A0A1S2VV65 · A0A1S2VV65_BIFLI

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 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 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
      BIFLH23_01468
      , BIFLH665_02241
      , BLJG463_01885
      , BLONGUMMC1_01326
      , HNS28_03550

Organism names

  • Taxonomic identifier
  • Strains
    • B.longum_ssp_infantis_4
    • Bifidobacterium_longum_subsp_infantis_JG_Bg463
    • LH_23
    • LH_665
    • BI-G201
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Bifidobacteriales > Bifidobacteriaceae > Bifidobacterium

Accessions

  • Primary accession
    A0A1S2VV65

Proteomes

Subcellular Location

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(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
    553
  • Mass (Da)
    60,925
  • Last updated
    2017-04-12 v1
  • Checksum
    8C8EA4ABEECD98C0
MVRRTHGNSQEHVTKHIFVTGGVVSSLGKGLTASSLGRLLRSRGIHVLQQKLDPYINVDPGTMNPFQHGEVYVTEDGAETDLDIGHYERFLDVFLSQKANVTTGQIYQEVLRKERAGEYLGQCVQVIPHITNEIKSRMRAQASDDVDVIITEIGGTVGDIESQPFLEAAREVRRDLGPDNCMFVHVSLVPYISAAHELKTKPTQHSVMMLRQLGISPDALVLRSDRPLNQSIKDKISLMCDVDAEGVVNCVDAPSIYDVPKILFEEGLDAYVVRELGLPFHDVDWDEWADLLERVHHPKHEVNIAIVGKYIDLPDAYLSVTEAIKAGGFANWAKVNVKWVAADRCETTEGAAAALDNVDGIVIPGGFGIRGIDGKIGALKFARETKLPALGLCLGLQSMVIEYSRHVLGIEDANSSEFEPDCANPVIATMEEQKDIVAGKGDMGHTMRLGSYPAELEEGSLVAELYGTTHVTERHRHRYEVNVAYKDRLREGGLRISGQSPDGELTEFVELPQDVHPFYVATQAHPEFKSRPTKPHPLFAGLVKAALGHQAAR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JABNND010000006
EMBL· GenBank· DDBJ
NQX50559.1
EMBL· GenBank· DDBJ
Genomic DNA
CABHML010000062
EMBL· GenBank· DDBJ
VUW83777.1
EMBL· GenBank· DDBJ
Genomic DNA
CABHNT010000046
EMBL· GenBank· DDBJ
VUX36580.1
EMBL· GenBank· DDBJ
Genomic DNA
CABWKE010000033
EMBL· GenBank· DDBJ
VWQ29128.1
EMBL· GenBank· DDBJ
Genomic DNA
CABWKH010000023
EMBL· GenBank· DDBJ
VWQ36433.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp