)
Binding site411L-glutamine (UniProtKB | ChEBI)
Binding site473L-glutamine (UniProtKB | ChEBI)
Active site521
Active site523

GO annotations

AspectTerm
Molecular Functionligase activity

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
      PV387_14215

Organism names

  • Taxonomic identifier
  • Strain
    • ME02-6987-2C
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces

Accessions

  • Primary accession
    A0AAJ2QKR5

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-272Amidoligase domain
Domain9-272CTP synthase N-terminal
Domain307-540Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    549
  • Mass (Da)
    60,103
  • Last updated
    2024-07-24 v1
  • Checksum
    43419C4AEF67B146
MPPKSSTTKHIFVTGGVASSLGKGLTASSLGMLLKARGLRVVMQKLDPYLNVDPGTMNPFQHGEVFVTNDGAETDLDIGHYERFLDRDLDGSANVTTGQVYSTVIAKERRGEYLGDTVQVIPHITNEIKHRIRRMATDEVDVVITEVGGTVGDIESLPFLETVRQVRHEVGRDNVFVVHISLLPYIGPSGELKTKPTQHSVAALRNIGIQPDAIVLRCDREVPTAIKRKISLMCDVDEAAVVACPDARSIYDIPKVIHTEGLDAYVVRRMDLPFRDVDWTTWDDLLDRVHNPEHEIVMALVGKYIDLPDAYLSVTEALRAGGFANKARVKIKWVTSDDCKTPAGARAQLGDVDAICIPGGFGERGVTGKVGAIQYARENGIPLLGLCLGLQCIVVEAARNLAGVADANSTEFDPATAHPVVSTMAEQLDIVAGEGDMGGTMRLGMYPAKLAEGSIVREVYDGKEYVEERHRHRYEVNNAYRAELEKKAGIVFSGTSPDGKLVEYVEYPRDVHPYLVATQAHPELRSRPTRPHPLFAGLVKAAVERKTSK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JARAXU010000063
EMBL· GenBank· DDBJ
MDX3367178.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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