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Database: UniProt
Entry: P07014
LinkDB: P07014
Original site: P07014 
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   11-JUN-2014, entry version 145.
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; 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 277:1453-1462(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
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 + a quinone = fumarate + a quinol.
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=2; 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_000913.3.
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   BioGrid; 849677; 1.
DR   DIP; DIP-10836N; -.
DR   IntAct; P07014; 8.
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; QYEKIRP; -.
DR   OrthoDB; EOG6CK7MG; -.
DR   PhylomeDB; P07014; -.
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   PRO; PR: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:0051536; F:iron-sulfur cluster binding; IDA:EcoCyc.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009060; P:aerobic respiration; IEP:EcoCyc.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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; 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; SSF46548; SSF46548; 1.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   TIGRFAMs; TIGR00384; dhsB; 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;
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
//
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