A0A090QM87 · A0A090QM87_9FLAO

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.

TypeIDPosition(s)Description
Binding site15CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site15UTP (UniProtKB | ChEBI)
Binding site16-21ATP (UniProtKB | ChEBI)
Binding site56L-glutamine (UniProtKB | ChEBI)
Binding site73ATP (UniProtKB | ChEBI)
Binding site73Mg2+ (UniProtKB | ChEBI)
Binding site143Mg2+ (UniProtKB | ChEBI)
Binding site150-152CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site190-195CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site190-195UTP (UniProtKB | ChEBI)
Binding site226CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site226UTP (UniProtKB | ChEBI)
Binding site244ATP (UniProtKB | ChEBI)
Binding site357L-glutamine (UniProtKB | ChEBI)
Active site384Nucleophile
Active site384Nucleophile; for glutamine hydrolysis
Binding site385-388L-glutamine (UniProtKB | ChEBI)
Binding site408L-glutamine (UniProtKB | ChEBI)
Binding site464L-glutamine (UniProtKB | ChEBI)
Active site509
Active site511

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular FunctionCTP synthase activity
Molecular Functionglutaminase activity
Molecular Functionmetal ion binding
Biological Process'de novo' CTP biosynthetic process
Biological Processglutamine metabolic 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
      JCM19294_960

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • JCM 19294
  • Taxonomic lineage
    Bacteria > Bacteroidota > Flavobacteriia > Flavobacteriales > Flavobacteriaceae > Nonlabens

Accessions

  • Primary accession
    A0A090QM87

Proteomes

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-269Amidoligase domain
Domain5-269CTP synthase N-terminal
Domain305-528Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    539
  • Mass (Da)
    60,423
  • Last updated
    2014-11-26 v1
  • Checksum
    AE1F87BC41595BA5
MAHAKYIFVTGGVTSSLGKGIIAASLAKLLQARGLRVTIQKLDPYINVDPGTLNPYEHGECYVTEDGAETDLDLGHYERFLNVNTSQANNVTTGRIYQSVIQKERRGEFLGKTVQVIPHITDEIKERIQILGKSGDYDVIITEIGGTVGDIESLPYIESVRQLQWELGDNNSLVIHLTLIPFLSAAGELKTKPTQHSVKTLMESGVQADILVCRTEHELSDEIRTKLARFCNVKPEAVIQSIDVETIYDVPNKMLLEGLDRVVIKQLHIETESQPNLKSWNEFVIKHKNPKSQVTIGLIGKYVELQDSYKSILEAFIHAGAENEVKVKIESIHSEYLEVENVEKKLSHLDGILVAPGFGERGIEGKIEAVRYARENGLPFFGICLGMQMAVIEYSRNVLGLKESNSIEMDDNTPHPVISLMEDQKNILDMGGTMRLGAWDCKLNGGKVSEIYGNELISERHRHRYEYNNEYRNQLEQAGLKTTGVNPKTDLVEIVEIENHPWFIGVQYHPEYKSTVANPHPLFKSFVAAAATFKSNKNK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BBML01000003
EMBL· GenBank· DDBJ
GAK96651.1
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