A0A4C2EF89 · A0A4C2EF89_9EURY

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 site26CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site26UTP (UniProtKB | ChEBI)
Binding site27-32ATP (UniProtKB | ChEBI)
Binding site84ATP (UniProtKB | ChEBI)
Binding site84Mg2+ (UniProtKB | ChEBI)
Binding site152Mg2+ (UniProtKB | ChEBI)
Binding site159-161CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site198-203CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site198-203UTP (UniProtKB | ChEBI)
Binding site234CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site234UTP (UniProtKB | ChEBI)
Binding site252ATP (UniProtKB | ChEBI)
Binding site364L-glutamine (UniProtKB | ChEBI)
Active site391Nucleophile
Active site391Nucleophile; for glutamine hydrolysis
Binding site392-395L-glutamine (UniProtKB | ChEBI)
Binding site415L-glutamine (UniProtKB | ChEBI)
Binding site472L-glutamine (UniProtKB | ChEBI)
Active site517
Active site519

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
      Harman_09470

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • MD130-1
  • Taxonomic lineage
    Archaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Haloarculaceae > Haloarcula

Accessions

  • Primary accession
    A0A4C2EF89

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-277Amidoligase domain
Domain16-277CTP synthase N-terminal
Domain314-536Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    553
  • Mass (Da)
    61,729
  • Last updated
    2019-07-03 v1
  • Checksum
    3740E95F738FD09C
MPTEPETDYDPELGRKFIFVTGGVMSGLGKGITAASTGRLLKNAGFDVTAVKIDPYLNVDAGTMNPFQHGEVYVLKDGGEVDLDLGNYERFLDIDMTFDHNVTTGKTYQHVIEKERAGDYLGRTVQIIPHITDDIKRRIREAAEGNDVCIIEVGGTVGDIEGMPYLEALRQFAHEEDEDDILFTHVTLVPYSKNGEQKTKPTQHSVKELRSIGLQPDILVGRCSDKLDIDTKEKIALFCDVPTEAVFSNPDVDDIYHVPLMVEEEGLDEYVMQELDIASEALPEDERENRWRDLVTQQTEGEVEVALVGKYDLEDAYMSVHEALKHAGLEKNVDVNVRWVNSEKMSDHHADRMREADAIVVPGGFGARGTEGKIDAIQYARENDVPFLGLCLGFQMAVVEYARNVLDLDDAHSAELDEDTPHPVIDILPEQYEIEDMGGTMRLGAHETDIDSNTLAATLYGGESCTERHRHRYEVNPEYIDDLEAAGLKFSGRAGNRMEILELAPEVHPYFIGTQFHPEFRSRPTRASPPFVGLLEAVLGDDPHTVTTEEVSH

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BIXZ01000001
EMBL· GenBank· DDBJ
GCF13012.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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