ID   SDHB_BACSU              Reviewed;         253 AA.
AC   P08066;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=Succinate dehydrogenase iron-sulfur subunit;
DE            EC=1.3.5.1;
GN   Name=sdhB; OrderedLocusNames=BSU28430;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / PY79;
RX   PubMed=3027051; DOI=10.1128/jb.169.2.864-873.1987;
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 complex.";
RL   J. Bacteriol. 169:864-873(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
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 subtilis
RT   chromosome containing genes responsible for stress responses, the
RT   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   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., 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., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., 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   PubMed=3114423; DOI=10.1099/00221287-132-11-3013;
RA   Cutting S.M., Mandelstam J.;
RT   "The nucleotide sequence and the transcription during sporulation of the
RT   gerE gene of Bacillus subtilis.";
RL   J. Gen. Microbiol. 132:3013-3024(1986).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + succinate = a quinol + fumarate;
CC         Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1;
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC       Note=Binds 1 [2Fe-2S] cluster.;
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC       Note=Binds 1 [3Fe-4S] cluster.;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 1 [4Fe-4S] cluster.;
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate
CC       from succinate (bacterial route): step 1/1.
CC   -!- SUBUNIT: In B.subtilis succinate dehydrogenase forms part of an enzyme
CC       complex containing three subunits: a flavoprotein, an iron-sulfur
CC       protein and cytochrome b-558.
CC   -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase
CC       iron-sulfur protein family. {ECO:0000305}.
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DR   EMBL; M13470; AAA22747.1; -; Genomic_DNA.
DR   EMBL; Z75208; CAA99548.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14803.1; -; Genomic_DNA.
DR   EMBL; M17642; AAA22471.1; -; Genomic_DNA.
DR   PIR; B27763; B27763.
DR   RefSeq; NP_390721.1; NC_000964.3.
DR   RefSeq; WP_003229569.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P08066; -.
DR   SMR; P08066; -.
DR   STRING; 224308.BSU28430; -.
DR   jPOST; P08066; -.
DR   PaxDb; 224308-BSU28430; -.
DR   DNASU; 937460; -.
DR   EnsemblBacteria; CAB14803; CAB14803; BSU_28430.
DR   GeneID; 937460; -.
DR   KEGG; bsu:BSU28430; -.
DR   PATRIC; fig|224308.179.peg.3088; -.
DR   eggNOG; COG0479; Bacteria.
DR   InParanoid; P08066; -.
DR   OrthoDB; 9804391at2; -.
DR   PhylomeDB; P08066; -.
DR   BioCyc; BSUB:BSU28430-MONOMER; -.
DR   BioCyc; MetaCyc:BSU28430-MONOMER; -.
DR   UniPathway; UPA00223; UER01005.
DR   Proteomes; UP000001570; Chromosome.
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 transfer activity; IEA:InterPro.
DR   GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR   GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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; 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   PANTHER; PTHR11921:SF29; SUCCINATE DEHYDROGENASE [UBIQUINONE] IRON-SULFUR SUBUNIT, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11921; SUCCINATE DEHYDROGENASE IRON-SULFUR PROTEIN; 1.
DR   Pfam; PF13085; Fer2_3; 1.
DR   Pfam; PF13183; Fer4_8; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 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; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; Oxidoreductase; Reference proteome; Transport;
KW   Tricarboxylic acid cycle.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..253
FT                   /note="Succinate dehydrogenase iron-sulfur subunit"
FT                   /id="PRO_0000158686"
FT   DOMAIN          146..174
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         64
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         69
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         155
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         158
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         212
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         218
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
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
//