FRDD_ECOLI
ID FRDD_ECOLI Reviewed; 119 AA.
AC P0A8Q3; P03806; Q2M6F1; Q47048;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 118.
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, ECO:0000303|PubMed:11850430};
DE Short=QFR subunit D {ECO:0000255|HAMAP-Rule:MF_00709, ECO:0000303|PubMed:11850430};
GN Name=frdD {ECO:0000255|HAMAP-Rule:MF_00709};
GN OrderedLocusNames=b4151, JW4112;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=7041115; DOI=10.1073/pnas.79.4.1111;
RA Grundstroem T., Jaurin B.;
RT "Overlap between ampC and frd operons on the Escherichia coli chromosome.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:1111-1115(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 82-119.
RX PubMed=6369321; DOI=10.1073/pnas.80.24.7556;
RA Olsson O., Bergstroem S., Lindberg F.P., Normark S.;
RT "ampC beta-lactamase hyperproduction in Escherichia coli: natural
RT ampicillin resistance generated by horizontal chromosomal DNA transfer from
RT Shigella.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:7556-7560(1983).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 109-119, AND INDUCTION.
RX PubMed=2999070; DOI=10.1128/jb.164.3.1100-1109.1985;
RA Jones H.M., Gunsalus R.P.;
RT "Transcription of the Escherichia coli fumarate reductase genes (frdABCD)
RT and their coordinate regulation by oxygen, nitrate, and fumarate.";
RL J. Bacteriol. 164:1100-1109(1985).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) IN COMPLEX WITH MENAQUINONE,
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=10373108; DOI=10.1126/science.284.5422.1961;
RA Iverson T.M., Luna-Chavez C., Cecchini G., Rees D.C.;
RT "Structure of the Escherichia coli fumarate reductase respiratory
RT complex.";
RL Science 284:1961-1966(1999).
RN [9] {ECO:0007744|PDB:1KF6, ECO:0007744|PDB:1KFY, ECO:0007744|PDB:1L0V}
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH MENAQUINONE AND
RP INHIBITORS, AND SUBUNIT.
RX PubMed=11850430; DOI=10.1074/jbc.m200815200;
RA Iverson T.M., Luna-Chavez C., Croal L.R., Cecchini G., Rees D.C.;
RT "Crystallographic studies of the Escherichia coli quinol-fumarate reductase
RT with inhibitors bound to the quinol-binding site.";
RL J. Biol. Chem. 277:16124-16130(2002).
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 (PubMed:10373108). The QFR enzyme
CC complex binds 2 quinones in or near the membrane; 1 near the [3Fe-4S]
CC cluster (QP is proximal to the [3Fe-4S] cluster, on the cytoplasmic
CC side of the membrane) while QD (the distal cluster) is on the other
CC side of the membrane. It is not clear if both of the quinol-binding
CC sites are functionally relevant (PubMed:10373108, PubMed:11850430).
CC {ECO:0000269|PubMed:10373108, ECO:0000269|PubMed:11850430}.
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 ECO:0000269|PubMed:10373108, ECO:0000269|PubMed:11850430}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00709, ECO:0000269|PubMed:15919996}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_00709, ECO:0000269|PubMed:10373108}.
CC -!- INDUCTION: Regulated at the transcriptional level in response to the
CC cellular availability of the alternate electron acceptors oxygen,
CC nitrate, and fumarate. {ECO:0000269|PubMed:2999070}.
CC -!- SIMILARITY: Belongs to the FrdD family. {ECO:0000255|HAMAP-
CC Rule:MF_00709}.
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DR EMBL; J01611; AAA23440.1; -; Genomic_DNA.
DR EMBL; V00277; CAA23536.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97050.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77111.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78155.1; -; Genomic_DNA.
DR EMBL; M11979; AAA23434.1; -; Genomic_DNA.
DR PIR; A04431; WMEC13.
DR RefSeq; NP_418575.1; NC_000913.3.
DR RefSeq; WP_000609663.1; NZ_STEB01000014.1.
DR PDB; 1KF6; X-ray; 2.70 A; D/P=1-119.
DR PDB; 1KFY; X-ray; 3.60 A; D/P=1-119.
DR PDB; 1L0V; X-ray; 3.30 A; D/P=1-119.
DR PDB; 2B76; X-ray; 3.30 A; D/P=1-119.
DR PDB; 3CIR; X-ray; 3.65 A; D/P=1-119.
DR PDB; 3P4P; X-ray; 2.80 A; D/P=1-119.
DR PDB; 3P4Q; X-ray; 3.35 A; D/P=1-119.
DR PDB; 3P4R; X-ray; 3.05 A; D/P=1-119.
DR PDB; 3P4S; X-ray; 3.10 A; D/P=1-119.
DR PDB; 4KX6; X-ray; 2.95 A; D/P=1-119.
DR PDB; 5VPN; X-ray; 4.22 A; D/H=1-119.
DR PDBsum; 1KF6; -.
DR PDBsum; 1KFY; -.
DR PDBsum; 1L0V; -.
DR PDBsum; 2B76; -.
DR PDBsum; 3CIR; -.
DR PDBsum; 3P4P; -.
DR PDBsum; 3P4Q; -.
DR PDBsum; 3P4R; -.
DR PDBsum; 3P4S; -.
DR PDBsum; 4KX6; -.
DR PDBsum; 5VPN; -.
DR AlphaFoldDB; P0A8Q3; -.
DR SMR; P0A8Q3; -.
DR BioGRID; 4262699; 457.
DR ComplexPortal; CPX-1967; Plasma membrane fumarate reductase complex.
DR DIP; DIP-9684N; -.
DR IntAct; P0A8Q3; 1.
DR STRING; 511145.b4151; -.
DR DrugBank; DB07490; 2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL.
DR DrugBank; DB07918; 2-heptyl-4-hydroxyquinoline N-oxide.
DR jPOST; P0A8Q3; -.
DR PaxDb; P0A8Q3; -.
DR PRIDE; P0A8Q3; -.
DR EnsemblBacteria; AAC77111; AAC77111; b4151.
DR EnsemblBacteria; BAE78155; BAE78155; BAE78155.
DR GeneID; 58391487; -.
DR GeneID; 948668; -.
DR KEGG; ecj:JW4112; -.
DR KEGG; eco:b4151; -.
DR PATRIC; fig|1411691.4.peg.2547; -.
DR EchoBASE; EB0329; -.
DR eggNOG; COG3080; Bacteria.
DR HOGENOM; CLU_168367_0_0_6; -.
DR OMA; ACYAFAG; -.
DR PhylomeDB; P0A8Q3; -.
DR BioCyc; EcoCyc:FUM-MEMB2; -.
DR BioCyc; MetaCyc:FUM-MEMB2; -.
DR BRENDA; 1.3.5.4; 2026.
DR EvolutionaryTrace; P0A8Q3; -.
DR PRO; PR:P0A8Q3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0045284; C:plasma membrane fumarate reductase complex; IDA:EcoCyc.
DR GO; GO:0102040; F:fumarate reductase (menaquinone); IMP:EcoCyc.
DR GO; GO:0000104; F:succinate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009061; P:anaerobic respiration; IMP:EcoCyc.
DR GO; GO:0044780; P:bacterial-type flagellum assembly; IMP:EcoCyc.
DR GO; GO:0006113; P:fermentation; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..119
FT /note="Fumarate reductase subunit D"
FT /id="PRO_0000196542"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10373108"
FT TRANSMEM 9..35
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:10373108"
FT TOPO_DOM 36..60
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:10373108"
FT TRANSMEM 61..89
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:10373108"
FT TOPO_DOM 90..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10373108"
FT TRANSMEM 97..115
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:10373108"
FT TOPO_DOM 116..119
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:10373108,
FT ECO:0000269|PubMed:15919996"
FT BINDING 15
FT /ligand="a menaquinone"
FT /ligand_id="ChEBI:CHEBI:16374"
FT /evidence="ECO:0007744|PDB:1L0V"
FT HELIX 11..27
FT /evidence="ECO:0007829|PDB:1KF6"
FT HELIX 29..37
FT /evidence="ECO:0007829|PDB:1KF6"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:1KF6"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:1KF6"
FT HELIX 52..59
FT /evidence="ECO:0007829|PDB:1KF6"
FT HELIX 62..89
FT /evidence="ECO:0007829|PDB:1KF6"
FT HELIX 97..116
FT /evidence="ECO:0007829|PDB:1KF6"
SQ SEQUENCE 119 AA; 13107 MW; E9D119342B1D5357 CRC64;
MINPNPKRSD EPVFWGLFGA GGMWSAIIAP VMILLVGILL PLGLFPGDAL SYERVLAFAQ
SFIGRVFLFL MIVLPLWCGL HRMHHAMHDL KIHVPAGKWV FYGLAAILTV VTLIGVVTI
