P0AC48 · FRDB_ECOL6
- ProteinFumarate reductase iron-sulfur subunit
- GenefrdB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids244 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth.
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 | plasma membrane | |
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 | metal ion binding | |
Molecular Function | succinate dehydrogenase (quinone) activity | |
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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP0AC48
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000158700 | 2-244 | Fumarate reductase iron-sulfur subunit | |||
Sequence: AEMKNLKIEVVRYNPEVDTAPHSAFYEVPYDATTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFLRDYTDGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNSRTADQGTNIQTPAQMAKYHQFSGCINCGLCYAACPQFGLNPEFIGPAAITLAHRYNEDSRDHGKKERMAQLNSQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVESSKDFLIATLKPR |
Interaction
Subunit
Fumarate dehydrogenase forms part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur, and two hydrophobic anchor proteins.
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 | |
---|---|---|---|---|
AE014075 EMBL· GenBank· DDBJ | AAN83663.1 EMBL· GenBank· DDBJ | Genomic DNA |