A0A6G4Z527 · A0A6G4Z527_STAAU

  • Protein
    Aspartate carbamoyltransferase
  • Gene
    pyrB
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes the condensation of carbamoyl phosphate and aspartate to form carbamoyl aspartate and inorganic phosphate, the committed step in the de novo pyrimidine nucleotide biosynthesis pathway.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site50carbamoyl phosphate (UniProtKB | ChEBI)
Binding site51carbamoyl phosphate (UniProtKB | ChEBI)
Binding site78L-aspartate (UniProtKB | ChEBI)
Binding site100carbamoyl phosphate (UniProtKB | ChEBI)
Binding site127carbamoyl phosphate (UniProtKB | ChEBI)
Binding site130carbamoyl phosphate (UniProtKB | ChEBI)
Binding site160L-aspartate (UniProtKB | ChEBI)
Binding site210L-aspartate (UniProtKB | ChEBI)
Binding site253carbamoyl phosphate (UniProtKB | ChEBI)
Binding site254carbamoyl phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionamino acid binding
Molecular Functionaspartate carbamoyltransferase activity
Biological Process'de novo' pyrimidine nucleobase biosynthetic process
Biological Process'de novo' UMP biosynthetic process
Biological Processamino acid metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Aspartate carbamoyltransferase
  • EC number
  • Alternative names
    • Aspartate transcarbamylase
      (ATCase
      )

Gene names

    • Name
      pyrB
    • ORF names
      G6Y33_08580

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • UG797
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus

Accessions

  • Primary accession
    A0A6G4Z527

Subcellular Location

Interaction

Subunit

Heterododecamer (2C3:3R2) of six catalytic PyrB chains organized as two trimers (C3), and six regulatory PyrI chains organized as three dimers (R2).

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-140Aspartate/ornithine carbamoyltransferase carbamoyl-P binding
Domain146-288Aspartate/ornithine carbamoyltransferase Asp/Orn-binding

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    293
  • Mass (Da)
    33,259
  • Last updated
    2020-08-12 v1
  • Checksum
    345C67C203DAFE24
MNHLLSMEHLSTDQIYKLIQKASQFKSGERQLPNFEGEYVANLFFENSTRTKCSFEMAELKLGLKTISFETSTSSVSKGESLYDTCKTLESIGCDLLVIRHPFNNYYEKLANINIPIANAGDGSGQHPTQSLLDLMTIYEEYGYFEGLNVLICGDIKNSRVARSNYHSLKALGANVMFNSPNAWIDDSLEAPYVNIDDVIETVDIVMLLRIQHERHGLAEETRFAADDYHQKHGLNEVRYNKLQEHAIVMHPAPVNRGVEIQSDLVEASKSRIFKQMENGVYLRMAVIDELLK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAALQE010000009
EMBL· GenBank· DDBJ
NGS70891.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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