FRDD_SALCH
ID FRDD_SALCH Reviewed; 119 AA.
AC Q57GN7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=SCH_4219;
OS Salmonella choleraesuis (strain SC-B67).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=321314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-B67;
RX PubMed=15781495; DOI=10.1093/nar/gki297;
RA Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA Lee Y.-S.;
RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT invasive and resistant zoonotic pathogen.";
RL Nucleic Acids Res. 33:1690-1698(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; AE017220; AAX68125.1; -; Genomic_DNA.
DR RefSeq; WP_001541348.1; NC_006905.1.
DR AlphaFoldDB; Q57GN7; -.
DR SMR; Q57GN7; -.
DR EnsemblBacteria; AAX68125; AAX68125; SCH_4219.
DR KEGG; sec:SCH_4219; -.
DR HOGENOM; CLU_168367_0_0_6; -.
DR OMA; ACYAFAG; -.
DR Proteomes; UP000000538; 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; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..119
FT /note="Fumarate reductase subunit D"
FT /id="PRO_1000045557"
FT TRANSMEM 25..45
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"
SQ SEQUENCE 119 AA; 13079 MW; 2E8FB8F18378ED03 CRC64;
MINPNPKRSD EPVFWGLFGA GGMWGAIIAP VIVLLVSIML PLGLFPGDAL SFERVLTFAQ
SFIGRVFLFL MIVLPLWCGL HRMHHAMHDL KIHVPAGKWV FYGLAAILTV VTAIGVITL
