FRDD_PECAS
ID FRDD_PECAS Reviewed; 118 AA.
AC Q6D029;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 81.
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=ECA3972;
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT subsp. atroseptica and characterization of virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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; BX950851; CAG76869.1; -; Genomic_DNA.
DR RefSeq; WP_011095466.1; NC_004547.2.
DR AlphaFoldDB; Q6D029; -.
DR SMR; Q6D029; -.
DR STRING; 218491.ECA3972; -.
DR EnsemblBacteria; CAG76869; CAG76869; ECA3972.
DR GeneID; 57210585; -.
DR KEGG; eca:ECA3972; -.
DR PATRIC; fig|218491.5.peg.4037; -.
DR eggNOG; COG3080; Bacteria.
DR HOGENOM; CLU_168367_0_0_6; -.
DR OMA; ACYAFAG; -.
DR OrthoDB; 2071715at2; -.
DR Proteomes; UP000007966; 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; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..118
FT /note="Fumarate reductase subunit D"
FT /id="PRO_1000045549"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00709"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00709"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00709"
SQ SEQUENCE 118 AA; 13043 MW; 36D9CD166844F034 CRC64;
MINPTPKRSD EPPFWGLFGA GGMWSAFFAP VIILLVGVML PLGMFPDALT YERIAAFSQS
FIGRVFLLLM IVLPLWCGLH RIHHAMHDLK IHVPAGKWVF YGLAAILTVV TVIGVVTL