A0A0G0DS17 · A0A0G0DS17_9BACT

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 site16CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site16UTP (UniProtKB | ChEBI)
Binding site17-22ATP (UniProtKB | ChEBI)
Binding site74ATP (UniProtKB | ChEBI)
Binding site74Mg2+ (UniProtKB | ChEBI)
Binding site144Mg2+ (UniProtKB | ChEBI)
Binding site151-153CTP (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 site362L-glutamine (UniProtKB | ChEBI)
Active site389Nucleophile
Active site389Nucleophile; for glutamine hydrolysis
Binding site390-393L-glutamine (UniProtKB | ChEBI)
Binding site413L-glutamine (UniProtKB | ChEBI)
Binding site473L-glutamine (UniProtKB | ChEBI)
Active site520
Active site522

GO annotations

AspectTerm
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
      UR51_C0010G0033

Organism names

Accessions

  • Primary accession
    A0A0G0DS17

Proteomes

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-269Amidoligase domain
Domain6-269CTP synthase N-terminal
Domain310-539Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    544
  • Mass (Da)
    61,914
  • Last updated
    2015-07-22 v1
  • Checksum
    1A3BF80D8D63A54D
MKNNKKYIFVLGGVMSGIGKGIATSSLGAILKARGYKPTAIKIDPYVNVDAGTMNPTEHGEVFVMDCGLETDQDMGNYERFMEINLPGENYMTTGSIYQKVINRERNLEYKGKCVQIIPHITDEVIRTIKNAAKNNEADIVLTEIGGTIGDYENMLFMEAARQMKLKHPKDVVFVMITYLPYPPKVGEMKTKPTQQAVRELNANGINPDIIIARSEVEIDKKRKEKIALFCNVNEKDIISAPDIDTVYEVPINFERDDLSRRILKKLELPTKKTDLKKWYNLVDNIKKSEKAVKIGIVGKYFGTGEFMLGDSYISVIEAVKHACYKAKVKPQIEWFNSEEFEKKGVDMNKLREYDGIVVPGGFGSRGIEGKINVIRYCRENKIPFLGLCYGMQLAVIEFARNVLKLKDAHTSEIDRKSKNLIIDIMPEQKKNLEDRNYGATMRLGAYPAFLSRDTIAYKAYGKKEISERHRHRWEVNPDYIERIEKGGLVFSGKSADGRLMEIAELPKSEHPFFLGTQFHPEFKSTPLSSHPLFFEFIKAARDK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LBPM01000010
EMBL· GenBank· DDBJ
KKP57877.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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