ID   FRDD_ALIFM              Reviewed;         120 AA.
AC   B5FBS8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Fumarate reductase subunit D {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=VFMJ11_2459;
OS   Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=388396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11;
RA   Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT   "Complete sequence of Vibrio fischeri strain MJ11.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Anchors the catalytic components of the fumarate reductase
CC       complex to the cell membrane, binds quinones. {ECO:0000255|HAMAP-
CC       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; CP001139; ACH66930.1; -; Genomic_DNA.
DR   RefSeq; WP_005421184.1; NC_011184.1.
DR   AlphaFoldDB; B5FBS8; -.
DR   SMR; B5FBS8; -.
DR   EnsemblBacteria; ACH66930; ACH66930; VFMJ11_2459.
DR   GeneID; 64244088; -.
DR   KEGG; vfm:VFMJ11_2459; -.
DR   HOGENOM; CLU_168367_0_0_6; -.
DR   OMA; ACYAFAG; -.
DR   Proteomes; UP000001857; Chromosome I.
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..120
FT                   /note="Fumarate reductase subunit D"
FT                   /id="PRO_1000132419"
FT   TRANSMEM        25..45
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        100..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00709"
SQ   SEQUENCE   120 AA;  13022 MW;  B1696FA11AD803A8 CRC64;
     MVNRNPKRSD EPVWWGLFGA GGTWFAMLTP VTILVLGILV PLGVIGPESM NYLRVAGFVT
     SIIGALFVIG SISMPMWHAM HRLHHGMHDL KFHTGTAGKI ACYAAAALAT VLSVVFIFMI