A0A423UF57 · A0A423UF57_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.
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 site25CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site25UTP (UniProtKB | ChEBI)
Binding site26-31ATP (UniProtKB | ChEBI)
Binding site83ATP (UniProtKB | ChEBI)
Binding site83Mg2+ (UniProtKB | ChEBI)
Binding site152Mg2+ (UniProtKB | ChEBI)
Binding site159-161CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site199-204CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site199-204UTP (UniProtKB | ChEBI)
Binding site235CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site235UTP (UniProtKB | ChEBI)
Binding site253ATP (UniProtKB | ChEBI)
Binding site366L-glutamine (UniProtKB | ChEBI)
Active site393Nucleophile
Active site393Nucleophile; for glutamine hydrolysis
Binding site394-397L-glutamine (UniProtKB | ChEBI)
Binding site417L-glutamine (UniProtKB | ChEBI)
Binding site478L-glutamine (UniProtKB | ChEBI)
Active site525
Active site527

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
      BMONG18_0497

Organism names

  • Taxonomic identifier
  • Strain
    • BMONG18
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Bifidobacteriales > Bifidobacteriaceae > Bifidobacterium

Accessions

  • Primary accession
    A0A423UF57

Proteomes

Subcellular Location

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-278Amidoligase domain
Domain15-278CTP synthase N-terminal
Domain313-544Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    555
  • Mass (Da)
    61,351
  • Last updated
    2019-05-08 v1
  • Checksum
    A2F4E7F16D9B1D0F
MARRQHGNSLKHVTKHIFVTGGVVSSLGKGLTASSLGRLLRSRGIRVLQQKLDPYINVDPGTMNPFQHGEVYVTEDGAETDLDIGHYERFLDVFLSQKANVTTGQIYQSVLNKERAGEYLGQCVQVIPHITNEIKSRMRAQASDDVDVIITEIGGTVGDIESQPFLEAAREVRRDLGPENCMFVHVSLVPYIAAAHELKTKPTQHSVMALRQLGIVPDALVLRSDRPLNDAIKAKISLMCDVDAEGVVNCIDAPSIYDVPKILFNEGLDAYVVRELELPFHDVDWKEWENLLDRVHHPKHEVNVAIVGKYIDLPDAYLSVTEAIKAGGFANYAKVNVEWIAADLCETTEGAKEQLKDVDGIVIPGGFGIRGIEGKIGALKFAREHQLPALGLCLGLQSMVIEYSRHVMGLEDANSSEFEPDCQNPVIATMEEQKAIVAGKGDMGHTMRLGSYPAELEKDSLVAKLYGTTHVTERHRHRYEVNVAYKDQLRSAGLRISGQSPDGELTEFIELPQDVHPFYVGTQAHPEFKSRPTKPHPLFAGLVKASLDHQKARLG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QRAJ01000002
EMBL· GenBank· DDBJ
ROT87330.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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