MFRB_WOLSU
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 03-AUG-2022, entry version 98.
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 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC 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 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC 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 reductase
CC (MFR), that catalyzes the reduction of fumarate using 8-
CC methylmenaquinol-6 as electron donor. The complex shows no succinate
CC 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, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:134356, ChEBI:CHEBI:134357;
CC Evidence={ECO:0000269|PubMed:19170876};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00465};
CC Note=Binds 1 2Fe-2S cluster. {ECO:0000255|PROSITE-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-ProRule:PRU00711};
CC -!- SUBUNIT: The MFR complex is composed of three subunits: a flavoprotein
CC (SdhA), an iron-sulfur protein (SdhB), and one hydrophobic anchor
CC protein (SdhE). {ECO:0000269|PubMed:19170876}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:19170876}. Cell
CC membrane {ECO:0000269|PubMed:19170876}; Peripheral membrane protein
CC {ECO:0000305|PubMed:19170876}; Periplasmic side
CC {ECO:0000269|PubMed:19170876}.
CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase
CC iron-sulfur protein family. {ECO:0000305}.
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DR EMBL; BX571662; CAE10930.1; -; Genomic_DNA.
DR RefSeq; WP_011139713.1; NC_005090.1.
DR AlphaFoldDB; Q7M826; -.
DR SMR; Q7M826; -.
DR STRING; 273121.WS1921; -.
DR EnsemblBacteria; CAE10930; CAE10930; WS1921.
DR KEGG; wsu:WS1921; -.
DR eggNOG; COG0479; Bacteria.
DR HOGENOM; CLU_044838_3_1_7; -.
DR OMA; DGQYFGP; -.
DR OrthoDB; 1605514at2; -.
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; 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; Electron transport; Iron; Iron-sulfur;
KW Membrane; Metal-binding; Oxidoreductase; Periplasm; Reference proteome;
KW Transport.
FT CHAIN 1..319
FT /note="8-methylmenaquinol:fumarate reductase iron-sulfur
FT subunit"
FT /id="PRO_0000437541"
FT DOMAIN 1..96
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 139..168
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 193..224
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 51
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 56
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 59
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 71
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 148
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 151
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 154
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 158
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 204
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 207
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 210
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 214
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="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
