ID   FRDD_VIBPA              Reviewed;         125 AA.
AC   Q87KY1;
DT   09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=VP2843;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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; BA000031; BAC61106.1; -; Genomic_DNA.
DR   RefSeq; NP_799222.1; NC_004603.1.
DR   RefSeq; WP_005456924.1; NC_004603.1.
DR   AlphaFoldDB; Q87KY1; -.
DR   SMR; Q87KY1; -.
DR   STRING; 223926.28807869; -.
DR   EnsemblBacteria; BAC61106; BAC61106; BAC61106.
DR   GeneID; 1190406; -.
DR   KEGG; vpa:VP2843; -.
DR   PATRIC; fig|223926.6.peg.2735; -.
DR   eggNOG; COG3080; Bacteria.
DR   HOGENOM; CLU_168367_0_0_6; -.
DR   OMA; ACYAFAG; -.
DR   Proteomes; UP000002493; Chromosome 1.
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..125
FT                   /note="Fumarate reductase subunit D"
FT                   /id="PRO_0000196555"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00709"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00709"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00709"
SQ   SEQUENCE   125 AA;  13630 MW;  BCAA0795075BF479 CRC64;
     MKPNYSVNTS PKRSDEPIWW GLFGAGGTWF AMLTPITVLV LGILVPLGVI DAEAMSYERV
     SAFATSIIGA LFIIGTLALP MWHAMHRVHH GMHDLKFHTG VIGKVACYAF AGLITALAVI
     FIFMI