A0A0E3QX51 · A0A0E3QX51_METBA

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.

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 site240ATP (UniProtKB | ChEBI)
Binding site352L-glutamine (UniProtKB | ChEBI)
Active site379Nucleophile
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 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
      MSBRM_2319

Organism names

  • Taxonomic identifier
  • Strain
    • MS
  • Taxonomic lineage
    Archaea > Euryarchaeota > Stenosarchaea group > Methanomicrobia > Methanosarcinales > Methanosarcinaceae > Methanosarcina

Accessions

  • Primary accession
    A0A0E3QX51

Proteomes

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-265Amidoligase domain
Domain2-265CTP synthase N-terminal
Domain300-521Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    534
  • Mass (Da)
    59,437
  • Last updated
    2015-06-24 v1
  • Checksum
    70D6F89754774F0B
MKYIIVTGGVMSGLGKGITIASIGRNLKNKGYKVTAIKIDPYINIDAGTMSPYQHGEVFVLKDGGEVDLDLGNYERFLDTELTRDHNLTTGKVYLEVISKERRGDYLGKTVQIIPHVTNEIKSRIRKVAARSGADICLIEIGGTVGDIESMPFLEAVRQMHREEPSENVAFIHVTLAMEDLQGEQKTKPSQHSVKELRALGLSPEVIVVRSKSPLQESAKEKIALFCDVPQELVISAHDANDIYEVPLEIEEQGLTTQLMKHLQLESNVENGAWKEMVARMHSTTNTVKLAIVGKYTNLEDSYLSILEAVKHGGIDNGCRVEVNMVEAEILEENPAEVEKLIQYDGILIPGGFGGRGTEGKMTAIKFARENDIPFLGICLGMQLAVIEFARNVAKLKGANSTEFDEDTPYPVIDLLPEQTSVAEMGGTMRLGDYEAILTEGSIAAKIYGTNYIVERHRHRYEVNPEFVDRLESYGIVFSGKNKNRMEIAEIPGKRFFFGSQFHPEFRSRPGRPSPPFNGLVAAMCKYRKEREGR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP009528
EMBL· GenBank· DDBJ
AKB55317.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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