UniProt functional annotation for P00363



	UniProt functional annotation for P00363

UniProt code: P00363.

Organism: Escherichia coli (strain K12).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.

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). {ECO:0000269|PubMed:10373108, ECO:0000269|PubMed:11850430, ECO:0000269|PubMed:24374335}.

Catalytic activity: Reaction=a quinone + succinate = a quinol + fumarate; Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.4; Evidence={ECO:0000269|PubMed:11850430};

Catalytic activity: Reaction=a menaquinone + succinate = a menaquinol + fumarate; Xref=Rhea:RHEA:27834, Rhea:RHEA-COMP:9537, Rhea:RHEA-COMP:9539, ChEBI:CHEBI:16374, ChEBI:CHEBI:18151, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031; EC=1.3.5.4; Evidence={ECO:0000305|PubMed:10373108};

Cofactor: Name=FAD; Xref=ChEBI:CHEBI:57692; Note=Binds 1 FAD covalently per subunit (PubMed:24374335, PubMed:26644464, PubMed:10373108). Flavinylated by SdhE, about 5% flavinylation occurs in the absence of SdhE (PubMed:24374335, PubMed:26644464). {ECO:0000269|PubMed:10373108, ECO:0000269|PubMed:24374335, ECO:0000269|PubMed:26644464};

Activity regulation: Inhibited by oxaloacetate, a substrate analog. {ECO:0000269|PubMed:10373108}.

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). {ECO:0000269|PubMed:10373108, ECO:0000269|PubMed:11850430, ECO:0000269|PubMed:20484676, ECO:0000269|PubMed:26644464, ECO:0000305|PubMed:26644464}.

Subcellular location: Cell inner membrane {ECO:0000305|PubMed:10373108, ECO:0000305|PubMed:20484676}; Peripheral membrane protein {ECO:0000305|PubMed:10373108}; Cytoplasmic side {ECO:0000305|PubMed:10373108}.

Disruption phenotype: No anaerobic growth on glycerol fumarate medium. {ECO:0000269|PubMed:24374335}.

Similarity: Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



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). {ECO:0000269\|PubMed:10373108, ECO:0000269\|PubMed:11850430, ECO:0000269\|PubMed:24374335}.


Catalytic activity:		Reaction=a quinone + succinate = a quinol + fumarate; Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.4; Evidence={ECO:0000269\|PubMed:11850430};
Catalytic activity:		Reaction=a menaquinone + succinate = a menaquinol + fumarate; Xref=Rhea:RHEA:27834, Rhea:RHEA-COMP:9537, Rhea:RHEA-COMP:9539, ChEBI:CHEBI:16374, ChEBI:CHEBI:18151, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031; EC=1.3.5.4; Evidence={ECO:0000305\|PubMed:10373108};
Cofactor:		Name=FAD; Xref=ChEBI:CHEBI:57692; Note=Binds 1 FAD covalently per subunit (PubMed:24374335, PubMed:26644464, PubMed:10373108). Flavinylated by SdhE, about 5% flavinylation occurs in the absence of SdhE (PubMed:24374335, PubMed:26644464). {ECO:0000269\|PubMed:10373108, ECO:0000269\|PubMed:24374335, ECO:0000269\|PubMed:26644464};
Activity regulation:		Inhibited by oxaloacetate, a substrate analog. {ECO:0000269\|PubMed:10373108}.
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). {ECO:0000269\|PubMed:10373108, ECO:0000269\|PubMed:11850430, ECO:0000269\|PubMed:20484676, ECO:0000269\|PubMed:26644464, ECO:0000305\|PubMed:26644464}.
Subcellular location:		Cell inner membrane {ECO:0000305\|PubMed:10373108, ECO:0000305\|PubMed:20484676}; Peripheral membrane protein {ECO:0000305\|PubMed:10373108}; Cytoplasmic side {ECO:0000305\|PubMed:10373108}.
Disruption phenotype:		No anaerobic growth on glycerol fumarate medium. {ECO:0000269\|PubMed:24374335}.
Similarity:		Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. {ECO:0000305}.