ID   FRDD_PROVU              Reviewed;         119 AA.
AC   P20924;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Fumarate reductase subunit D {ECO:0000255|HAMAP-Rule:MF_00709};
DE   AltName: Full=Fumarate reductase 13 kDa hydrophobic protein {ECO:0000255|HAMAP-Rule:MF_00709};
DE   AltName: Full=Quinol-fumarate reductase subunit D {ECO:0000255|HAMAP-Rule:MF_00709};
DE            Short=QFR subunit D {ECO:0000255|HAMAP-Rule:MF_00709};
GN   Name=frdD {ECO:0000255|HAMAP-Rule:MF_00709};
OS   Proteus vulgaris.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=585;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3308458; DOI=10.1111/j.1432-1033.1987.tb13362.x;
RA   Cole S.T.;
RT   "Nucleotide sequence and comparative analysis of the frd operon encoding
RT   the fumarate reductase of Proteus vulgaris. Extensive sequence divergence
RT   of the membrane anchors and absence of an frd-linked ampC cephalosporinase
RT   gene.";
RL   Eur. J. Biochem. 167:481-488(1987).
CC   -!- FUNCTION: Two distinct, membrane-bound, FAD-containing enzymes are
CC       responsible for the catalysis of fumarate and succinate
CC       interconversion; fumarate reductase is used in anaerobic growth, and
CC       succinate dehydrogenase is used in aerobic growth. Anchors the
CC       catalytic components of the fumarate reductase complex to the cell
CC       inner membrane, binds quinones. {ECO:0000255|HAMAP-Rule:MF_00709}.
CC   -!- SUBUNIT: Part of an enzyme complex containing four subunits: a
CC       flavoprotein (FrdA), an iron-sulfur protein (FrdB), and two hydrophobic
CC       anchor proteins (FrdC and FrdD). {ECO:0000255|HAMAP-Rule:MF_00709}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00709, ECO:0000305}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_00709}.
CC   -!- SIMILARITY: Belongs to the FrdD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00709}.
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DR   EMBL; X06144; CAA29504.1; -; Genomic_DNA.
DR   PIR; S00110; RDEB13.
DR   AlphaFoldDB; P20924; -.
DR   SMR; P20924; -.
DR   STRING; 585.DR95_2061; -.
DR   eggNOG; COG3080; Bacteria.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045284; C:plasma membrane fumarate reductase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0000104; F:succinate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006106; P:fumarate metabolic process; IEA:InterPro.
DR   CDD; cd00547; QFR_TypeD_subunitD; 1.
DR   Gene3D; 1.20.1300.10; -; 1.
DR   HAMAP; MF_00709; Fumarate_red_D; 1.
DR   InterPro; IPR003418; Fumarate_red_D.
DR   InterPro; IPR034804; SQR/QFR_C/D.
DR   Pfam; PF02313; Fumarate_red_D; 1.
DR   PIRSF; PIRSF000179; FrdD; 1.
DR   SUPFAM; SSF81343; SSF81343; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..119
FT                   /note="Fumarate reductase subunit D"
FT                   /id="PRO_0000196550"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00709"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00709"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00709"
FT   CONFLICT        89
FT                   /note="D -> H (in Ref. 1; CAA29504)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   119 AA;  13201 MW;  6B245D05683CD44B CRC64;
     MNQNQLPKRS DEPIFWGLFG AGGMWSAIVS PAIIILLGIL IPMGIAPEAF TYDRIMAFSQ
     GFIGRIFLLL MIILPVWCAL HRIHHTLHDF KVHVPASNWV FYGAAAIISV IAIIGVFTL