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Database: UniProt
Entry: Q92JJ8
LinkDB: Q92JJ8
Original site: Q92JJ8 
ID   SDHB_RICCN              Reviewed;         261 AA.
AC   Q92JJ8;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   16-JAN-2019, entry version 116.
DE   RecName: Full=Succinate dehydrogenase iron-sulfur subunit;
DE            EC=1.3.5.1;
GN   Name=sdhB; OrderedLocusNames=RC0069;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M.,
RA   Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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:49601;
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;
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.
CC   -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate
CC       reductase iron-sulfur protein family. {ECO:0000305}.
DR   EMBL; AE006914; AAL02607.1; -; Genomic_DNA.
DR   PIR; E97708; E97708.
DR   RefSeq; WP_010976754.1; NC_003103.1.
DR   ProteinModelPortal; Q92JJ8; -.
DR   SMR; Q92JJ8; -.
DR   PRIDE; Q92JJ8; -.
DR   EnsemblBacteria; AAL02607; AAL02607; RC0069.
DR   GeneID; 928594; -.
DR   KEGG; rco:RC0069; -.
DR   PATRIC; fig|272944.4.peg.81; -.
DR   HOGENOM; HOG000160590; -.
DR   KO; K00240; -.
DR   OMA; DGQYFGP; -.
DR   BioCyc; RCON272944:G1FZG-110-MONOMER; -.
DR   UniPathway; UPA00223; UER01005.
DR   Proteomes; UP000000816; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
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; IPR006058; 2Fe2S_fd_BS.
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; SSF46548; SSF46548; 1.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   TIGRFAMs; TIGR00384; dhsB; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 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; Complete proteome; Electron transport; Iron;
KW   Iron-sulfur; Metal-binding; Oxidoreductase; Transport;
KW   Tricarboxylic acid cycle.
FT   CHAIN         1    261       Succinate dehydrogenase iron-sulfur
FT                                subunit.
FT                                /FTId=PRO_0000158690.
FT   DOMAIN       28    119       2Fe-2S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00465}.
FT   DOMAIN      161    191       4Fe-4S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        80     80       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL        85     85       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL       100    100       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL       171    171       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       174    174       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       177    177       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       181    181       Iron-sulfur 3 (3Fe-4S). {ECO:0000250}.
FT   METAL       228    228       Iron-sulfur 3 (3Fe-4S). {ECO:0000250}.
FT   METAL       234    234       Iron-sulfur 3 (3Fe-4S). {ECO:0000250}.
FT   METAL       238    238       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   BINDING     186    186       Ubiquinone; shared with SdhD subunit.
FT                                {ECO:0000250}.
SQ   SEQUENCE   261 AA;  29703 MW;  4B69ED8BB7022CE6 CRC64;
     MAELRLPPNS VVKKGREHKE QEEMLKPRKI KIYRYDPDLD KNPTIDSFEI DLSKTGPMIL
     DALIKIKNEI DSTLTFRRSC REGICGSCAM NIDGTNTLAC IKPIEDISGD IKIYPLPHMK
     VVKDLVPDMS HFYAQYESIE PWLKTDSPTP SNSERLQSIK DREKLDGLYE CILCACCSTS
     CPSYWWNGDK YLGPAILLQA YRWIADSRDD NTGERLEALE DPFKLYRCHT IMNCTKTCPK
     GLNPAKAIGK IKSLIAERHG L
//
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