Q8TKW5 · PYRG_METAC

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.

Type
IDPosition(s)Description
Binding site12CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site12UTP (UniProtKB | ChEBI)
Binding site13-18ATP (UniProtKB | ChEBI)
Binding site53L-glutamine (UniProtKB | ChEBI)
Binding site70ATP (UniProtKB | ChEBI)
Binding site70Mg2+ (UniProtKB | ChEBI)
Binding site140Mg2+ (UniProtKB | ChEBI)
Binding site147-149CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site186-191CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site186-191UTP (UniProtKB | ChEBI)
Binding site222CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site222UTP (UniProtKB | ChEBI)
Binding site352L-glutamine (UniProtKB | ChEBI)
Active site379Nucleophile; for glutamine hydrolysis
Binding site380-383L-glutamine (UniProtKB | ChEBI)
Binding site403L-glutamine (UniProtKB | ChEBI)
Binding site460L-glutamine (UniProtKB | ChEBI)
Active site503
Active site505

GO annotations

AspectTerm
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 ProcessCTP 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
    • Ordered locus names
      MA_3279

Organism names

Accessions

  • Primary accession
    Q8TKW5

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001382591-534CTP synthase

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-265Amidoligase domain
Domain289-530Glutamine amidotransferase type-1

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    534
  • Mass (Da)
    59,730
  • Last updated
    2002-06-01 v1
  • Checksum
    2AC6AE3C578072DB
MKYIVVTGGVMSGLGKGITIASIGRNLKNKGYKVTAIKIDPYINIDAGTMSPYQHGEVFVLRDGGEVDLDLGNYERFLDTELTRDHNLTTGKIYQEVIAKERRGDYLGKTVQIIPHITNEIKSRIRKVAARSGADVCLVEIGGTVGDIESMPFLEAVRQMHREEPSENIVFIHVTLVMEDLQGEQKTKPSQHSVKELRALGLSPEVIVTRSKTPLQESAKEKIALFCDVPQELVISAHDAADIYEVPLEIEEQGLTTRLMKHLKLESSVEDNGWREMVSRMKSTTEEVKLAIVGKYTNLEDSYLSILEAVKHGGIDNGCKVEVNMVEAETLEEDPAEIEKLRQFDGILIPGGFGGRGTEGKMLAIKFARENDVPFLGICLGMQLAVIEFARNVVNLENANSTEFDEDTPYPVIDILPEQTGVADMGGTMRLGDYDAILKDGSLATKLYGTNYIVERHRHRYEVNPEFVDRLESFGIVFSGKNKNRMEIAEIPDKRFFFASQFHPEFRSRPGRPSPPFKGLVRAMCKYNKEKEGQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE010299
EMBL· GenBank· DDBJ
AAM06649.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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