A0A6I4NRD5 · A0A6I4NRD5_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 site465L-glutamine (UniProtKB | ChEBI)
Active site510
Active site512

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
      GON26_20145

Organism names

Accessions

  • Primary accession
    A0A6I4NRD5

Proteomes

Subcellular Location

Interaction

Subunit

Homotetramer.

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    537
  • Mass (Da)
    59,729
  • Last updated
    2020-08-12 v1
  • Checksum
    738BC91BE1B8400B
MNQTKYIFVTGGVTSSLGKGIIAASLAKLLQGRGYRTTIQKFDPYINVDPGTLNPYEHGECYVTDDGAETDLDLGHYERFLNVPTSQANNVTTGRVYLSVIEKERRGEFLGKTVQVVPHITNEIKDRMQLLGKSGDYDIVITEIGGTVGDIESLPYIESVRQLVWELGENNGIVIHLTLVPYLAAAGELKTKPTQHSVKTLMESGIKADILVCRTEHELSQELRSKLALFCNVKKEAVIQSIDASTIYEVPNLMLEEGLDVVALKKLDLPKKAAPDLKNWNTFLRRLKNPKQTVNIGLIGKYVEMQDCYKSILEAFIHAGAANETKVNVISIHSEHINIDNVAEKLGVLDGVLVAPGFGERGIEGKIEAVRYARENNIPFFGICLGMQMSVIEYSRNILGYAEANSTEMNENTKHPVVNLMEEQKTITDKGGTMRLGAWKCDIKEGTLAHKIYGQTTISERHRHRYEYNNKYKDELQKAGLIASGVNPDTGLVEIIELDNHPFFIGVQYHPEYKSTVANPHPIFVNFVAAAVNAIKK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WSTB01000016
EMBL· GenBank· DDBJ
MWB96681.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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