A0A929BWQ1 · A0A929BWQ1_UNCCH

  • Protein
    Aspartate carbamoyltransferase
  • Gene
    pyrB
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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 site84L-aspartate (UniProtKB | ChEBI)
Binding site105carbamoyl phosphate (UniProtKB | ChEBI)
Binding site133carbamoyl phosphate (UniProtKB | ChEBI)
Binding site136carbamoyl phosphate (UniProtKB | ChEBI)
Binding site166L-aspartate (UniProtKB | ChEBI)
Binding site261L-aspartate (UniProtKB | ChEBI)
Binding site302carbamoyl phosphate (UniProtKB | ChEBI)
Binding site303carbamoyl phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionamino acid binding
Molecular Functionaspartate carbamoyltransferase activity
Biological Process'de novo' pyrimidine nucleobase biosynthetic process
Biological Processamino acid metabolic process
Biological Processpyrimidine ribonucleotide biosynthetic 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
      IMY81_01645

Organism names

Accessions

  • Primary accession
    A0A929BWQ1

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
Domain6-145Aspartate/ornithine carbamoyltransferase carbamoyl-P binding
Domain253-337Aspartate/ornithine carbamoyltransferase Asp/Orn-binding
Domain367-409Aspartate carbamoyltransferase regulatory subunit C-terminal

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    473
  • Mass (Da)
    52,205
  • Last updated
    2023-02-22 v1
  • Checksum
    82AB50779D8DF76C
MNLSGRSLVTIDDLSNGEIAAVFALADEMSYSIKEQLAVCRGKVMASLFFEPSTRTRLSFEAAMHRLGGSVISAVDTKATSLAKGESIADMARVIGSYADIIVIRHPWEGTARVVADYAGVPVINAGDGGHQHPTQTLLDLYTIKKERKAIKGLKIALWGDLKYGRTVHSLIFALAKLGANIIFCPTPGFEVPEHVIQKLIAEYGGELEKLDASEQVGKEGASPLDAIYITPGSPHQLAMMPNISIQVELKRGVDALYVTRPQKERFATGEEGEGLKTRYPVVDKKLLKEKEFEKTIIMHPLPRVDELACELDADPRSMYFKQAARGVPVRMALIALLLGAKEVTVPDKEGSSTGIDYPAYRHDLGLKCPNPRCVSVQKSEIKYIKPAFKIVSTKPMTLRCTYCEHGFEPKYVASSHWHEGMLEYKKYHSAESHWARTIRPENLIVFNSAGEAEARGFKPSHYATVPHKKNDG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JADFVB010000067
EMBL· GenBank· DDBJ
MBE9477929.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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