ID DHSB_BACSU Reviewed; 253 AA. AC P08066; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 04-NOV-2008, entry version 83. DE RecName: Full=Succinate dehydrogenase iron-sulfur subunit; DE EC=1.3.99.1; GN Name=sdhB; OrderedLocusNames=BSU28430; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168 / PY79; RX MEDLINE=87109084; PubMed=3027051; RA Phillips M.K., Hederstedt L., Hasnain S., Rutberg L., Guest J.R.; RT "Nucleotide sequence encoding the flavoprotein and iron-sulfur protein RT subunits of the Bacillus subtilis PY79 succinate dehydrogenase RT complex."; RL J. Bacteriol. 169:864-873(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=97124191; PubMed=8969504; RA Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J., RA Emmerson P.T., Harwood C.R.; RT "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus RT subtilis chromosome containing genes responsible for stress responses, RT the utilization of plant cell walls and primary metabolism."; RL Microbiology 142:3067-3078(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 112-253. RX MEDLINE=87310370; PubMed=3114423; RA Cutting S.M., Mandelstam J.; RT "The nucleotide sequence and the transcription during sporulation of RT the gerE gene of Bacillus subtilis."; RL J. Gen. Microbiol. 132:3013-3024(1986). 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: In B.subtilis succinate dehydrogenase forms part of an CC enzyme complex containing three subunits: a flavoprotein, an iron- CC sulfur protein and cytochrome b-558. CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate CC reductase iron-sulfur protein family. 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; M13470; AAA22747.1; -; Genomic_DNA. DR EMBL; Z75208; CAA99548.1; -; Genomic_DNA. DR EMBL; Z99118; CAB14803.1; -; Genomic_DNA. DR EMBL; M17642; AAA22471.1; -; Genomic_DNA. DR PIR; B27763; B27763. DR RefSeq; NP_390721.1; -. DR HSSP; P17596; 1QLA. DR GeneID; 937460; -. DR GenomeReviews; AL009126_GR; BSU28430. DR KEGG; bsu:BSU28430; -. DR NMPDR; fig|224308.1.peg.2846; -. DR SubtiList; BG10353; sdhB. DR HOGENOM; P08066; -. DR BioCyc; BSUB224308:BSU2839-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: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 InterPro; IPR001450; 4Fe4S_Fe_S_bd. DR InterPro; IPR012675; b-grasp_ferredoxin-like. 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 Pfam; PF00037; Fer4; 1. DR TIGRFAMs; TIGR00384; dhsB; 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 INIT_MET 1 1 Removed. FT CHAIN 2 253 Succinate dehydrogenase iron-sulfur FT subunit. FT /FTId=PRO_0000158686. FT DOMAIN 146 174 4Fe-4S ferredoxin-type. FT METAL 64 64 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 69 69 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 72 72 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 84 84 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 155 155 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 158 158 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 161 161 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 165 165 Iron-sulfur 3 (3Fe-4S) (By similarity). FT METAL 212 212 Iron-sulfur 3 (3Fe-4S) (By similarity). FT METAL 218 218 Iron-sulfur 3 (3Fe-4S) (By similarity). FT METAL 222 222 Iron-sulfur 2 (4Fe-4S) (By similarity). SQ SEQUENCE 253 AA; 28418 MW; C20E095CDD960B3E CRC64; MSEQKTIRFI ITRQDTADST PYDEEFEIPY RPNLNVISAL MEIRRNPVNV KGEKTTPVTW DMNCLEEVCG ACSMVINGKP RQSCTALIDQ LEQPIRLKPM KTFPVVRDLQ VDRSRMFDSL KKVKAWIPID GTYDLGPGPR MPEKRRQWAY ELSKCMTCGV CLEACPNVNS KSKFMGPAPM SQVRLFNAHP TGAMNKSERL EALMDEGGLA DCGNSQNCVQ SCPKGIPLTT SIAALNRDTN LQAFRNFFGS DRV //