T5CGT2 · T5CGT2_HELPX

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 site59carbamoyl phosphate (UniProtKB | ChEBI)
Binding site60carbamoyl phosphate (UniProtKB | ChEBI)
Binding site87L-aspartate (UniProtKB | ChEBI)
Binding site109carbamoyl phosphate (UniProtKB | ChEBI)
Binding site137carbamoyl phosphate (UniProtKB | ChEBI)
Binding site140carbamoyl phosphate (UniProtKB | ChEBI)
Binding site173L-aspartate (UniProtKB | ChEBI)
Binding site223L-aspartate (UniProtKB | ChEBI)
Binding site266carbamoyl phosphate (UniProtKB | ChEBI)
Binding site267carbamoyl 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
      N411_01735

Organism names

  • Taxonomic identifier
  • Strain
    • FD535
  • Taxonomic lineage
    Bacteria > Campylobacterota > Epsilonproteobacteria > Campylobacterales > Helicobacteraceae > Helicobacter

Accessions

  • Primary accession
    T5CGT2

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
Domain6-149Aspartate/ornithine carbamoyltransferase carbamoyl-P binding
Domain159-303Aspartate/ornithine carbamoyltransferase Asp/Orn-binding

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    307
  • Mass (Da)
    34,105
  • Last updated
    2013-11-13 v1
  • MD5 Checksum
    2A175D95A36E3F52640C8E9675B893D1
MPKKCRHLLQTSDLSLDEIKLLLNKASVYANDFNAVSLEIKEKMHNKIIVALFFENSTRTVSSFEIASLRLGAKIVKLNMQTSSTSKGETLIDTFKNIHAMQPDAIITRHAFSSAPFKLAEFSQCPLINAGSGVSAHPTQALLDLLTLYRHFGSLENLKGKKIAFIGDVKNSRVANSNIKLLQRLGLEIMLCAPSSMLPSVSLKTTHNIEEAIGFADILMSLRTQTERHNAPIFASLKDYGNAYCITQKRLEAHAKNKEVIILHPGPVHRDIDIESAVLEDKRSKVLEQVKNGVAMRMAVLEFLLLD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AKHP02000067
EMBL· GenBank· DDBJ
EQL56482.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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