A0A0Q7AST6 · A0A0Q7AST6_9ACTN

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 site55carbamoyl phosphate (UniProtKB | ChEBI)
Binding site56carbamoyl phosphate (UniProtKB | ChEBI)
Binding site83L-aspartate (UniProtKB | ChEBI)
Binding site105carbamoyl phosphate (UniProtKB | ChEBI)
Binding site135carbamoyl phosphate (UniProtKB | ChEBI)
Binding site138carbamoyl phosphate (UniProtKB | ChEBI)
Binding site173L-aspartate (UniProtKB | ChEBI)
Binding site227L-aspartate (UniProtKB | ChEBI)
Binding site268carbamoyl phosphate (UniProtKB | ChEBI)
Binding site269carbamoyl 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
      ASC77_22570

Organism names

  • Taxonomic identifier
  • Strain
    • Root1257
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Propionibacteriales > Nocardioidaceae > Nocardioides

Accessions

  • Primary accession
    A0A0Q7AST6

Proteomes

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).

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-147Aspartate/ornithine carbamoyltransferase carbamoyl-P binding
Domain160-306Aspartate/ornithine carbamoyltransferase Asp/Orn-binding

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    318
  • Mass (Da)
    34,256
  • Last updated
    2016-01-20 v1
  • Checksum
    4616E89E149A6E4B
MKRHLLSAADLSRDDAELVLATADEMRSLADRPIKKLPALRGRTVVNLFFEDSTRTRISFEAAAKRLSADVINFSAKGSSLSKGESLKDTALTLEAMGADAVVVRHGASGAPHLLAHSGWVRSSVVNAGDGTHEHPTQALLDAFTMWKHLGESKPGGLEGRRIAIVGDVLHSRVARSNALLLRTLGAEVTLVAPPTLLPVGIEGWPVETSYDLDGVLPKADAVMMLRVQRERMHGGFFPTAREYSRRYGLDGKRMAMLQDHTIVMHPGPMVRGMEITADVADSDRSVIVEQVTNGVAVRMAVLYLLLGGSEPAVGGEE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LMDV01000014
EMBL· GenBank· DDBJ
KQW43074.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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