ID   FRDD_SHIDS              Reviewed;         119 AA.
AC   Q328H3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 75.
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}; OrderedLocusNames=SDY_4395;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00709}.
CC   -!- SIMILARITY: Belongs to the FrdD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00709}.
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DR   EMBL; CP000034; ABB64282.1; -; Genomic_DNA.
DR   RefSeq; WP_000609663.1; NC_007606.1.
DR   RefSeq; YP_405773.1; NC_007606.1.
DR   AlphaFoldDB; Q328H3; -.
DR   SMR; Q328H3; -.
DR   STRING; 300267.SDY_4395; -.
DR   EnsemblBacteria; ABB64282; ABB64282; SDY_4395.
DR   GeneID; 58391487; -.
DR   KEGG; sdy:SDY_4395; -.
DR   PATRIC; fig|300267.13.peg.5191; -.
DR   HOGENOM; CLU_168367_0_0_6; -.
DR   OMA; ACYAFAG; -.
DR   Proteomes; UP000002716; Chromosome.
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; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..119
FT                   /note="Fumarate reductase subunit D"
FT                   /id="PRO_1000045560"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00709"
FT   TRANSMEM        55..75
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"
SQ   SEQUENCE   119 AA;  13107 MW;  E9D119342B1D5357 CRC64;
     MINPNPKRSD EPVFWGLFGA GGMWSAIIAP VMILLVGILL PLGLFPGDAL SYERVLAFAQ
     SFIGRVFLFL MIVLPLWCGL HRMHHAMHDL KIHVPAGKWV FYGLAAILTV VTLIGVVTI