A0A202E9L4 · A0A202E9L4_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.

Type
IDPosition(s)Description
Binding site26CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site26UTP (UniProtKB | ChEBI)
Binding site27-32ATP (UniProtKB | ChEBI)
Binding site67L-glutamine (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 site515
Active site517

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
      B2G88_10825

Organism names

  • Taxonomic identifier
  • Strain
    • CGMCC 1.3597
  • Taxonomic lineage
    Archaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Natrialbaceae > Natronolimnobius

Accessions

  • Primary accession
    A0A202E9L4

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-277Amidoligase domain
Domain16-276CTP synthase N-terminal
Domain314-534Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    548
  • Mass (Da)
    60,904
  • Last updated
    2017-09-27 v1
  • Checksum
    A3D1DC85B2D0EA07
MPTESDTDYDPTLGNKFIFVTGGVMSGLGKGITAASTGRLLKNAGFDVTAVKIDPYLNVDAGTMNPYQHGEVYVLKDGGEVDLDLGNYERFLDVDMTSDHNITTGKTYQHVIEKERAGDYLGKTVQIIPHITNDIKRRIREAAEGTDVCIVEVGGTVGDIEGMPYLEALRQFAHEEDDEDILFTHVTLVPYSKNGEQKTKPTQHSVKEVRSIGLQPDVIVGRCEDKLEPETKEKIALFCDIPTDAVFSNPDVEDVYHVPLMVEEEGLDQYVLERFGMAEDALPEGERTNGWREIVTTEKDGAIDIALVGKYDLEDAYMSIHESLKHAGFEVGVDVNVHWVSADEMADGHDGQLEGMDGIIVPGGFGMRGTEGKIEAVRYARENDVPFLGLCLGFQMAVVEYARNVLGYEDAHSAEMEADTPHPVIDILPEQYEVENMGGTMRLGEHTTVIEPETLAYDLYEDTSCTERHRHRYEVNPEYFEDFEDEPLVFSGTAGNRMEILELEDHPYFFGTQYHPEYTSRPGQPSPPFLGLVEAVLSTQAPVADADD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MWPH01000002
EMBL· GenBank· DDBJ
OVE84858.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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