Q0AXG1 · PYRB_SYNWW

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.

131220406080100120140160180200220240260280300
TypeIDPosition(s)Description
Binding site58carbamoyl phosphate (UniProtKB | ChEBI)
Binding site59carbamoyl phosphate (UniProtKB | ChEBI)
Binding site86L-aspartate (UniProtKB | ChEBI)
Binding site108carbamoyl phosphate (UniProtKB | ChEBI)
Binding site136carbamoyl phosphate (UniProtKB | ChEBI)
Binding site139carbamoyl phosphate (UniProtKB | ChEBI)
Binding site169L-aspartate (UniProtKB | ChEBI)
Binding site223L-aspartate (UniProtKB | ChEBI)
Binding site264carbamoyl phosphate (UniProtKB | ChEBI)
Binding site265carbamoyl 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
      Swol_1284

Organism names

Accessions

  • Primary accession
    Q0AXG1

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10000000231-312Aspartate 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
    312
  • Mass (Da)
    34,503
  • Last updated
    2006-10-17 v1
  • Checksum
    31244E2C5C5C8A68
MKLDRKDLLGLRDLSREETELILNTAIPMKDVICRDIKKVPTLRGKALVTVFYENSTRTRTSFELAGKYLSADTVNLSVSTSSVQKGESLRDTIKTIEVMGFDLMVMRHAMSGTPHYVARNTRMRVINAGDGANEHPTQALLDMYTIKEKKGTLESLKVAIVGDILHSRVARSNIYGLSKFGCDIRVVGPATLMPPGIEKLGVKSYYSLDEAINGVDVINILRIQRERQVSGLFPSLDEYAQLYMLSPQTLARAKDDVLVLHPGPINRGVEISSELADSAQALINEQVTNGVAIRMALLFLMMGGGRDEITY

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000448
EMBL· GenBank· DDBJ
ABI68593.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp