Q251Y8 · Q251Y8_DESHY
- ProteinPyruvate:ferredoxin oxidoreductase
- GeneporA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1176 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
Catalytic activity
- CoA + 2 oxidized [2Fe-2S]-[ferredoxin] + pyruvate = acetyl-CoA + CO2 + H+ + 2 reduced [2Fe-2S]-[ferredoxin]
Cofactor
Note: Binds 3 [4Fe-4S] clusters per subunit.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 30 | pyruvate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Site | 30 | Important for catalytic activity | ||||
Sequence: T | ||||||
Binding site | 63 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Site | 63 | Important for catalytic activity | ||||
Sequence: E | ||||||
Binding site | 113 | pyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Site | 113 | Important for catalytic activity | ||||
Sequence: R | ||||||
Binding site | 691 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 694 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 697 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 701 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 747 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 750 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 753 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 757 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 814 | [4Fe-4S] cluster 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 817 | [4Fe-4S] cluster 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 819 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 842 | [4Fe-4S] cluster 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 842 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 966-969 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: GDGW | ||||||
Binding site | 995-1000 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: TEVYSN | ||||||
Site | 1000 | Important for catalytic activity | ||||
Sequence: N | ||||||
Binding site | 1075 | [4Fe-4S] cluster 3 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | iron ion binding | |
Molecular Function | pyruvate synthase activity | |
Molecular Function | thiamine pyrophosphate binding | |
Biological Process | electron transport chain |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePyruvate:ferredoxin oxidoreductase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Desulfitobacteriaceae > Desulfitobacterium
Accessions
- Primary accessionQ251Y8
Proteomes
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 682-711 | 4Fe-4S ferredoxin-type | ||||
Sequence: IVPEWDVEKCIQCNQCSYVCPHAAIRPFLL | ||||||
Domain | 738-769 | 4Fe-4S ferredoxin-type | ||||
Sequence: LRVQVSPLDCTGCGNCAEVCPAKGKALVMKDA |
Sequence similarities
Belongs to the pyruvate:ferredoxin/flavodoxin oxidoreductase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,176
- Mass (Da)127,871
- Last updated2006-04-18 v1
- Checksum620C2D3403366739
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP008230 EMBL· GenBank· DDBJ | BAE81904.1 EMBL· GenBank· DDBJ | Genomic DNA |