FRDD_SALA4
ID FRDD_SALA4 Reviewed; 119 AA.
AC B5F2L8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 57.
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=SeAg_B4618;
OS Salmonella agona (strain SL483).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=454166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL483;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001138; ACH49261.1; -; Genomic_DNA.
DR RefSeq; WP_000609650.1; NC_011149.1.
DR AlphaFoldDB; B5F2L8; -.
DR SMR; B5F2L8; -.
DR EnsemblBacteria; ACH49261; ACH49261; SeAg_B4618.
DR KEGG; sea:SeAg_B4618; -.
DR HOGENOM; CLU_168367_0_0_6; -.
DR OMA; ACYAFAG; -.
DR Proteomes; UP000008819; 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_1000132408"
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; 13049 MW; 9A8FA23199A22D19 CRC64;
MINPNPKRSD EPVFWGLFGA GGMWGAIIAP VIVLLVGIML PLGLFPGDAL SFERVLTFAQ
SFIGRVFLFL MIVLPLWCGL HRMHHAMHDL KIHVPAGKWV FYGLAAILTV VTAIGVITL
