ID SDHB_ECOLI Reviewed; 238 AA. AC P07014; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1988, sequence version 1. DT 24-JAN-2024, entry version 201. DE RecName: Full=Succinate dehydrogenase iron-sulfur subunit; DE EC=1.3.5.1; GN Name=sdhB; OrderedLocusNames=b0724, JW0714; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX PubMed=6388571; DOI=10.1042/bj2230507; RA Darlison M.G., Guest J.R.; RT "Nucleotide sequence encoding the iron-sulphur protein subunit of the RT succinate dehydrogenase of Escherichia coli."; RL Biochem. J. 223:507-517(1984). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=8905232; DOI=10.1093/dnares/3.3.137; RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H., RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., RA Horiuchi T.; RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to RT the 12.7-28.0 min region on the linkage map."; RL DNA Res. 3:137-155(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 231-238. RX PubMed=6376123; DOI=10.1111/j.1432-1033.1984.tb08199.x; RA Darlison M.G., Spencer M.E., Guest J.R.; RT "Nucleotide sequence of the sucA gene encoding the 2-oxoglutarate RT dehydrogenase of Escherichia coli K12."; RL Eur. J. Biochem. 141:351-359(1984). RN [6] RP PROTEIN SEQUENCE OF 1-11. RC STRAIN=K12 / EMG2; RX PubMed=9298646; DOI=10.1002/elps.1150180807; RA Link A.J., Robison K., Church G.M.; RT "Comparing the predicted and observed properties of proteins encoded in the RT genome of Escherichia coli K-12."; RL Electrophoresis 18:1259-1313(1997). RN [7] RP SUBUNIT, AND SUBCELLULAR LOCATION. RC STRAIN=BL21-DE3; RX PubMed=16079137; DOI=10.1074/jbc.m506479200; RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., RA von Heijne G., Daley D.O.; RT "Protein complexes of the Escherichia coli cell envelope."; RL J. Biol. Chem. 280:34409-34419(2005). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR CLUSTERS RP AND UBIQUINONE, COFACTOR, AND SUBUNIT. RX PubMed=12560550; DOI=10.1126/science.1079605; RA Yankovskaya V., Horsefield R., Toernroth S., Luna-Chavez C., Miyoshi H., RA Leger C., Byrne B., Cecchini G., Iwata S.; RT "Architecture of succinate dehydrogenase and reactive oxygen species RT generation."; RL Science 299:700-704(2003). RN [9] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR CLUSTERS, RP COFACTOR, AND SUBUNIT. RX PubMed=16407191; DOI=10.1074/jbc.m508173200; RA Horsefield R., Yankovskaya V., Sexton G., Whittingham W., Shiomi K., RA Omura S., Byrne B., Cecchini G., Iwata S.; RT "Structural and computational analysis of the quinone-binding site of RT complex II (succinate-ubiquinone oxidoreductase): a mechanism of electron RT transfer and proton conduction during ubiquinone reduction."; RL J. Biol. Chem. 281:7309-7316(2006). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR CLUSTERS, RP COFACTOR, AND SUBUNIT. RX PubMed=19710024; DOI=10.1074/jbc.m109.010058; RA Ruprecht J., Yankovskaya V., Maklashina E., Iwata S., Cecchini G.; RT "Structure of Escherichia coli succinate:quinone oxidoreductase with an RT occupied and empty quinone-binding site."; RL J. Biol. Chem. 284:29836-29846(2009). 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 growth, CC and the succinate dehydrogenase is used in aerobic growth. 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: Part of an enzyme complex containing four subunits: a CC flavoprotein, an iron-sulfur, cytochrome b-556, and a hydrophobic CC anchor protein. The complex forms trimers. CC {ECO:0000269|PubMed:12560550, ECO:0000269|PubMed:16079137, CC ECO:0000269|PubMed:16407191, ECO:0000269|PubMed:19710024}. CC -!- INTERACTION: CC P07014; P0AC41: sdhA; NbExp=2; IntAct=EBI-1035514, EBI-371263; CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000269|PubMed:16079137}; Peripheral membrane protein CC {ECO:0000269|PubMed:16079137}. CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase CC iron-sulfur protein family. {ECO:0000305}. 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; J01619; AAA23896.1; -; Genomic_DNA. DR EMBL; X01070; CAA25534.1; -; Genomic_DNA. DR EMBL; U00096; AAC73818.1; -; Genomic_DNA. DR EMBL; AP009048; BAA35391.1; -; Genomic_DNA. DR EMBL; X00661; CAA25279.1; -; Genomic_DNA. DR PIR; A28837; DEECSI. DR RefSeq; NP_415252.1; NC_000913.3. DR RefSeq; WP_001235254.1; NZ_SSZK01000033.1. DR PDB; 1NEK; X-ray; 2.60 A; B=1-238. DR PDB; 1NEN; X-ray; 2.90 A; B=1-238. DR PDB; 2ACZ; X-ray; 3.10 A; B=1-238. DR PDB; 2WDQ; X-ray; 2.40 A; B/F/J=1-238. DR PDB; 2WDR; X-ray; 3.20 A; B/F/J=1-238. DR PDB; 2WDV; X-ray; 3.20 A; B/F/J=1-238. DR PDB; 2WP9; X-ray; 2.70 A; B/F/J=1-238. DR PDB; 2WS3; X-ray; 3.20 A; B/F/J=1-238. DR PDB; 2WU2; X-ray; 2.50 A; B/F/J=1-238. DR PDB; 2WU5; X-ray; 2.80 A; B/F/J=1-238. DR PDB; 6WU6; EM; 3.60 A; B/F/J=1-238. DR PDB; 7JZ2; EM; 2.50 A; B/F/J=1-238. DR PDBsum; 1NEK; -. DR PDBsum; 1NEN; -. DR PDBsum; 2ACZ; -. DR PDBsum; 2WDQ; -. DR PDBsum; 2WDR; -. DR PDBsum; 2WDV; -. DR PDBsum; 2WP9; -. DR PDBsum; 2WS3; -. DR PDBsum; 2WU2; -. DR PDBsum; 2WU5; -. DR PDBsum; 6WU6; -. DR PDBsum; 7JZ2; -. DR AlphaFoldDB; P07014; -. DR EMDB; EMD-21906; -. DR EMDB; EMD-22528; -. DR SMR; P07014; -. DR BioGRID; 4261950; 32. DR BioGRID; 849677; 4. DR ComplexPortal; CPX-1931; Respiratory chain complex II. DR DIP; DIP-10836N; -. DR IntAct; P07014; 8. DR STRING; 511145.b0724; -. DR DrugBank; DB07671; 2-[1-METHYLHEXYL]-4,6-DINITROPHENOL. DR DrugBank; DB04631; Atpenin A5. DR DrugBank; DB08690; Ubiquinone Q2. DR jPOST; P07014; -. DR PaxDb; 511145-b0724; -. DR EnsemblBacteria; AAC73818; AAC73818; b0724. DR GeneID; 945300; -. DR KEGG; ecj:JW0714; -. DR KEGG; eco:b0724; -. DR PATRIC; fig|1411691.4.peg.1548; -. DR EchoBASE; EB0925; -. DR eggNOG; COG0479; Bacteria. DR HOGENOM; CLU_044838_0_2_6; -. DR InParanoid; P07014; -. DR OMA; DGQYFGP; -. DR OrthoDB; 9804391at2; -. DR PhylomeDB; P07014; -. DR BioCyc; EcoCyc:SDH-FE-S; -. DR BioCyc; MetaCyc:SDH-FE-S; -. DR UniPathway; UPA00223; UER01005. DR EvolutionaryTrace; P07014; -. DR PHI-base; PHI:7965; -. DR PRO; PR:P07014; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0016020; C:membrane; NAS:ComplexPortal. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045281; C:succinate dehydrogenase complex; IPI:ComplexPortal. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IMP:EcoCyc. DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IDA:EcoCyc. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IMP:EcoCyc. DR GO; GO:0009055; F:electron transfer activity; IMP:EcoCyc. DR GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC. DR GO; GO:0051536; F:iron-sulfur cluster binding; IDA:EcoCyc. 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:0019646; P:aerobic electron transport chain; NAS:ComplexPortal. DR GO; GO:0009060; P:aerobic respiration; IEP:EcoCyc. 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; IPR001041; 2Fe-2S_ferredoxin-type. 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; PF13534; Fer4_17; 1. DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1. DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 1. PE 1: Evidence at protein level; KW 2Fe-2S; 3D-structure; 3Fe-4S; 4Fe-4S; Cell inner membrane; Cell membrane; KW Direct protein sequencing; Electron transport; Iron; Iron-sulfur; Membrane; KW Metal-binding; Oxidoreductase; Reference proteome; Transport; KW Tricarboxylic acid cycle. FT CHAIN 1..238 FT /note="Succinate dehydrogenase iron-sulfur subunit" FT /id="PRO_0000158688" FT DOMAIN 8..97 FT /note="2Fe-2S ferredoxin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465" FT DOMAIN 139..169 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 55 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT BINDING 60 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT BINDING 75 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT BINDING 149 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT BINDING 152 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT BINDING 155 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT BINDING 159 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT BINDING 164 FT /ligand="a ubiquinone" FT /ligand_id="ChEBI:CHEBI:16389" FT /ligand_note="ligand shared with SdhD subunit" FT /evidence="ECO:0000269|PubMed:12560550" FT BINDING 206 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT BINDING 212 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT BINDING 216 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT STRAND 2..9 FT /evidence="ECO:0007829|PDB:2WDQ" FT TURN 12..14 FT /evidence="ECO:0007829|PDB:2WDQ" FT STRAND 19..26 FT /evidence="ECO:0007829|PDB:2WDQ" FT STRAND 29..31 FT /evidence="ECO:0007829|PDB:7JZ2" FT HELIX 35..45 FT /evidence="ECO:0007829|PDB:2WDQ" FT STRAND 54..60 FT /evidence="ECO:0007829|PDB:2WDQ" FT STRAND 64..67 FT /evidence="ECO:0007829|PDB:2WDQ" FT STRAND 70..73 FT /evidence="ECO:0007829|PDB:2WDQ" FT HELIX 74..76 FT /evidence="ECO:0007829|PDB:2WDQ" FT HELIX 79..81 FT /evidence="ECO:0007829|PDB:2WDQ" FT STRAND 89..92 FT /evidence="ECO:0007829|PDB:2WDQ" FT STRAND 97..101 FT /evidence="ECO:0007829|PDB:2WDQ" FT STRAND 103..105 FT /evidence="ECO:0007829|PDB:2ACZ" FT HELIX 108..116 FT /evidence="ECO:0007829|PDB:2WDQ" FT STRAND 125..127 FT /evidence="ECO:0007829|PDB:7JZ2" FT STRAND 130..132 FT /evidence="ECO:0007829|PDB:2WDQ" FT HELIX 137..141 FT /evidence="ECO:0007829|PDB:2WDQ" FT TURN 142..148 FT /evidence="ECO:0007829|PDB:2WDQ" FT HELIX 156..158 FT /evidence="ECO:0007829|PDB:2WDQ" FT HELIX 160..164 FT /evidence="ECO:0007829|PDB:2WDQ" FT TURN 166..168 FT /evidence="ECO:0007829|PDB:2WDQ" FT HELIX 172..182 FT /evidence="ECO:0007829|PDB:2WDQ" FT HELIX 190..195 FT /evidence="ECO:0007829|PDB:2WDQ" FT TURN 200..205 FT /evidence="ECO:0007829|PDB:2WDQ" FT HELIX 211..215 FT /evidence="ECO:0007829|PDB:2WDQ" FT HELIX 222..237 FT /evidence="ECO:0007829|PDB:2WDQ" SQ SEQUENCE 238 AA; 26770 MW; 226F60C55F5AC35A CRC64; MRLEFSIYRY NPDVDDAPRM QDYTLEADEG RDMMLLDALI QLKEKDPSLS FRRSCREGVC GSDGLNMNGK NGLACITPIS ALNQPGKKIV IRPLPGLPVI RDLVVDMGQF YAQYEKIKPY LLNNGQNPPA REHLQMPEQR EKLDGLYECI LCACCSTSCP SFWWNPDKFI GPAGLLAAYR FLIDSRDTET DSRLDGLSDA FSVFRCHSIM NCVSVCPKGL NPTRAIGHIK SMLLQRNA //