ID DHSB_ECOLI Reviewed; 238 AA.
AC P07014;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 01-MAY-2013, entry version 135.
DE RecName: Full=Succinate dehydrogenase iron-sulfur subunit;
DE EC=1.3.99.1;
GN Name=sdhB; OrderedLocusNames=b0724, JW0714;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6388571;
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.,
RA Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
RA Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
RA Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
RA Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
RA Yano M., Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome
RT corresponding to 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.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1474(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
RT MG1655 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
RT in the 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
RP CLUSTERS AND UBIQUINONE, COFACTOR, AND SUBUNIT.
RX PubMed=12560550; DOI=10.1126/science.1079605;
RA Yankovskaya V., Horsefield R., Toernroth S., Luna-Chavez C.,
RA Miyoshi H., 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
RP CLUSTERS, 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
RT electron 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
RP CLUSTERS, 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
RT an 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
CC growth, and the succinate dehydrogenase is used in aerobic growth.
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 fumarate 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 -!- INTERACTION:
CC P0AC41:sdhA; NbExp=5; IntAct=EBI-1035514, EBI-371263;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane
CC protein.
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.
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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_000913.2.
DR RefSeq; YP_489004.1; NC_007779.1.
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; 2AD0; Model; -; 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 PDBsum; 1NEK; -.
DR PDBsum; 1NEN; -.
DR PDBsum; 2ACZ; -.
DR PDBsum; 2AD0; -.
DR PDBsum; 2WDQ; -.
DR PDBsum; 2WDR; -.
DR PDBsum; 2WDV; -.
DR PDBsum; 2WP9; -.
DR PDBsum; 2WS3; -.
DR PDBsum; 2WU2; -.
DR PDBsum; 2WU5; -.
DR ProteinModelPortal; P07014; -.
DR SMR; P07014; 1-238.
DR DIP; DIP-10836N; -.
DR IntAct; P07014; 4.
DR STRING; 511145.b0724; -.
DR PaxDb; P07014; -.
DR PRIDE; P07014; -.
DR EnsemblBacteria; AAC73818; AAC73818; b0724.
DR EnsemblBacteria; BAA35391; BAA35391; BAA35391.
DR GeneID; 12932956; -.
DR GeneID; 945300; -.
DR KEGG; ecj:Y75_p0704; -.
DR KEGG; eco:b0724; -.
DR PATRIC; 32116643; VBIEscCol129921_0754.
DR EchoBASE; EB0925; -.
DR EcoGene; EG10932; sdhB.
DR eggNOG; COG0479; -.
DR HOGENOM; HOG000160590; -.
DR KO; K00240; -.
DR OMA; NCSRTCP; -.
DR ProtClustDB; PRK05950; -.
DR BioCyc; EcoCyc:SDH-FE-S; -.
DR BioCyc; ECOL316407:JW0714-MONOMER; -.
DR BioCyc; MetaCyc:SDH-FE-S; -.
DR UniPathway; UPA00223; UER01005.
DR EvolutionaryTrace; P07014; -.
DR Genevestigator; P07014; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 carrier activity; IMP:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000104; F:succinate dehydrogenase activity; IEA:EC.
DR GO; GO:0009060; P:aerobic respiration; IEP:EcoCyc.
DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1060.10; -; 1.
DR Gene3D; 3.10.20.30; -; 1.
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.
DR InterPro; IPR012285; Fum_reductase_C.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR004489; Succ_DH/fum_Rdtase_Fe-S.
DR InterPro; IPR025192; Succ_DH/fum_Rdtase_N.
DR Pfam; PF13085; Fer2_3; 1.
DR SUPFAM; SSF54292; Ferredoxin; 1.
DR SUPFAM; SSF46548; Helical_ferredxn; 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 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; 3Fe-4S; 4Fe-4S; Cell inner membrane;
KW Cell membrane; Complete proteome; Direct protein sequencing;
KW Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Transport;
KW Tricarboxylic acid cycle.
FT CHAIN 1 238 Succinate dehydrogenase iron-sulfur
FT subunit.
FT /FTId=PRO_0000158688.
FT DOMAIN 8 97 2Fe-2S ferredoxin-type.
FT DOMAIN 139 169 4Fe-4S ferredoxin-type.
FT METAL 55 55 Iron-sulfur 1 (2Fe-2S).
FT METAL 60 60 Iron-sulfur 1 (2Fe-2S).
FT METAL 75 75 Iron-sulfur 1 (2Fe-2S).
FT METAL 149 149 Iron-sulfur 2 (4Fe-4S).
FT METAL 152 152 Iron-sulfur 2 (4Fe-4S).
FT METAL 155 155 Iron-sulfur 2 (4Fe-4S).
FT METAL 159 159 Iron-sulfur 3 (3Fe-4S).
FT METAL 206 206 Iron-sulfur 3 (3Fe-4S).
FT METAL 212 212 Iron-sulfur 3 (3Fe-4S).
FT METAL 216 216 Iron-sulfur 2 (4Fe-4S).
FT BINDING 164 164 Ubiquinone; shared with SdhD subunit.
FT STRAND 2 9
FT TURN 12 14
FT STRAND 19 26
FT STRAND 29 31
FT HELIX 35 45
FT STRAND 54 60
FT STRAND 64 67
FT STRAND 70 73
FT HELIX 74 76
FT HELIX 79 81
FT STRAND 89 92
FT STRAND 97 101
FT STRAND 103 105
FT HELIX 108 116
FT STRAND 130 132
FT HELIX 137 141
FT TURN 142 148
FT HELIX 156 158
FT HELIX 160 164
FT TURN 166 168
FT HELIX 172 182
FT HELIX 190 195
FT TURN 200 205
FT HELIX 211 215
FT HELIX 222 237
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
//
