MFRE_WOLSU
ID MFRE_WOLSU Reviewed; 284 AA.
AC Q7M825;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=8-methylmenaquinol:fumarate reductase membrane anchor subunit {ECO:0000303|PubMed:19170876};
DE Short=MFR membrane anchor subunit {ECO:0000303|PubMed:19170876};
DE EC=1.3.5.- {ECO:0000269|PubMed:19170876};
GN Name=sdhE {ECO:0000303|PubMed:19170876};
GN Synonyms=sdhC {ECO:0000312|EMBL:CAE10931.1};
GN OrderedLocusNames=WS1922 {ECO:0000312|EMBL:CAE10931.1};
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: Membrane anchor 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 succinate
CC oxidation activity. Is involved in anaerobic metabolism. SdhE likely
CC contains the quinol/quinone binding site.
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 -!- 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}. Note=Membrane association is most likely
CC mediated via amphipathic helices. {ECO:0000305|PubMed:19170876}.
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DR EMBL; BX571662; CAE10931.1; -; Genomic_DNA.
DR RefSeq; WP_011139714.1; NC_005090.1.
DR AlphaFoldDB; Q7M825; -.
DR SMR; Q7M825; -.
DR STRING; 273121.WS1922; -.
DR EnsemblBacteria; CAE10931; CAE10931; WS1922.
DR KEGG; wsu:WS1922; -.
DR eggNOG; COG2048; Bacteria.
DR HOGENOM; CLU_052147_1_0_7; -.
DR OMA; SCCGASH; -.
DR OrthoDB; 647535at2; -.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR004017; Cys_rich_dom.
DR Pfam; PF02754; CCG; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Electron transport; Membrane; Oxidoreductase; Periplasm;
KW Reference proteome; Transport.
FT CHAIN 1..284
FT /note="8-methylmenaquinol:fumarate reductase membrane
FT anchor subunit"
FT /id="PRO_0000437542"
SQ SEQUENCE 284 AA; 30655 MW; 8FCC234FF78C0699 CRC64;
MQKEFAFFPG CVLSQAAIES KKSIEAIAPV LGIKLREIEG WSCCGASQAQ CVDPLATLVA
NARNLALAEQ MNLPVLTTCS TCLLMLTRAK AELDRGAKDQ INSFLAKGNM SYQGTSEVTS
LLWVLAQNVE ELKSKVKKPL SNLKVAVFYG CHSLRPEKDL GFESSTNPTS FETIVKALGA
QVVPFEKRLN CCGFHAVYPA ESSAMKMTSG IINTAAKSEA HCVVTPCPLC QMQLDIYQED
AQKIAKSKER VPVLHLSQLV GLALGIPAKE LGLNHNVIDA TKLG