Q9ZM81 · PYRB_HELPJ

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.

130720406080100120140160180200220240260280300
TypeIDPosition(s)Description
Binding site59carbamoyl phosphate (UniProtKB | ChEBI)
Binding site60carbamoyl phosphate (UniProtKB | ChEBI)
Binding site87L-aspartate (UniProtKB | ChEBI)
Binding site109carbamoyl phosphate (UniProtKB | ChEBI)
Binding site137carbamoyl phosphate (UniProtKB | ChEBI)
Binding site140carbamoyl phosphate (UniProtKB | ChEBI)
Binding site173L-aspartate (UniProtKB | ChEBI)
Binding site223L-aspartate (UniProtKB | ChEBI)
Binding site266carbamoyl phosphate (UniProtKB | ChEBI)
Binding site267carbamoyl 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 catalytic subunit
  • EC number
  • Alternative names
    • Aspartate transcarbamylase
      (ATCase
      )

Gene names

    • Name
      pyrB
    • Ordered locus names
      jhp_0341

Organism names

Accessions

  • Primary accession
    Q9ZM81

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001131421-307Aspartate 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).

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    307
  • Mass (Da)
    34,183
  • Last updated
    1999-05-01 v1
  • Checksum
    3B8607592B309028
MPKKCRHLLQTSDLSLDEIKLLLNKASVYANDFNAVSLETREKMQDKIIVALFFENSTRTVSSFEIASLRLGAKIVKLNMQTSSTSKGETLIDTFKNIHAMQPDAIITRHAFSSAPFKLAEFSQCPLINAGSGTSAHPTQALLDLLTLYRHFGSLENLKGKKIAFIGDVKNSRVANSNIKLLQRLGLEIMLCAPSSMLPITPLKTTHNIEEAIGFADILMSLRTQTERHNAPIFASLKDYGNAYCITQKRLETHAKNKEVIILHPGPVHRDIDIESAVLEDKRSKVLEQVKNGVAMRMAVLEFLLLD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE001439
EMBL· GenBank· DDBJ
AAD05915.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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