ID   FRDD_MYCBT              Reviewed;         125 AA.
AC   C1ANJ0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 56.
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=JTY_1581;
OS   Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=561275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Tokyo 172 / ATCC 35737 / TMC 1019;
RX   PubMed=19200449; DOI=10.1016/j.vaccine.2009.01.034;
RA   Seki M., Honda I., Fujita I., Yano I., Yamamoto S., Koyama A.;
RT   "Whole genome sequence analysis of Mycobacterium bovis bacillus Calmette-
RT   Guerin (BCG) Tokyo 172: a comparative study of BCG vaccine substrains.";
RL   Vaccine 27:1710-1716(2009).
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 membrane {ECO:0000255|HAMAP-Rule:MF_00709};
CC       Multi-pass membrane protein {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; AP010918; BAH25869.1; -; Genomic_DNA.
DR   RefSeq; WP_003407771.1; NZ_CP014566.1.
DR   AlphaFoldDB; C1ANJ0; -.
DR   SMR; C1ANJ0; -.
DR   KEGG; mbt:JTY_1581; -.
DR   HOGENOM; CLU_168367_0_0_11; -.
DR   OMA; ACYAFAG; -.
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   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 membrane; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..125
FT                   /note="Fumarate reductase subunit D"
FT                   /id="PRO_1000147957"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00709"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00709"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00709"
SQ   SEQUENCE   125 AA;  13754 MW;  B08F79AD3113166A CRC64;
     MTPSTSDARS RRRSAEPFLW LLFSAGGMVT ALVAPVLLLL FGLAFPLGWL DAPDHGHLLA
     MVRNPITKLV VLVLVVLALF HAAHRFRFVL DHGLQLGRFD RVIALWCYGM AVLGSATAGW
     MLLTM