A1SJE8 · PYRB_NOCSJ

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.

Catalytic activity

Pathway

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

Features

Showing features for binding site.

132450100150200250300
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
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 catalytic subunit
  • EC number
  • Alternative names
    • Aspartate transcarbamylase
      (ATCase
      )

Gene names

    • Name
      pyrB
    • Ordered locus names
      Noca_2428

Organism names

Accessions

  • Primary accession
    A1SJE8

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003211271-324Aspartate carbamoyltransferase catalytic subunit

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

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    324
  • Mass (Da)
    35,078
  • Last updated
    2007-02-06 v1
  • Checksum
    7E5EE1337FFE7A2D
MKRHLLSAGDLSRDDAELVLRTAAELRELADRPIKKLPALRGRTVVNLFFEDSTRTRISFEAAAKRLSADVINFAAKGSSLSKGESLKDTALTLEAMGADAVVVRHGASGAPHRLAHSGWVRSSVVNAGDGTHEHPTQALLDAFTMWRHLGQGKEQSLDGRRIAIVGDVLHSRVARSNALLLKTLGAEVTLVAPPTLLPVGIDTWPVETSYDLDAVLPKADAVMMLRVQRERMSGGFFPTAREYSRRYGLDGRRMATLQDHTIVMHPGPMVRGMEITADVADSDRSVIVEQVTNGVAVRMAVLYLLLGGSEPAVSTSSTNEAEE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000509
EMBL· GenBank· DDBJ
ABL81933.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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