A0A956ERL9 · A0A956ERL9_UNCMY

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 site57L-glutamine (UniProtKB | ChEBI)
Binding site74ATP (UniProtKB | ChEBI)
Binding site74Mg2+ (UniProtKB | ChEBI)
Binding site142Mg2+ (UniProtKB | ChEBI)
Binding site149-151CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site189-194CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site189-194UTP (UniProtKB | ChEBI)
Binding site225CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site225UTP (UniProtKB | ChEBI)
Binding site243ATP (UniProtKB | ChEBI)
Binding site356L-glutamine (UniProtKB | ChEBI)
Active site383Nucleophile
Active site383Nucleophile; for glutamine hydrolysis
Binding site384-387L-glutamine (UniProtKB | ChEBI)
Binding site407L-glutamine (UniProtKB | ChEBI)
Binding site464L-glutamine (UniProtKB | ChEBI)
Active site509
Active site511

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular FunctionCTP synthase activity
Molecular Functionmetal ion binding
Biological ProcessCTP 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
      KC492_02080

Organism names

Accessions

  • Primary accession
    A0A956ERL9

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-268Amidoligase domain
Domain6-268CTP synthase N-terminal
Domain304-528Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    554
  • Mass (Da)
    60,489
  • Last updated
    2023-02-22 v1
  • Checksum
    82B009C5B5F29007
MSRRTKFVLVTGGVVSSIGKGLAAASIGALMEARGLRVTHMKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERYTSARLSRASNLTTGRIYEAVISKERRGEYLGATVQVIPHITDEIKAGIKRASKDADICIIEIGGTVGDIESLPFLEAIRQLKVEEGNENAVSVHVTLVPHIATAGELKTKPTQHSVREMREIGIQPDILICRCDRPIARGLKEKIALFSNVKVDSVISAVDVGCIYELPLVLHAEGLDDQIAERLNIWSRSPDLAAWKRVAERFKKPGNGSVKIGIVGKYVHLKDSYKSLHESIVHGGLENDVSVQFEYIDSEQLEGANAASILVGLDAILVPGGFGDRGVEGKISAIRFARENGVPYFGICLGMQLAVIEFARNVASIENATSSEFEKDAKHAVIDLMPDQRGVTDKGGTMRLGAYPCEIKAGTKAAEAYGELKISERHRHRYEFNNEYREALEGKGLVLSGLSPDGRLVELVELPNHPYFVGCQFHPEFKSRPMSPHPLFSKFVAAAVARREEIKKAAQSDAKDAPEAGLN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAGQIW010000140
EMBL· GenBank· DDBJ
MCA9639442.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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