FRDD_SERP5
ID FRDD_SERP5 Reviewed; 119 AA.
AC A8G8T4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-2022, entry version 69.
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=Spro_0416;
OS Serratia proteamaculans (strain 568).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=399741;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=568;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000826; ABV39524.1; -; Genomic_DNA.
DR RefSeq; WP_012004879.1; NC_009832.1.
DR AlphaFoldDB; A8G8T4; -.
DR SMR; A8G8T4; -.
DR STRING; 399741.Spro_0416; -.
DR EnsemblBacteria; ABV39524; ABV39524; Spro_0416.
DR KEGG; spe:Spro_0416; -.
DR eggNOG; COG3080; Bacteria.
DR HOGENOM; CLU_168367_0_0_6; -.
DR OMA; ACYAFAG; -.
DR OrthoDB; 2071715at2; -.
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_1000062071"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00709"
FT TRANSMEM 55..75
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; 12921 MW; F238256D9066FBB4 CRC64;
MINQAPKRSD EPVFWGLFGA GGMWGAIIAP AIVLLVGILL PLGLFPGDAL GYDRILAFCQ
SLIGRLFLLL MIILPLWCGL HRIHHAMHDL KIHVPAGKWV FYGLAAILSV VTVIGVVTL
