P0AC47 · FRDB_ECOLI
- ProteinFumarate reductase iron-sulfur subunit
- GenefrdB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids244 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; fumarate reductase is used during anaerobic growth, and succinate dehydrogenase is used during aerobic growth. The QFR enzyme complex binds 2 quinones in or near the membrane; 1 near the [3Fe-4S] cluster (QP is proximal to the [3Fe-4S] cluster, on the cytoplasmic side of the membrane) while QD (the distal cluster) is on the other side of the membrane. It is not clear if both of the quinol-binding sites are functionally relevant (PubMed:10373108, PubMed:11850430).
Catalytic activity
- a quinone + succinate = a quinol + fumarate
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 [2Fe-2S] cluster.
Note: Binds 1 [3Fe-4S] cluster.
Note: Binds 1 [4Fe-4S] cluster.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 14 | a menaquinone (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 58 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 63 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 66 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 78 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 149 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 152 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 155 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 159 | [3Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 205 | [3Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 211 | [3Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 215 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 226-229 | a menaquinone (UniProtKB | ChEBI) | ||||
Sequence: QQGK |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | membrane | |
Cellular Component | plasma membrane fumarate reductase complex | |
Molecular Function | 2 iron, 2 sulfur cluster binding | |
Molecular Function | 3 iron, 4 sulfur cluster binding | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | electron transfer activity | |
Molecular Function | iron-sulfur cluster binding | |
Molecular Function | metal ion binding | |
Molecular Function | succinate dehydrogenase (quinone) activity | |
Biological Process | anaerobic electron transport chain | |
Biological Process | anaerobic respiration | |
Biological Process | bacterial-type flagellum assembly | |
Biological Process | fermentation | |
Biological Process | tricarboxylic acid cycle |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFumarate reductase iron-sulfur subunit
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP0AC47
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Peripheral membrane protein
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 58 | Affects center 1 (2Fe-2S). | ||||
Sequence: C → S | ||||||
Mutagenesis | 63 | Affects center 1 (2Fe-2S). | ||||
Sequence: C → S | ||||||
Mutagenesis | 66 | Affects center 1 (2Fe-2S). | ||||
Sequence: C → S | ||||||
Mutagenesis | 78 | Affects center 1 (2Fe-2S). | ||||
Sequence: C → S |
Chemistry
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000158698 | 2-244 | Fumarate reductase iron-sulfur subunit | |||
Sequence: AEMKNLKIEVVRYNPEVDTAPHSAFYEVPYDATTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFLRDYTDGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNSRTADQGTNIQTPAQMAKYHQFSGCINCGLCYAACPQFGLNPEFIGPAAITLAHRYNEDSRDHGKKERMAQLNSQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVESSKDFLIATLKPR |
Proteomic databases
Interaction
Subunit
Part of an enzyme complex containing four subunits: a flavoprotein (FrdA), an iron-sulfur protein (FrdB), and two hydrophobic anchor proteins (FrdC and FrdD).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P0AC47 | frdA P00363 | 4 | EBI-906724, EBI-550480 | |
BINARY | P0AC47 | mutT P08337 | 4 | EBI-906724, EBI-1121389 | |
BINARY | P0AC47 | ompW P0A915 | 2 | EBI-906724, EBI-1132929 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 16-97 | 2Fe-2S ferredoxin-type | ||||
Sequence: PEVDTAPHSAFYEVPYDATTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFLRDYTDGMKVEALANF | ||||||
Domain | 140-169 | 4Fe-4S ferredoxin-type | ||||
Sequence: MAKYHQFSGCINCGLCYAACPQFGLNPEFI |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length244
- Mass (Da)27,123
- Last updated2007-01-23 v2
- ChecksumAC1D7A73244D7AC0
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J01611 EMBL· GenBank· DDBJ | AAA23438.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U14003 EMBL· GenBank· DDBJ | AAA97052.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC77113.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE78157.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
V00277 EMBL· GenBank· DDBJ | CAA23534.1 EMBL· GenBank· DDBJ | Genomic DNA |