A0A0X1TJT8 · A0A0X1TJT8_9FIRM
- ProteinDihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit
- GenepyrK
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids256 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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:
Note: Binds 1 FAD per subunit.
Note: Binds 1 [2Fe-2S] cluster per subunit.
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 53-56 | FAD (UniProtKB | ChEBI) | ||||
Sequence: RPIS | ||||||
Binding site | 70-72 | FAD (UniProtKB | ChEBI) | ||||
Sequence: IYR | ||||||
Binding site | 77-78 | FAD (UniProtKB | ChEBI) | ||||
Sequence: GT | ||||||
Binding site | 222 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 227 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 230 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 243 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 2 iron, 2 sulfur cluster binding | |
Molecular Function | electron transfer activity | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | metal ion binding | |
Molecular Function | oxidoreductase activity | |
Biological Process | 'de novo' UMP biosynthetic process |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Erysipelotrichia > Erysipelotrichales > Turicibacteraceae > Turicibacter
Accessions
- Primary accessionA0A0X1TJT8
Proteomes
Interaction
Subunit
Heterotetramer of 2 PyrK and 2 PyrD type B subunits.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-102 | FAD-binding FR-type | ||||
Sequence: RKVQNMTVVSQKLIAKNVYEIILSGNLVQGMLQAGQFVNIKINEVAYPLLRRPISICEINQELNQFKMIYRAEGEGTKLLSQKQAGEQVDILGPLGTGFDI |
Sequence similarities
Belongs to the PyrK family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length256
- Mass (Da)28,169
- Last updated2016-04-13 v1
- Checksum5DE55CE4FED7420C
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP013476 EMBL· GenBank· DDBJ | AMC08349.1 EMBL· GenBank· DDBJ | Genomic DNA |