A0A229GIM5 · A0A229GIM5_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.

Type
IDPosition(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 site148Mg2+ (UniProtKB | ChEBI)
Binding site155-157CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site195-200CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site195-200UTP (UniProtKB | ChEBI)
Binding site231CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site231UTP (UniProtKB | ChEBI)
Binding site249ATP (UniProtKB | ChEBI)
Binding site362L-glutamine (UniProtKB | ChEBI)
Active site389Nucleophile
Active site389Nucleophile; for glutamine hydrolysis
Binding site390-393L-glutamine (UniProtKB | ChEBI)
Binding site413L-glutamine (UniProtKB | ChEBI)
Binding site475L-glutamine (UniProtKB | ChEBI)
Active site523
Active site525

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
      B7755_47550

Organism names

  • Taxonomic identifier
  • Strain
    • NBS 14/10
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces

Accessions

  • Primary accession
    A0A229GIM5

Subcellular Location

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-274Amidoligase domain
Domain11-274CTP synthase N-terminal
Domain309-542Glutamine amidotransferase
Region548-589Disordered

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    589
  • Mass (Da)
    63,522
  • Last updated
    2017-10-25 v1
  • Checksum
    7F52C5CB4ECF0BD3
MAIAAKPTTTKHIFVTGGVASSLGKGLTASSLGALLKARGLRVTMQKLDPYLNVDPGTMNPFQHGEVFVTNDGAETDLDIGHYERFLDVDLDGSANVTTGQVYSTVIAKERRGEYLGDTVQVIPHITNEIKHRIRRMATDDVDVVITEVGGTVGDIESLPFLESVRQVRHEVGRDNVFVVHISLLPYIGPSGELKTKPTQHSVAALRNIGIQPDAIVLRADREVPTSIKRKVSLMCDVDEAAVVAAIDAKSIYDIPKVLHSEGLDAYVVRRLDLPFRDVEWTQWDDLLKRVHQPDHEVTVALVGKYIDLPDAYLSVTEALRAGGFANNARVKIKWVTSDDCRTAAGARQQLGDVDAVCVPGGFGDRGVNGKVGAITYARENKIPLLGLCLGLQCIVIEASRNLAGIEGANSTEFEPATSDPVISTMAEQLDIVAGEGDMGGTMRLGMYPAKLGEGTIVREVYGDQPYVEERHRHRYEVNNAYRGELEKKAGLLFSGTSPDNKLVEYVEYPREVHPYLVGTQAHPELRSRPTRPHPLFAGLVKAAVARQSAQSGQPEAQAAQAAPAARSGAEAAAVAGQPGAPSGQRAKA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NCSM01000066
EMBL· GenBank· DDBJ
OXL23529.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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