A0A4P6TWE0 · A0A4P6TWE0_STRSO

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 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 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
      D0Z67_05760

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • KCTC 9819
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces

Accessions

  • Primary accession
    A0A4P6TWE0

Proteomes

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    555
  • Mass (Da)
    60,781
  • Last updated
    2019-07-31 v1
  • Checksum
    B019F6F3E0F79816
MPPKSTTTKHIFVTGGVASSLGKGLTASSLGMLLKARGLRVVMQKLDPYLNVDPGTMNPFQHGEVFVTNDGAETDLDIGHYERFLDRDLDGSANVTTGQVYSTVIAKERRGEYLGDTVQVIPHITNEIKHRIRRMATDEVDVVITEVGGTVGDIESLPFLETVRQVRHEVGRDNVFVVHISLLPYIGPSGELKTKPTQHSVAALRNIGIQPDAIVLRCDREVPTAIKRKISLMCDVDEDAVVACPDARSIYDIPKVIHGEGLDAYVVRKLDLPFRDVDWTTWDDLLDRVHKPDHEITLALVGKYIDLPDAYLSVTEALRAGGFANRARVKIKWVTSDDCKTPAGAAAALGDVDGICIPGGFGDRGVLGKVGAIRYARENKIPLLGLCLGLQCIVVEAARNLADIPDANSTEFDPATGHPVISTMAEQMDIVAGEGDMGGTMRLGMYPAKLAEGSIVREVYDGKEYVEERHRHRYEVNNSYRAELEKKAGIVFSGTSPDGKLVEYVEYPREVHPYLVATQAHPELRSRPTRPHPLFAGLVKASVERKTAGKPKNSK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP032229
EMBL· GenBank· DDBJ
QBJ89858.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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