A0A0X1TJT8 · A0A0X1TJT8_9FIRM

  • Protein
    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 site53-56FAD (UniProtKB | ChEBI)
Binding site70-72FAD (UniProtKB | ChEBI)
Binding site77-78FAD (UniProtKB | ChEBI)
Binding site222[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site227[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site230[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site243[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
    Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit
  • Alternative names
    • Dihydroorotate oxidase B, electron transfer subunit

Gene names

    • Name
      pyrK
    • ORF names
      AT726_05000

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • H121
  • Taxonomic lineage
    Bacteria > Bacillota > Erysipelotrichia > Erysipelotrichales > Turicibacteraceae > Turicibacter

Accessions

  • Primary accession
    A0A0X1TJT8

Proteomes

Interaction

Subunit

Heterotetramer of 2 PyrK and 2 PyrD type B subunits.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-102FAD-binding FR-type

Sequence similarities

Belongs to the PyrK family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    256
  • Mass (Da)
    28,169
  • Last updated
    2016-04-13 v1
  • Checksum
    5DE55CE4FED7420C
MRKVQNMTVVSQKLIAKNVYEIILSGNLVQGMLQAGQFVNIKINEVAYPLLRRPISICEINQELNQFKMIYRAEGEGTKLLSQKQAGEQVDILGPLGTGFDIEDVQANETVVLVGGGIGVPPMYEMAKRLHAKGNKVIAVLGFASSVDVFYEEEFKAYADVYITTMDGSHGYKGNVVELINAKQLNFDWIYGCGPKVMLKAIDEQFGQTKKGYLSFEERMACGIGACYACVCQLNSGKMARVCKEGPVFKLGEVAL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP013476
EMBL· GenBank· DDBJ
AMC08349.1
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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp