C5EXH7 · C5EXH7_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.

Catalytic activity

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.

Features

Showing features for binding site.

130320406080100120140160180200220240260280300
TypeIDPosition(s)Description
Binding site50carbamoyl phosphate (UniProtKB | ChEBI)
Binding site51carbamoyl phosphate (UniProtKB | ChEBI)
Binding site78L-aspartate (UniProtKB | ChEBI)
Binding site100carbamoyl phosphate (UniProtKB | ChEBI)
Binding site128carbamoyl phosphate (UniProtKB | ChEBI)
Binding site131carbamoyl phosphate (UniProtKB | ChEBI)
Binding site161L-aspartate (UniProtKB | ChEBI)
Binding site211L-aspartate (UniProtKB | ChEBI)
Binding site250carbamoyl phosphate (UniProtKB | ChEBI)
Binding site251carbamoyl 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
  • EC number
  • Alternative names
    • Aspartate transcarbamylase
      (ATCase
      )

Gene names

    • Name
      pyrB
    • ORF names
      HPMG_00445

Organism names

  • Taxonomic identifier
  • Strain
    • MIT 98-5489
  • Taxonomic lineage
    Bacteria > Campylobacterota > Epsilonproteobacteria > Campylobacterales > Helicobacteraceae > Helicobacter

Accessions

  • Primary accession
    C5EXH7

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
Domain3-140Aspartate/ornithine carbamoyltransferase carbamoyl-P binding
Domain147-287Aspartate/ornithine carbamoyltransferase Asp/Orn-binding

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    303
  • Mass (Da)
    34,040
  • Last updated
    2009-07-28 v1
  • Checksum
    4F7AFEFC88D5E55F
MPRHLIETQDFSKQEIERLLELAEQFLDGKPRNSLKNHTIITIFFENSTRTLSSFEVATKRLGGNVVRLDVSRSSTSKGETLFDTAANLNAMQPSAIIVRHKSAGVPNILSHYVSCSIVNGGDGAHAHPTQALLDLLTLKKHLGNLEGKKIAIVGDIKNSRVANSNMELLSRFGMEVILVGPPHFIPKTSLRHCLYLKEVLDEVDAIMSLRTQTERHNSPIYSSLKDYASDYCITKEMLQERNIILLHPGPVHRNIDISDEMLRDSRSKVLEQVTNGVAIRMAVLETLITQNIPKNYQNFPYF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DS990441
EMBL· GenBank· DDBJ
EEQ62988.1
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.
Help