ID DHSB_SALTY Reviewed; 238 AA. AC Q8ZQU2; DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 06-JUN-2002, sequence version 2. DT 25-NOV-2008, entry version 49. DE RecName: Full=Succinate dehydrogenase iron-sulfur subunit; DE EC=1.3.99.1; GN Name=sdhB; OrderedLocusNames=STM0735; OS Salmonella typhimurium. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=602; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX MEDLINE=21534948; PubMed=11677609; DOI=10.1038/35101614; RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., RA Waterston R., Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium RT LT2."; RL Nature 413:852-856(2001). 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. CC -!- COFACTOR: Binds 1 3Fe-4S cluster. CC -!- COFACTOR: Binds 1 4Fe-4S cluster. CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle. CC -!- SUBUNIT: Part of an enzyme complex containing four subunits: a CC flavoprotein, an iron-sulfur, cytochrome b-556, and an hydrophobic CC anchor protein (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 ferredoxin-type domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE008730; AAL19679.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_459720.1; -. DR HSSP; P07014; 1NEK. DR SMR; Q8ZQU2; 1-238. DR GeneID; 1252255; -. DR GenomeReviews; AE006468_GR; STM0735. DR KEGG; stm:STM0735; -. DR StyGene; SG?????; sdhB. DR HOGENOM; Q8ZQU2; -. DR BioCyc; STYP99287:STM0735-MON; -. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. DR GO; GO:0000104; F:succinate dehydrogenase activity; IEA:EC. DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR001450; 4Fe4S_Fe_S_bd. DR InterPro; IPR012675; b-grasp_ferredoxin-like. DR InterPro; IPR001041; Ferredoxin. DR InterPro; IPR012285; Fum_reductase_C. DR InterPro; IPR004489; Succ_DHase/fum_Rdtase_Fe-S. DR Gene3D; G3DSA:3.10.20.30; Ferredoxin_fold; 1. DR Gene3D; G3DSA:1.10.1060.10; Fum_reductase_C; 1. DR TIGRFAMs; TIGR00384; dhsB; 1. DR PROSITE; PS00197; 2FE2S_FER_1; FALSE_NEG. 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; Complete proteome; Electron transport; Iron; KW Iron-sulfur; Metal-binding; Oxidoreductase; Transport; KW Tricarboxylic acid cycle. FT CHAIN 1 238 Succinate dehydrogenase iron-sulfur FT subunit. FT /FTId=PRO_0000158692. FT DOMAIN 1 97 2Fe-2S ferredoxin-type. FT DOMAIN 139 169 4Fe-4S ferredoxin-type. FT METAL 55 55 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 60 60 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 63 63 Iron-sulfur 1 (2Fe-2S) (Potential). FT METAL 75 75 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 206 206 Iron-sulfur 3 (3Fe-4S) (By similarity). FT METAL 212 212 Iron-sulfur 3 (3Fe-4S) (By similarity). FT METAL 216 216 Iron-sulfur 2 (4Fe-4S) (By similarity). SQ SEQUENCE 238 AA; 26733 MW; 7628F9F9F95611F3 CRC64; MKLEFSIYRY NPDVDNAPRM QDYTLEGEEG RDMMLLDALI QLKEKDPSLS FRRSCREGVC GSDGLNMNGK NGLACITPIS ALTQPGKKIV IRPLPGLPVI RDLVVDMGQF YAQYEKIKPY LLNNGQNPPA REHLQMPEQR EKLDGLYECI LCACCSTSCP SFWWNPDKFI GPAGLLAAYR FLIDSRDTET DSRLEGMSDA FSVFRCHSIM NCVSVCPKGL NPTRAIGHIK SMLLQRSA //