A0A0E3LIN0 · A0A0E3LIN0_9EURY

  • Protein
    Probable dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit
  • Gene
    pyrK
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Responsible for channeling the electrons from the oxidation of dihydroorotate from the FMN redox center in the PyrD type B subunit to the ultimate electron acceptor NAD+.

Cofactor

Protein has several cofactor binding sites:
FAD (UniProtKB | Rhea| CHEBI:57692 )

Note: Binds 1 FAD per subunit.
[2Fe-2S] cluster (UniProtKB | Rhea| CHEBI:190135 )

Note: Binds 1 [2Fe-2S] cluster per subunit.
[2Fe-2S] cluster (UniProtKB | Rhea| CHEBI:190135 )

Note: Binds 1 [2Fe-2S] cluster per subunit.

Pathway

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

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site211[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site216[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site219[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site229[2Fe-2S] cluster (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Function2 iron, 2 sulfur cluster binding
Molecular Functionelectron transfer activity
Molecular Functionflavin adenine dinucleotide binding
Molecular Functionmetal ion binding
Molecular Functionoxidoreductase activity
Biological Process'de novo' UMP biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Probable dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit
  • Alternative names
    • Dihydroorotate oxidase B, electron transfer subunit

Gene names

    • Name
      pyrK
    • ORF names
      MSKOL_0529

Organism names

  • Taxonomic identifier
  • Strain
    • Kolksee
  • Taxonomic lineage
    Archaea > Euryarchaeota > Stenosarchaea group > Methanomicrobia > Methanosarcinales > Methanosarcinaceae > Methanosarcina

Accessions

  • Primary accession
    A0A0E3LIN0

Proteomes

Interaction

Subunit

Heterotetramer of 2 PyrK and 2 PyrD type B subunits.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-89FAD-binding FR-type

Sequence similarities

Belongs to the PyrK family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    259
  • Mass (Da)
    28,025
  • Last updated
    2015-06-24 v1
  • Checksum
    E5912688DBEF8F12
MLPLNATILKIDEESPSIRTFFFDFQFETMNPGQFVMVWVRGVDEVPMGLSSKNSITVQKVGEATSKLFELKEGDSFGLRGPYGKGFSLPSEGEKTLVIAGGVGAAPLVPYAEAARSAGSEVHTVLGARSAGDLLFEKRFAEAGEVYISTDDGSKGTKGFVTDVLNSLNLSVYDKIAVCGPEIMMASVFRLLEDREVLDKSEFSLHRYFKCGIGVCGACCIDKSGLRVCRDGPVFSGVQLMDSELGKYTRDASGRRVKI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP009524
EMBL· GenBank· DDBJ
AKB46306.1
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.
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