P00363 · FRDA_ECOLI
- ProteinFumarate reductase flavoprotein subunit
- GenefrdA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids602 (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
Activity regulation
Inhibited by oxaloacetate, a substrate analog.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 12-16 | FAD (UniProtKB | ChEBI) | ||||
Sequence: GAGGA | ||||||
Binding site | 36-38 | FAD (UniProtKB | ChEBI) | ||||
Sequence: ISK | ||||||
Binding site | 44-52 | FAD (UniProtKB | ChEBI) | ||||
Sequence: SHTVAAEGG | ||||||
Binding site | 156-158 | FAD (UniProtKB | ChEBI) | ||||
Sequence: HFV | ||||||
Binding site | 192-193 | FAD (UniProtKB | ChEBI) | ||||
Sequence: AT | ||||||
Binding site | 212 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 233 | |||||
Sequence: H | ||||||
Active site | 249 | |||||
Sequence: R | ||||||
Binding site | 356-357 | FAD (UniProtKB | ChEBI) | ||||
Sequence: HY | ||||||
Binding site | 380 | FAD (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 391-397 | FAD (UniProtKB | ChEBI) | ||||
Sequence: RLGSNSL |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Cellular Component | plasma membrane fumarate reductase complex | |
Molecular Function | electron transfer activity | |
Molecular Function | FAD binding | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | succinate dehydrogenase (quinone) activity | |
Molecular Function | succinate dehydrogenase activity | |
Biological Process | anaerobic electron transport chain | |
Biological Process | anaerobic respiration | |
Biological Process | bacterial-type flagellum assembly | |
Biological Process | DNA damage response | |
Biological Process | fermentation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFumarate reductase flavoprotein subunit
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP00363
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Peripheral membrane protein
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
No anaerobic growth on glycerol fumarate medium.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 45 | Inactivates enzyme. | ||||
Sequence: H → R | ||||||
Mutagenesis | 45 | Decreased ability (greater than 70%) to reduce fumarate. | ||||
Sequence: H → S, C, or Y | ||||||
Mutagenesis | 131 | Increased cross-linking to SdhE, FrdA is slightly less flavinylated. | ||||
Sequence: K → M | ||||||
Mutagenesis | 177 | No longer forms cross-link to SdhE, FrdA is still flavinylated. | ||||
Sequence: M → A | ||||||
Mutagenesis | 178 | Decreased cross-linking to SdhE, FrdA is still flavinylated. | ||||
Sequence: E → A | ||||||
Mutagenesis | 207 | Increased cross-linking to SdhE, FrdA is flavinylated. | ||||
Sequence: G → M | ||||||
Mutagenesis | 233 | Severely affects succinate oxidation, decreases fumarate oxidation by 75%. | ||||
Sequence: H → S | ||||||
Mutagenesis | 240 | Increased cross-linking to SdhE, FrdA is flavinylated. | ||||
Sequence: S → M | ||||||
Mutagenesis | 248 | Does not inactivate enzyme. | ||||
Sequence: C → S or A | ||||||
Mutagenesis | 249 | Inactivates enzyme. | ||||
Sequence: R → H or L |
Chemistry
PTM/Processing
Features
Showing features for initiator methionine, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000158660 | 2-602 | Fumarate reductase flavoprotein subunit | |||
Sequence: QTFQADLAIVGAGGAGLRAAIAAAQANPNAKIALISKVYPMRSHTVAAEGGSAAVAQDHDSFEYHFHDTVAGGDWLCEQDVVDYFVHHCPTEMTQLELWGCPWSRRPDGSVNVRRFGGMKIERTWFAADKTGFHMLHTLFQTSLQFPQIQRFDEHFVLDILVDDGHVRGLVAMNMMEGTLVQIRANAVVMATGGAGRVYRYNTNGGIVTGDGMGMALSHGVPLRDMEFVQYHPTGLPGSGILMTEGCRGEGGILVNKNGYRYLQDYGMGPETPLGEPKNKYMELGPRDKVSQAFWHEWRKGNTISTPRGDVVYLDLRHLGEKKLHERLPFICELAKAYVGVDPVKEPIPVRPTAHYTMGGIETDQNCETRIKGLFAVGECSSVGLHGANRLGSNSLAELVVFGRLAGEQATERAATAGNGNEAAIEAQAAGVEQRLKDLVNQDGGENWAKIRDEMGLAMEEGCGIYRTPELMQKTIDKLAELQERFKRVRITDTSSVFNTDLLYTIELGHGLNVAECMAHSAMARKESRGAHQRLDEGCTERDDVNFLKHTLAFRDADGTTRLEYSDVKITTLPPAKRVYGGEADAADKAEAANKKEKANG | ||||||
Modified residue | 45 | Tele-8alpha-FAD histidine | ||||
Sequence: H |
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) (PubMed:10373108, PubMed:11850430).
Can be cross-linked to SdhE (PubMed:26644464).
Purified from membrane fractions associated with protoporphyrinogen IX dehydrogenase (hemG) (PubMed:20484676).
Can be cross-linked to SdhE (PubMed:26644464).
Purified from membrane fractions associated with protoporphyrinogen IX dehydrogenase (hemG) (PubMed:20484676).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P00363 | frdB P0AC47 | 4 | EBI-550480, EBI-906724 | |
BINARY | P00363 | hemG P0ACB4 | 2 | EBI-550480, EBI-1115706 | |
BINARY | P00363 | ydcZ P76111 | 2 | EBI-550480, EBI-550492 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 581-602 | Disordered | ||||
Sequence: YGGEADAADKAEAANKKEKANG | ||||||
Compositional bias | 583-602 | Basic and acidic residues | ||||
Sequence: GEADAADKAEAANKKEKANG |
Sequence similarities
Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length602
- Mass (Da)65,972
- Last updated2007-01-23 v3
- Checksum3306D7FF6E198AE9
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 386 | in Ref. 1; AAA23437 | ||||
Sequence: L → P | ||||||
Compositional bias | 583-602 | Basic and acidic residues | ||||
Sequence: GEADAADKAEAANKKEKANG |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J01611 EMBL· GenBank· DDBJ | AAA23437.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U14003 EMBL· GenBank· DDBJ | AAA97053.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC77114.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE78158.1 EMBL· GenBank· DDBJ | Genomic DNA |