A0A076JJP4 · A0A076JJP4_9BIFI

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 site24CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site24UTP (UniProtKB | ChEBI)
Binding site25-30ATP (UniProtKB | ChEBI)
Binding site82ATP (UniProtKB | ChEBI)
Binding site82Mg2+ (UniProtKB | ChEBI)
Binding site151Mg2+ (UniProtKB | ChEBI)
Binding site158-160CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site198-203CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site198-203UTP (UniProtKB | ChEBI)
Binding site234CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site234UTP (UniProtKB | ChEBI)
Binding site252ATP (UniProtKB | ChEBI)
Binding site365L-glutamine (UniProtKB | ChEBI)
Active site392Nucleophile
Active site392Nucleophile; for glutamine hydrolysis
Binding site393-396L-glutamine (UniProtKB | ChEBI)
Binding site416L-glutamine (UniProtKB | ChEBI)
Binding site477L-glutamine (UniProtKB | ChEBI)
Active site524
Active site526

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
      BCOR_0760

Organism names

  • Taxonomic identifier
  • Strain
    • LMG 18911
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Bifidobacteriales > Bifidobacteriaceae > Bifidobacterium

Accessions

  • Primary accession
    A0A076JJP4

Proteomes

Subcellular Location

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-277Amidoligase domain
Domain14-277CTP synthase N-terminal
Domain312-543Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    553
  • Mass (Da)
    60,907
  • Last updated
    2014-10-29 v1
  • MD5 Checksum
    B6D2E4FB1B50269A273C97A5641B8081
MVREHGNSQGHITKHIFVTGGVVSSLGKGLTASSLGRLLRSRGIRVLQQKLDPYINVDPGTMNPFQHGEVYVTEDGAETDLDIGHYERFLDVFLSQKANVTTGQIYQSVLRKERAGEYLGQCVQVIPHVTNEIKSRMRAQAGDDVDVIITEIGGTVGDIESQPFMEAAREVRRDIGADNCMFVHVSLVPYIAAAHELKTKPTQHSVMALRQLGIAPDALVLRSDRPLSQSIKDKISLMCDVDAEGVVNCVDAPSIYDVPKILYSEGLDAYVVRKLELPFHDVDWNEWEDLLERVHNPRNRVTVAIVGKYIDLPDAYLSVIEAIKAGGFANWAKVDVKLVTADSCETMDGAREALQGVDGIVIPGGFGVRGIEGKLGALRYARETKLPALGICLGLQSMVIEYARHVLGLEDANSSEFEPNCEHPVIATMEEQKDIVAGHGDMGHTMRLGAYPAILRQDSLVAELYGKTEVSERHRHRYEVSVAYKQDLDKAGLHISGTSPDGQLTEFVELPKDRHPFYVGTQAHPEFKSRPTKPHPLFAGLVKASIEHQQAAD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP007287
EMBL· GenBank· DDBJ
AII74771.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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