A0A2M8WKN3 · A0A2M8WKN3_9RHOB

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

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.

TypeIDPosition(s)Description
Binding site18Zn2+ 1 (UniProtKB | ChEBI)
Binding site20Zn2+ 1 (UniProtKB | ChEBI)
Binding site20-22substrate
Binding site46substrate
Binding site104Zn2+ 1 (UniProtKB | ChEBI); via carbamate group
Binding site104Zn2+ 2 (UniProtKB | ChEBI); via carbamate group
Binding site141Zn2+ 2 (UniProtKB | ChEBI)
Binding site141substrate
Binding site179Zn2+ 2 (UniProtKB | ChEBI)
Binding site224substrate
Active site252
Binding site252Zn2+ 1 (UniProtKB | ChEBI)
Binding site256substrate
Binding site268substrate

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functiondihydroorotase activity
Molecular Functionzinc ion binding
Biological Process'de novo' pyrimidine nucleobase biosynthetic process
Biological Process'de novo' UMP 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
      BC777_0323

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DSM 29128
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Rhodobacterales > Paracoccaceae > Yoonia

Accessions

  • Primary accession
    A0A2M8WKN3

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue104N6-carboxylysine

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain16-314Amidohydrolase-related

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    350
  • Mass (Da)
    38,610
  • Last updated
    2018-04-25 v1
  • Checksum
    D623BF87FD6D5856
MPDKHLTSLTIRRPDDWHLHLRDGEMLKAVLPETTRHFARAIIMPNLVPPVVTAEQAVAYRTRIMAAVPEGARFTPLMTLYLTEATDPEDVRAAHADAIATAVKLYPAGATTNSASGVRDFEKVRPVLEVMAEIGMPLCVHGEVTDSQIDIFDREAVFIEKVLKPLRKKVPDLKIVMEHVTTQNAVDYVRDSHKNMAATITTHHLIINRNHILAGGIKPHFYCLPVAKREAHRVALVQAAVSGDKRFFLGTDSAPHTDPLKLQACGCAGIFTAPNTMSCLAEVFDAAGRITKLEDFTSLNGPRFYGLPPNEETITLTKGAPVTYPEQIETGDGPVTVFDPGFDLHWRVEE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PGTY01000001
EMBL· GenBank· DDBJ
PJI91495.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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