B6JL11 · PYRD_HELP2

Function

function

Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.

Catalytic activity

Cofactor

FMN (UniProtKB | Rhea| CHEBI:58210 )

Note: Binds 1 FMN per subunit.

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.

Features

Showing features for binding site, active site.

135150100150200250300350
TypeIDPosition(s)Description
Binding site67-71FMN (UniProtKB | ChEBI)
Binding site71substrate
Binding site91FMN (UniProtKB | ChEBI)
Binding site116-120substrate
Binding site145FMN (UniProtKB | ChEBI)
Binding site178FMN (UniProtKB | ChEBI)
Binding site178substrate
Active site181Nucleophile
Binding site183substrate
Binding site214FMN (UniProtKB | ChEBI)
Binding site242FMN (UniProtKB | ChEBI)
Binding site243-244substrate
Binding site262FMN (UniProtKB | ChEBI)
Binding site291FMN (UniProtKB | ChEBI)
Binding site312-313FMN (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentplasma membrane
Molecular Functiondihydroorotate dehydrogenase (quinone) activity
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
    Dihydroorotate dehydrogenase (quinone)
  • EC number
  • Alternative names
    • DHOdehase
      (DHOD
      ; DHODase
      )
    • Dihydroorotate oxidase

Gene names

    • Name
      pyrD
    • Ordered locus names
      HPP12_0432

Organism names

Accessions

  • Primary accession
    B6JL11

Proteomes

Subcellular Location

Cell membrane
; Peripheral membrane protein

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10001002661-351Dihydroorotate dehydrogenase (quinone)

Interaction

Subunit

Monomer.

Structure

Family & Domains

Sequence similarities

Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    351
  • Mass (Da)
    38,947
  • Last updated
    2008-12-16 v1
  • Checksum
    9FC5BC960667394F
MLYSLLKKYLFSLDAEDAHEKVCKILKMLSSSPFLCNLIDSQWGYKNPKLENEILGLHFPNPLGLAAGFDKNASMLRALIAFGFGYLEAGTLTNEAQMGNERPRLFRHIEEESLQNAMGFNNHGAVLGVRSFKHFAPYKTPIGINLGKNKHIEQAHALEDYKAVLNKCLNIGDYYTFNLSSPNTPNLRDLQNKAFVNELFCMAKEMTHKPLFLKIAPDLETDDMLEIVNSAIGAGAHGIIATNTTIDKSLVFAPKEMGGLSGKCLTKKSREIFKELAKAFFNQSVLVSVGGISDAKEAYERIKMGASLLQIYSAFIYNGPNLCQNILKDLVKLLQKDGFLSVKEAIGADLR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001217
EMBL· GenBank· DDBJ
ACJ07589.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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