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Database: UniProt
Entry: Q7M826
LinkDB: Q7M826
Original site: Q7M826 
ID   MFRB_WOLSU              Reviewed;         319 AA.
AC   Q7M826;
DT   05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   16-JAN-2019, entry version 89.
DE   RecName: Full=8-methylmenaquinol:fumarate reductase iron-sulfur subunit {ECO:0000303|PubMed:19170876};
DE            Short=MFR iron-sulfur subunit {ECO:0000303|PubMed:19170876};
DE            EC=1.3.5.- {ECO:0000269|PubMed:19170876};
GN   Name=sdhB {ECO:0000303|PubMed:19170876, ECO:0000312|EMBL:CAE10930.1};
GN   OrderedLocusNames=WS1921 {ECO:0000312|EMBL:CAE10930.1};
OS   Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS   11488 / FDC 602W) (Vibrio succinogenes).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Wolinella.
OX   NCBI_TaxID=273121;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W;
RX   PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA   Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA   Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA   Meyer F., Lederer H., Schuster S.C.;
RT   "Complete genome sequence and analysis of Wolinella succinogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, SUBUNIT, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W;
RX   PubMed=19170876; DOI=10.1111/j.1365-2958.2008.06581.x;
RA   Juhnke H.D., Hiltscher H., Nasiri H.R., Schwalbe H., Lancaster C.R.;
RT   "Production, characterization and determination of the real catalytic
RT   properties of the putative 'succinate dehydrogenase' from Wolinella
RT   succinogenes.";
RL   Mol. Microbiol. 71:1088-1101(2009).
CC   -!- FUNCTION: Iron-sulfur subunit of 8-methylmenaquinol:fumarate
CC       reductase (MFR), that catalyzes the reduction of fumarate using 8-
CC       methylmenaquinol-6 as electron donor. The complex shows no
CC       succinate oxidation activity. Is involved in anaerobic metabolism.
CC       {ECO:0000269|PubMed:19170876}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=8-methylmenaquinone-6 + succinate = 8-methylmenaquinol-6
CC         + fumarate; Xref=Rhea:RHEA:51848, ChEBI:CHEBI:29806,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:134356, ChEBI:CHEBI:134357;
CC         Evidence={ECO:0000269|PubMed:19170876};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00465};
CC       Note=Binds 1 2Fe-2S cluster. {ECO:0000255|PROSITE-
CC       ProRule:PRU00465};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00711};
CC       Note=Binds 2 [4Fe-4S] cluster. {ECO:0000255|PROSITE-
CC       ProRule:PRU00711};
CC   -!- SUBUNIT: The MFR complex is composed of three subunits: a
CC       flavoprotein (SdhA), an iron-sulfur protein (SdhB), and one
CC       hydrophobic anchor protein (SdhE). {ECO:0000269|PubMed:19170876}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:19170876}.
CC       Cell membrane {ECO:0000269|PubMed:19170876}; Peripheral membrane
CC       protein {ECO:0000305|PubMed:19170876}; Periplasmic side
CC       {ECO:0000269|PubMed:19170876}.
CC   -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate
CC       reductase iron-sulfur protein family. {ECO:0000305}.
DR   EMBL; BX571662; CAE10930.1; -; Genomic_DNA.
DR   RefSeq; WP_011139713.1; NC_005090.1.
DR   ProteinModelPortal; Q7M826; -.
DR   STRING; 273121.WS1921; -.
DR   EnsemblBacteria; CAE10930; CAE10930; WS1921.
DR   KEGG; wsu:WS1921; -.
DR   eggNOG; ENOG4105E33; Bacteria.
DR   eggNOG; COG0479; LUCA.
DR   HOGENOM; HOG000160590; -.
DR   KO; K00240; -.
DR   OMA; DGQYFGP; -.
DR   OrthoDB; 1605514at2; -.
DR   BioCyc; WSUC273121:G1GTD-1817-MONOMER; -.
DR   Proteomes; UP000000422; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 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:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 1.10.1060.10; -; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
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   Pfam; PF13183; Fer4_8; 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; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   1: Evidence at protein level;
KW   2Fe-2S; 4Fe-4S; Cell membrane; Complete proteome; Electron transport;
KW   Iron; Iron-sulfur; Membrane; Metal-binding; Oxidoreductase; Periplasm;
KW   Reference proteome; Transport.
FT   CHAIN         1    319       8-methylmenaquinol:fumarate reductase
FT                                iron-sulfur subunit.
FT                                /FTId=PRO_0000437541.
FT   DOMAIN        1     96       2Fe-2S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00465}.
FT   DOMAIN      139    168       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      193    224       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        51     51       Iron-sulfur (2Fe-2S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00465}.
FT   METAL        56     56       Iron-sulfur (2Fe-2S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00465}.
FT   METAL        59     59       Iron-sulfur (2Fe-2S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00465}.
FT   METAL        71     71       Iron-sulfur (2Fe-2S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00465}.
FT   METAL       148    148       Iron-sulfur (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       151    151       Iron-sulfur (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       154    154       Iron-sulfur (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       158    158       Iron-sulfur (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       204    204       Iron-sulfur (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       207    207       Iron-sulfur (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       210    210       Iron-sulfur (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       214    214       Iron-sulfur (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
SQ   SEQUENCE   319 AA;  35554 MW;  11F00A2944A55463 CRC64;
     MKFIIDRFDG KKNYEQIYTL AKEDIEAKTL LGVLLLIKQT QDITLNFTAS CRMAICGACA
     VRVNGHSYLA CDTKMTELFE EYKNSDTFRI SPLGNHRVIS DLVVDWEPAI ENLRKIKPGL
     VAKSEFSAKE GCQQNQEEFD RIIKQWDCIL CGSCVSECNK FSADQSDYME PFVFTQAWRL
     ANDSRSKDPM IHVKPAVANG LWNCVHCHEC TNRCPKHISA AEDIANLRVM AMKKGLNTGV
     GPAHAKAFHT DLVEGSGRLN EIRLALRIEG VATVARTGMA ITLMRAGKMN PLEIFGGHTI
     KGHEDLVKMI DAAKAATKE
//
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