ID FRDB_ECOL6 Reviewed; 244 AA. AC P0AC48; P00364; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 04-NOV-2026, entry version 118. DE RecName: Full=Fumarate reductase iron-sulfur subunit; DE EC=1.3.5.1 {ECO:0000250|UniProtKB:P0AC47}; DE AltName: Full=Quinol-fumarate reductase iron-sulfur subunit; DE Short=QFR iron-sulfur subunit; GN Name=frdB; OrderedLocusNames=c5241; OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=199310; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CFT073 / ATCC 700928 / UPEC; RX PubMed=12471157; DOI=10.1073/pnas.252529799; RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., RA Donnenberg M.S., Blattner F.R.; RT "Extensive mosaic structure revealed by the complete genome sequence of RT uropathogenic Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002). CC -!- FUNCTION: Two distinct, membrane-bound, FAD-containing enzymes are CC responsible for the catalysis of fumarate and succinate CC interconversion; the fumarate reductase is used in anaerobic growth, CC and the succinate dehydrogenase is used in aerobic growth. CC {ECO:0000250|UniProtKB:P0AC47}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a quinone + succinate = fumarate + a quinol; CC Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806, CC ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1; CC Evidence={ECO:0000250|UniProtKB:P0AC47}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a menaquinone + succinate = a menaquinol + fumarate; CC Xref=Rhea:RHEA:27834, Rhea:RHEA-COMP:9537, Rhea:RHEA-COMP:9539, CC ChEBI:CHEBI:16374, ChEBI:CHEBI:18151, ChEBI:CHEBI:29806, CC ChEBI:CHEBI:30031; EC=1.3.5.1; CC Evidence={ECO:0000250|UniProtKB:P0AC47}; CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; CC Evidence={ECO:0000250|UniProtKB:P0AC47}; CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250|UniProtKB:P0AC47}; CC -!- COFACTOR: CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; CC Evidence={ECO:0000250|UniProtKB:P0AC47}; CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250|UniProtKB:P0AC47}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250|UniProtKB:P0AC47}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P0AC47}; CC -!- SUBUNIT: Fumarate dehydrogenase forms part of an enzyme complex CC containing four subunits: a flavoprotein, an iron-sulfur, and two CC hydrophobic anchor proteins. {ECO:0000250|UniProtKB:P0AC47}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000250|UniProtKB:P0AC47}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:P0AC47}; Cytoplasmic side CC {ECO:0000250|UniProtKB:P0AC47}. CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase CC iron-sulfur protein family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE014075; AAN83663.1; -; Genomic_DNA. DR RefSeq; WP_000829498.1; NC_004431.1. DR AlphaFoldDB; P0AC48; -. DR SMR; P0AC48; -. DR STRING; 199310.c5241; -. DR GeneID; 67175179; -. DR GeneID; 93777669; -. DR KEGG; ecc:c5241; -. DR eggNOG; COG0479; Bacteria. DR HOGENOM; CLU_044838_3_2_6; -. DR OMA; AACKNRS; -. DR BioCyc; ECOL199310:C5241-MONOMER; -. DR Proteomes; UP000001410; Chromosome. DR AbasyAtlas; P0AC48; -. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro. DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro. DR GO; GO:0008177; F:succinate dehydrogenase (quinone) activity; ISS:UniProtKB. DR GO; GO:0009061; P:anaerobic respiration; IEA:TreeGrafter. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR FunFam; 1.10.1060.10:FF:000002; Succinate dehydrogenase iron-sulfur subunit; 1. DR FunFam; 3.10.20.30:FF:000009; Succinate dehydrogenase iron-sulfur subunit; 1. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1. DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR012675; Beta-grasp_dom_sf. DR InterPro; IPR009051; Helical_ferredxn. DR InterPro; IPR004489; Succ_DH/fum_Rdtase_Fe-S. DR InterPro; IPR025192; Succ_DH/fum_Rdtase_N. DR NCBIfam; TIGR00384; dhsB; 1. DR NCBIfam; NF009051; PRK12385.1; 1. DR NCBIfam; NF004616; sdhB; 1. DR PANTHER; PTHR43551; FUMARATE REDUCTASE IRON-SULFUR SUBUNIT; 1. DR PANTHER; PTHR43551:SF2; FUMARATE REDUCTASE IRON-SULFUR SUBUNIT; 1. DR Pfam; PF13085; Fer2_3; 1. DR Pfam; PF13237; Fer4_10; 1. DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1. DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1. DR PROSITE; PS00197; 2FE2S_FER_1; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 1. PE 3: Inferred from homology; KW 2Fe-2S; 3Fe-4S; 4Fe-4S; Cell inner membrane; Cell membrane; KW Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; KW Oxidoreductase; Reference proteome; Transport; Tricarboxylic acid cycle. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P0AC47" FT CHAIN 2..244 FT /note="Fumarate reductase iron-sulfur subunit" FT /id="PRO_0000158700" FT DOMAIN 16..97 FT /note="2Fe-2S ferredoxin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465" FT DOMAIN 140..169 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 14 FT /ligand="a menaquinone" FT /ligand_id="ChEBI:CHEBI:16374" FT /evidence="ECO:0000250|UniProtKB:P0AC47" FT BINDING 58 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250|UniProtKB:P0AC47" FT BINDING 63 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250|UniProtKB:P0AC47" FT BINDING 66 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250|UniProtKB:P0AC47" FT BINDING 78 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250|UniProtKB:P0AC47" FT BINDING 149 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250|UniProtKB:P0AC47" FT BINDING 152 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250|UniProtKB:P0AC47" FT BINDING 155 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250|UniProtKB:P0AC47" FT BINDING 159 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT /evidence="ECO:0000250|UniProtKB:P0AC47" FT BINDING 205 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT /evidence="ECO:0000250|UniProtKB:P0AC47" FT BINDING 211 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT /evidence="ECO:0000250|UniProtKB:P0AC47" FT BINDING 215 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250|UniProtKB:P0AC47" FT BINDING 226..229 FT /ligand="a menaquinone" FT /ligand_id="ChEBI:CHEBI:16374" FT /evidence="ECO:0000250|UniProtKB:P0AC47" SQ SEQUENCE 244 AA; 27123 MW; AC1D7A73244D7AC0 CRC64; MAEMKNLKIE VVRYNPEVDT APHSAFYEVP YDATTSLLDA LGYIKDNLAP DLSYRWSCRM AICGSCGMMV NNVPKLACKT FLRDYTDGMK VEALANFPIE RDLVVDMTHF IESLEAIKPY IIGNSRTADQ GTNIQTPAQM AKYHQFSGCI NCGLCYAACP QFGLNPEFIG PAAITLAHRY NEDSRDHGKK ERMAQLNSQN GVWSCTFVGY CSEVCPKHVD PAAAIQQGKV ESSKDFLIAT LKPR //