A0A1W9PG24 · A0A1W9PG24_9HELI

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 site49carbamoyl phosphate (UniProtKB | ChEBI)
Binding site50carbamoyl phosphate (UniProtKB | ChEBI)
Binding site77L-aspartate (UniProtKB | ChEBI)
Binding site99carbamoyl phosphate (UniProtKB | ChEBI)
Binding site127carbamoyl phosphate (UniProtKB | ChEBI)
Binding site130carbamoyl phosphate (UniProtKB | ChEBI)
Binding site160L-aspartate (UniProtKB | ChEBI)
Binding site210L-aspartate (UniProtKB | ChEBI)
Binding site249carbamoyl phosphate (UniProtKB | ChEBI)
Binding site250carbamoyl phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionamino acid binding
Molecular Functionaspartate carbamoyltransferase activity
Molecular FunctionDNA binding
Biological Process'de novo' pyrimidine nucleobase biosynthetic process
Biological Process'de novo' UMP biosynthetic process
Biological Processamino acid metabolic process
Biological Processregulation of DNA-templated transcription

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
      B5M52_07650

Organism names

Accessions

  • Primary accession
    A0A1W9PG24

Proteomes

Subcellular Location

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
Domain1-21HTH merR-type

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    291
  • Mass (Da)
    32,386
  • Last updated
    2017-07-05 v1
  • Checksum
    54DB62430E490840
MQHLIRTDDFSVEEIEQLLADAEYFSQVGFNRILQDKLIITLFFENSTRTKSSFEIAAKRLGAEIVHLDIAKSSTKKGETLVDTAANLDAMGPNAIIVRHANAGVPKILSKHTKTSIINAGDGAHAHPTQALLDLFTLKKHFGDLKGKKIAIVGDIKNSRVANSNIELLQRFGLNITLVSPPQFMPKTDLPSTYNLRDVIDSVDIIMSLRTQTERHSQQTYASLKDYASDFCITKELIGERDITILHPGPVHRNVDIDDAMLADKRCKVLDQVSNGVLIRMAVLKKLIYDL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MZGN01000122
EMBL· GenBank· DDBJ
OQX57331.1
EMBL· GenBank· DDBJ
Genomic DNA

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