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 24-JUL-2007, entry version 17. DE Fumarate reductase iron-sulfur subunit (EC 1.3.99.1). GN Name=frdB; OrderedLocusNames=c_5241; OS Escherichia coli O6. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=217992; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC; RX MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799; RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., RA Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., RA Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., RA Mobley H.L.T., Donnenberg M.S., Blattner F.R.; RT "Extensive mosaic structure revealed by the complete genome sequence RT of 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 CC growth, and the succinate dehydrogenase is used in aerobic growth CC (By similarity). CC -!- CATALYTIC ACTIVITY: Succinate + acceptor = fumarate + reduced CC acceptor. CC -!- COFACTOR: Binds 1 2Fe-2S cluster (By similarity). CC -!- COFACTOR: Binds 1 3Fe-4S cluster (By similarity). CC -!- COFACTOR: Binds 1 4Fe-4S cluster (By similarity). 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 (By similarity). CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate CC reductase iron-sulfur protein family. CC -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain. CC -!- SIMILARITY: Contains 1 4Fe-4S type ferredoxin domain. 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 SMR; P0AC48; 2-244. DR GenomeReviews; AE014075_GR; c_5241. DR KEGG; ecc:c5241; -. DR GO; GO:0000104; F:succinate dehydrogenase activity; IEA:EC. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR001450; 4Fe4S_Fe_S_bd. DR InterPro; IPR012675; b-grasp_ferredoxin-like. DR InterPro; IPR004489; DhsB. DR InterPro; IPR001041; Ferredoxin. DR InterPro; IPR012285; Fum_reductase_C. DR Gene3D; G3DSA:3.10.20.30; Ferredoxin_fold; 1. DR Gene3D; G3DSA:1.10.1060.10; Fum_reductase_C; 1. DR Pfam; PF00111; Fer2; 1. DR Pfam; PF00037; Fer4; 1. DR PIRSF; PIRSF000176; FRD_IP; 1. DR TIGRFAMs; TIGR00384; dhsB; 1. DR PROSITE; PS00197; 2FE2S_FER_1; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS00198; 4FE4S_FERREDOXIN; 1. PE 3: Inferred from homology; KW 2Fe-2S; 3Fe-4S; 4Fe-4S; Complete proteome; Electron transport; Iron; KW Iron-sulfur; Metal-binding; Oxidoreductase; Transport; KW Tricarboxylic acid cycle. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 244 Fumarate reductase iron-sulfur subunit. FT /FTId=PRO_0000158700. FT DOMAIN 16 97 2Fe-2S ferredoxin-type. FT METAL 58 58 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 63 63 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 66 66 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 78 78 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 149 149 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 152 152 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 155 155 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 159 159 Iron-sulfur 3 (3Fe-4S) (By similarity). FT METAL 205 205 Iron-sulfur 3 (3Fe-4S) (By similarity). FT METAL 211 211 Iron-sulfur 3 (3Fe-4S) (By similarity). FT METAL 215 215 Iron-sulfur 2 (4Fe-4S) (By similarity). 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 //