W5TE24 · W5TE24_9NOCA

  • Protein
    CTP synthase
  • Gene
    pyrG
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.

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 site42CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site42UTP (UniProtKB | ChEBI)
Binding site43-48ATP (UniProtKB | ChEBI)
Binding site100ATP (UniProtKB | ChEBI)
Binding site100Mg2+ (UniProtKB | ChEBI)
Binding site174Mg2+ (UniProtKB | ChEBI)
Binding site181-183CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site221-226CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site221-226UTP (UniProtKB | ChEBI)
Binding site257CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site257UTP (UniProtKB | ChEBI)
Binding site275ATP (UniProtKB | ChEBI)
Binding site388L-glutamine (UniProtKB | ChEBI)
Active site415Nucleophile
Active site415Nucleophile; for glutamine hydrolysis
Binding site416-419L-glutamine (UniProtKB | ChEBI)
Binding site438L-glutamine (UniProtKB | ChEBI)
Binding site499L-glutamine (UniProtKB | ChEBI)
Active site546
Active site548

GO annotations

AspectTerm
Cellular Componentcytosol
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
      NONO_c25970

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • SH22a
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Nocardiaceae > Nocardia

Accessions

  • Primary accession
    W5TE24

Proteomes

Subcellular Location

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-300Amidoligase domain
Domain32-300CTP synthase N-terminal
Domain335-565Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    595
  • Mass (Da)
    64,565
  • Last updated
    2014-04-16 v1
  • Checksum
    173F6D48CD175363
MAFVSQPNFVLAWGSVSQSRIPARSPHQTATKHIFVSGGVASSLGKGLTASSLGQLLTSRGLRVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDVGHYERFLDRNLSRDANVTTGQVYSSVIAKERRGEYLGDTVQVIPHITDEIKDRILAMSGPDLEGQTPDVVITEIGGTVGDIESQPFLEAARQIRHEVGRENCFFLHVTLVPYLAPSGELKTKPTQHSVAALRNIGIQPDALILRCDREVPQGLKNKIALMCDVDVDACISTPDAPSIYDIPKVLHREGLDAYVVRKLGLPFRDVDWTVWGDLLDRVHNPREAVTVALVGKYVDLPDAYLSVTEALRAGGFAAKAKVNIRWVQSDECETPEGAQHHLGDVDAVLIPGGFGIRGIEGKVGAIRFARTRSIPLLGLCLGLQCVVIEAARSVGLEDANSAEFEPDTTHPVISTMADQAQAVAGEADLGGTMRLGAYPAVLEAGSVVAQTYGETEVSERHRHRFEVNNAYRDKIGQSGLRFSGTSPDGHLVEFVELPADVHPYFVATQAHPELKSRPTRPHPLFAGLVNAALDYKAAERLPVEIHAEDEAADDAERVGR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP006850
EMBL· GenBank· DDBJ
AHH17389.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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