ID FRDB_ECOL6 STANDARD; PRT; 243 AA. AC P0AC48; P00364; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 07-FEB-2006, entry version 4. DE Fumarate reductase iron-sulfur protein (EC 1.3.99.1). GN Name=frdB; OrderedLocusNames=c5241; 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; AE016771; AAN83663.1; -; Genomic_DNA. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR001450; 4Fe4S_Fe_S_bd. DR InterPro; IPR004489; DhsB. DR InterPro; IPR001041; Ferredoxin. DR InterPro; IPR012675; Ferredoxin_fold. DR InterPro; IPR012285; Fum_reductase_C. DR Pfam; PF00111; Fer2; 1. DR Pfam; PF00037; Fer4; 1. DR PRINTS; PR00353; 4FE4SFRDOXIN. 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. 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 0 0 By similarity. FT CHAIN 1 243 Fumarate reductase iron-sulfur protein. FT /FTId=PRO_0000158700. FT DOMAIN 15 96 2Fe-2S ferredoxin-type. FT METAL 57 57 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 62 62 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 65 65 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 77 77 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 148 148 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 151 151 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 154 154 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 158 158 Iron-sulfur 3 (3Fe-4S) (By similarity). FT METAL 204 204 Iron-sulfur 3 (3Fe-4S) (By similarity). FT METAL 210 210 Iron-sulfur 3 (3Fe-4S) (By similarity). FT METAL 214 214 Iron-sulfur 2 (4Fe-4S) (By similarity). SQ SEQUENCE 243 AA; 26992 MW; 5C1D7A6CF0DF33D0 CRC64; AEMKNLKIEV VRYNPEVDTA PHSAFYEVPY DATTSLLDAL GYIKDNLAPD LSYRWSCRMA ICGSCGMMVN NVPKLACKTF LRDYTDGMKV EALANFPIER DLVVDMTHFI ESLEAIKPYI IGNSRTADQG TNIQTPAQMA KYHQFSGCIN CGLCYAACPQ FGLNPEFIGP AAITLAHRYN EDSRDHGKKE RMAQLNSQNG VWSCTFVGYC SEVCPKHVDP AAAIQQGKVE SSKDFLIATL KPR //