SDHB_ECOLI
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 03-AUG-2022, entry version 195.
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; 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 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; P07014; -.
DR PRIDE; P07014; -.
DR EnsemblBacteria; AAC73818; AAC73818; b0724.
DR EnsemblBacteria; BAA35391; BAA35391; BAA35391.
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 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; IDA:ComplexPortal.
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 transfer 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:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
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 CDD; cd00207; fer2; 1.
DR Gene3D; 1.10.1060.10; -; 1.
DR Gene3D; 3.10.20.30; -; 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 Pfam; PF13085; Fer2_3; 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; 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
