MFRA_WOLSU
ID MFRA_WOLSU Reviewed; 613 AA.
AC Q7M827;
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 flavoprotein subunit {ECO:0000303|PubMed:19170876};
DE Short=MFR flavoprotein subunit {ECO:0000303|PubMed:19170876};
DE EC=1.3.5.- {ECO:0000269|PubMed:19170876};
DE Flags: Precursor;
GN Name=sdhA {ECO:0000303|PubMed:19170876, ECO:0000312|EMBL:CAE10929.1};
GN OrderedLocusNames=WS1920 {ECO:0000312|EMBL:CAE10929.1};
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, COFACTOR, SUBCELLULAR LOCATION, SUBUNIT,
RP MUTAGENESIS OF 7-ARG-ARG-8 AND ALA-86, AND IDENTIFICATION BY MASS
RP 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: Flavoprotein 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. SdhA contains
CC the dicarboxylate reduction site. {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=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000305|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=Is exported to the periplasm via
CC the Tat pathway. {ECO:0000269|PubMed:19170876}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC {ECO:0000255|PROSITE-ProRule:PRU00648}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000305}.
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DR EMBL; BX571662; CAE10929.1; -; Genomic_DNA.
DR RefSeq; WP_011139712.1; NC_005090.1.
DR AlphaFoldDB; Q7M827; -.
DR SMR; Q7M827; -.
DR STRING; 273121.WS1920; -.
DR EnsemblBacteria; CAE10929; CAE10929; WS1920.
DR KEGG; wsu:WS1920; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_014312_6_2_7; -.
DR OMA; HWEWHMF; -.
DR OrthoDB; 153138at2; -.
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:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR Gene3D; 3.50.50.60; -; 1.
DR Gene3D; 3.90.700.10; -; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR InterPro; IPR030664; SdhA/FrdA/AprA.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR11632; PTHR11632; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR SUPFAM; SSF46977; SSF46977; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF56425; SSF56425; 1.
DR TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Electron transport; FAD; Flavoprotein; Membrane;
KW Oxidoreductase; Periplasm; Reference proteome; Signal; Transport.
FT SIGNAL 1..33
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 34..613
FT /note="8-methylmenaquinol:fumarate reductase flavoprotein
FT subunit"
FT /id="PRO_0000437540"
FT ACT_SITE 319
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 53..58
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 78..93
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 255
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 387
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 413
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 424
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 429..430
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT MUTAGEN 7..8
FT /note="RR->QQ: Highly decreases MFR activity in the
FT periplasm due to the disruption of the signal peptide."
FT /evidence="ECO:0000269|PubMed:19170876"
FT MUTAGEN 86
FT /note="A->H: Leads to covalent attachment of FAD to the
FT enzyme. Is still not able to catalyze succinate oxidation."
FT /evidence="ECO:0000269|PubMed:19170876"
SQ SEQUENCE 613 AA; 66517 MW; 6B2C969D147B4B57 CRC64;
MSEQFTRREF LQSACITMGA LAVSTSGVDR AFASSSLPIN TSGIPSCDVL IIGSGAAGLR
AAVAARKKDP SLNVIVVSKV MPTRSATTMA EGGINGVIDF SEGDSFALHA YDTVKGGDFL
VDQDTAMKFA EHAGEAIHEL DYIGMPFSRD KNGKVDKRYA GGASKIRCNF SADKTGHILT
HTCLDDALKN GVKFLMDHQL LDIGVDNGRC EGVVLRDIRT GTIAPVRAKS VVLATGGYTR
VFWNRTSTPY IATGDGAASA MRAGVAFKDP EMLQFHPTGV CHGGVLITEA ARGEGGILLN
NQGERFMKNY AKKMELAPRD IVSRSIETEI REGRAFGKGM EAYVLLDVTH LGKEKIMRNL
PQIRHIGLLF ENMDLVEKPI AIRPTAHYSM GGIDVMGLES MSTAIPGLFA AGEAACVSIH
GANRLGGNSL CDTVVTGKIA GTNAASFASS AGFGSGTHLH DLTLKWMSRF KEVANGKGEV
NEMYAIREEL GAVNWDNMGV FRTESRLVAL EDKHNELQAR YDALRIPNTN PVFNTAFTEY
VELGNILLAS RAARMGAEAR KESRGSHYRE DYIKRDDANF LKHSMVTMDS NGKLHLGWKD
VVVTQFKIEE RKY
