A0A934TNJ1 · A0A934TNJ1_9BURK

Function

function

Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 2 Zn2+ ions per subunit.

Pathway

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

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site14Zn2+ 1 (UniProtKB | ChEBI)
Binding site16Zn2+ 1 (UniProtKB | ChEBI)
Binding site16-18substrate
Binding site42substrate
Binding site99Zn2+ 1 (UniProtKB | ChEBI); via carbamate group
Binding site99Zn2+ 2 (UniProtKB | ChEBI); via carbamate group
Binding site136Zn2+ 2 (UniProtKB | ChEBI)
Binding site136substrate
Binding site174Zn2+ 2 (UniProtKB | ChEBI)
Binding site219substrate
Active site247
Binding site247Zn2+ 1 (UniProtKB | ChEBI)
Binding site251substrate
Binding site263substrate

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functiondihydroorotase activity
Molecular Functionzinc ion binding
Biological Process'de novo' pyrimidine nucleobase biosynthetic process
Biological Processpyrimidine ribonucleotide biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Dihydroorotase
  • EC number
  • Short names
    DHOase

Gene names

    • Name
      pyrC
    • ORF names
      JJB11_00210

Organism names

  • Taxonomic identifier
  • Strain
    • KACC 17527
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Comamonadaceae > Ramlibacter

Accessions

  • Primary accession
    A0A934TNJ1

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue99N6-carboxylysine

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain12-310Amidohydrolase-related

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    344
  • Mass (Da)
    37,737
  • Last updated
    2023-02-22 v1
  • Checksum
    7ABF19A1C9A3E627
MSQTLTITRPDDWHLHVRDGAAMASVVPHSAAQFARALIMPNLKPPVTTAALANAYRERILAAVPKGVQFQPLMSLYLTDHLAPGEIARARADGVVAVKLYPAGATTNSAAGVTDIRKTYPTLEAMQRAGMLLLVHGEVTDPDVDIFDREAVFLETKLQPLRRDFPELKIVVEHMTTKEAVQYVRDADRFTAGTITAHHLLYNRNAIFTGGIRPHYYCLPVLKREVHRQALVDAATSGSAKFFLGTDSAPHPAVLKEHALGCAGCYTALSAMELYAEAFDNAGALDKLEGFASFHGADFYGLPRNTGKLTLKREEWQLPEKVPFGEAELKPLRGGEMLPWRVVA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAEPWM010000001
EMBL· GenBank· DDBJ
MBK6004497.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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