A0A9D1A9V7 · A0A9D1A9V7_9FIRM

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 site51carbamoyl phosphate (UniProtKB | ChEBI)
Binding site52carbamoyl phosphate (UniProtKB | ChEBI)
Binding site80L-aspartate (UniProtKB | ChEBI)
Binding site101carbamoyl phosphate (UniProtKB | ChEBI)
Binding site129carbamoyl phosphate (UniProtKB | ChEBI)
Binding site132carbamoyl phosphate (UniProtKB | ChEBI)
Binding site162L-aspartate (UniProtKB | ChEBI)
Binding site225L-aspartate (UniProtKB | ChEBI)
Binding site264carbamoyl phosphate (UniProtKB | ChEBI)
Binding site265carbamoyl 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
  • EC number
  • Alternative names
    • Aspartate transcarbamylase
      (ATCase
      )

Gene names

    • Name
      pyrB
    • ORF names
      IAB31_01735

Organism names

  • Taxonomic identifier
  • Strain
    • ChiSjej4B22-8148
  • Taxonomic lineage
    Bacteria > Bacillati > Bacillota > Clostridia > Lachnospirales > Lachnospiraceae > Lachnospiraceae incertae sedis > Candidatus Choladousia

Accessions

  • Primary accession
    A0A9D1A9V7

Proteomes

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
Domain2-141Aspartate/ornithine carbamoyltransferase carbamoyl-P binding
Domain149-299Aspartate/ornithine carbamoyltransferase Asp/Orn-binding

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    306
  • Mass (Da)
    34,165
  • Last updated
    2023-05-03 v1
  • MD5 Checksum
    CD98E22FCBA6FDB7EEDA10B732CC1B25
MRHLMSPLDFSVEELDRLLDLANDIEANPAKYAHACTGKKLATLFYEPSTRTRLSFEAAMLNLGGSVLGFSSADSSSAAKGESVADTIRVISCYADICAMRHPKEGAPLVASLHSSIPVINAGDGGHQHPTQTLTDLLTIRSLKGRLGNLTIGLCGDLKFGRTVHSLIHALVRYPNVSFVLISPEELRIPDYIRDDVLRANHCSFKEVVRLEDALPELDLLYMTRVQRERFFNEEDYVRMKDFYILDKAKMKLAGPDMLVLHPLPRVNEIAVEVDADPRAVYFKQAQYGVYVRMALMLTLLEVKVC

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DVGK01000027
EMBL· GenBank· DDBJ
HIR12626.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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