FRDB_ECOLI
ID FRDB_ECOLI Reviewed; 244 AA.
AC P0AC47; P00364; Q2M6E9;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Fumarate reductase iron-sulfur subunit;
DE EC=1.3.5.4;
DE AltName: Full=Quinol-fumarate reductase iron-sulfur subunit {ECO:0000303|PubMed:11850430};
DE Short=QFR iron-sulfur subunit {ECO:0000303|PubMed:11850430};
GN Name=frdB; OrderedLocusNames=b4153, JW4114;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-9.
RC STRAIN=K12;
RX PubMed=6751816; DOI=10.1111/j.1432-1033.1982.tb06768.x;
RA Cole S.T., Grundstroem T., Jaurin B., Robinson J.J., Weiner J.H.;
RT "Location and nucleotide sequence of frdB, the gene coding for the iron-
RT sulphur protein subunit of the fumarate reductase of Escherichia coli.";
RL Eur. J. Biochem. 126:211-216(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 236-244.
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 [6]
RP MUTAGENESIS OF CYS-58; CYS-63; CYS-66 AND CYS-78.
RX PubMed=2174169; DOI=10.1073/pnas.87.22.8965;
RA Werth M.T., Cecchini G., Manodori A., Ackrell B.A.C., Schroeder I.,
RA Gunsalus R.P., Johnson M.K.;
RT "Site-directed mutagenesis of conserved cysteine residues in Escherichia
RT coli fumarate reductase: modification of the spectroscopic and
RT electrochemical properties of the [2Fe-2S] cluster.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:8965-8969(1990).
RN [7]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (2FE-2S);
RP IRON-SULFUR (3FE-4S); IRON-SULFUR (4FE-4S) AND MENAQUINONE, COFACTOR,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
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) OF 2-244 IN COMPLEX WITH IRON-SULFUR
RP (2FE-2S); IRON-SULFUR (3FE-4S); IRON-SULFUR (4FE-4S); 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 during anaerobic growth,
CC and succinate dehydrogenase is used during aerobic growth. The QFR
CC enzyme complex binds 2 quinones in or near the membrane; 1 near the
CC [3Fe-4S] cluster (QP is proximal to the [3Fe-4S] cluster, on the
CC cytoplasmic side of the membrane) while QD (the distal cluster) is on
CC the other side of the membrane. It is not clear if both of the quinol-
CC binding sites are functionally relevant (PubMed:10373108,
CC PubMed:11850430). {ECO:0000269|PubMed:10373108,
CC ECO:0000269|PubMed:11850430}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + succinate = a quinol + fumarate;
CC Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.4;
CC Evidence={ECO:0000269|PubMed:11850430};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a menaquinone + succinate = a menaquinol + fumarate;
CC Xref=Rhea:RHEA:27834, Rhea:RHEA-COMP:9537, Rhea:RHEA-COMP:9539,
CC ChEBI:CHEBI:16374, ChEBI:CHEBI:18151, ChEBI:CHEBI:29806,
CC ChEBI:CHEBI:30031; EC=1.3.5.4;
CC Evidence={ECO:0000305|PubMed:10373108};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:10373108};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:10373108};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000269|PubMed:10373108};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000269|PubMed:10373108};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:10373108};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:10373108};
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:0000269|PubMed:10373108,
CC ECO:0000269|PubMed:11850430}.
CC -!- INTERACTION:
CC P0AC47; P00363: frdA; NbExp=4; IntAct=EBI-906724, EBI-550480;
CC P0AC47; P08337: mutT; NbExp=4; IntAct=EBI-906724, EBI-1121389;
CC P0AC47; P0A915: ompW; NbExp=2; IntAct=EBI-906724, EBI-1132929;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:10373108}; Peripheral membrane protein
CC {ECO:0000305|PubMed:10373108}; Cytoplasmic side
CC {ECO:0000305|PubMed:10373108}.
CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase
CC iron-sulfur protein family. {ECO:0000305}.
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DR EMBL; J01611; AAA23438.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97052.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77113.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78157.1; -; Genomic_DNA.
DR EMBL; V00277; CAA23534.1; -; Genomic_DNA.
DR PIR; A00377; RDECFS.
DR RefSeq; NP_418577.1; NC_000913.3.
DR RefSeq; WP_000829498.1; NZ_STEB01000014.1.
DR PDB; 1KF6; X-ray; 2.70 A; B/N=2-244.
DR PDB; 1KFY; X-ray; 3.60 A; B/N=2-244.
DR PDB; 1L0V; X-ray; 3.30 A; B/N=2-244.
DR PDB; 2B76; X-ray; 3.30 A; B/N=2-244.
DR PDB; 3CIR; X-ray; 3.65 A; B/N=2-244.
DR PDB; 3P4P; X-ray; 2.80 A; B/N=2-244.
DR PDB; 3P4Q; X-ray; 3.35 A; B/N=2-244.
DR PDB; 3P4R; X-ray; 3.05 A; B/N=2-244.
DR PDB; 3P4S; X-ray; 3.10 A; B/N=2-244.
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 AlphaFoldDB; P0AC47; -.
DR SMR; P0AC47; -.
DR BioGRID; 4262701; 452.
DR BioGRID; 852958; 2.
DR ComplexPortal; CPX-1967; Plasma membrane fumarate reductase complex.
DR DIP; DIP-9682N; -.
DR IntAct; P0AC47; 7.
DR STRING; 511145.b4153; -.
DR DrugBank; DB07490; 2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL.
DR DrugBank; DB07918; 2-heptyl-4-hydroxyquinoline N-oxide.
DR jPOST; P0AC47; -.
DR PaxDb; P0AC47; -.
DR PRIDE; P0AC47; -.
DR EnsemblBacteria; AAC77113; AAC77113; b4153.
DR EnsemblBacteria; BAE78157; BAE78157; BAE78157.
DR GeneID; 67414773; -.
DR GeneID; 948666; -.
DR KEGG; ecj:JW4114; -.
DR KEGG; eco:b4153; -.
DR PATRIC; fig|1411691.4.peg.2545; -.
DR EchoBASE; EB0327; -.
DR eggNOG; COG0479; Bacteria.
DR HOGENOM; CLU_044838_3_2_6; -.
DR InParanoid; P0AC47; -.
DR OMA; AFASDCR; -.
DR PhylomeDB; P0AC47; -.
DR BioCyc; EcoCyc:FUM-FE-S; -.
DR BioCyc; MetaCyc:FUM-FE-S; -.
DR EvolutionaryTrace; P0AC47; -.
DR PRO; PR:P0AC47; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0045284; C:plasma membrane fumarate reductase complex; IDA:EcoCyc.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0009055; F:electron transfer activity; IDA:EcoCyc.
DR GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; ISM:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009061; P:anaerobic respiration; IMP:EcoCyc.
DR GO; GO:0044780; P:bacterial-type flagellum assembly; IMP:EcoCyc.
DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IMP:EcoCyc.
DR GO; GO:0006113; P:fermentation; IMP:EcoCyc.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 1.10.1060.10; -; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR004489; Succ_DH/fum_Rdtase_Fe-S.
DR InterPro; IPR025192; Succ_DH/fum_Rdtase_N.
DR Pfam; PF13085; Fer2_3; 1.
DR Pfam; PF13183; Fer4_8; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR TIGRFAMs; TIGR00384; dhsB; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; 3Fe-4S; 4Fe-4S; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Oxidoreductase; Reference proteome; Transport;
KW Tricarboxylic acid cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6751816"
FT CHAIN 2..244
FT /note="Fumarate reductase iron-sulfur subunit"
FT /id="PRO_0000158698"
FT DOMAIN 16..97
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 140..169
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 14
FT /ligand="a menaquinone"
FT /ligand_id="ChEBI:CHEBI:16374"
FT /evidence="ECO:0000269|PubMed:10373108,
FT ECO:0007744|PDB:1L0V"
FT BINDING 58
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:10373108,
FT ECO:0007744|PDB:1KF6, ECO:0007744|PDB:1KFY,
FT ECO:0007744|PDB:1L0V"
FT BINDING 63
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:10373108,
FT ECO:0007744|PDB:1KF6, ECO:0007744|PDB:1KFY,
FT ECO:0007744|PDB:1L0V"
FT BINDING 66
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:10373108,
FT ECO:0007744|PDB:1KF6, ECO:0007744|PDB:1KFY,
FT ECO:0007744|PDB:1L0V"
FT BINDING 78
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:10373108,
FT ECO:0007744|PDB:1KF6, ECO:0007744|PDB:1KFY,
FT ECO:0007744|PDB:1L0V"
FT BINDING 149
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:10373108,
FT ECO:0007744|PDB:1KF6, ECO:0007744|PDB:1KFY,
FT ECO:0007744|PDB:1L0V"
FT BINDING 152
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:10373108,
FT ECO:0007744|PDB:1KF6, ECO:0007744|PDB:1KFY,
FT ECO:0007744|PDB:1L0V"
FT BINDING 155
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:10373108,
FT ECO:0007744|PDB:1KF6, ECO:0007744|PDB:1KFY,
FT ECO:0007744|PDB:1L0V"
FT BINDING 159
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000269|PubMed:10373108,
FT ECO:0007744|PDB:1KF6, ECO:0007744|PDB:1KFY,
FT ECO:0007744|PDB:1L0V"
FT BINDING 205
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000269|PubMed:10373108,
FT ECO:0007744|PDB:1KF6, ECO:0007744|PDB:1KFY,
FT ECO:0007744|PDB:1L0V"
FT BINDING 211
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000269|PubMed:10373108,
FT ECO:0007744|PDB:1KF6, ECO:0007744|PDB:1KFY,
FT ECO:0007744|PDB:1L0V"
FT BINDING 215
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:10373108,
FT ECO:0007744|PDB:1KF6, ECO:0007744|PDB:1KFY,
FT ECO:0007744|PDB:1L0V"
FT BINDING 226..229
FT /ligand="a menaquinone"
FT /ligand_id="ChEBI:CHEBI:16374"
FT /evidence="ECO:0000269|PubMed:10373108,
FT ECO:0007744|PDB:1L0V"
FT MUTAGEN 58
FT /note="C->S: Affects center 1 (2Fe-2S)."
FT /evidence="ECO:0000269|PubMed:2174169"
FT MUTAGEN 63
FT /note="C->S: Affects center 1 (2Fe-2S)."
FT /evidence="ECO:0000269|PubMed:2174169"
FT MUTAGEN 66
FT /note="C->S: Affects center 1 (2Fe-2S)."
FT /evidence="ECO:0000269|PubMed:2174169"
FT MUTAGEN 78
FT /note="C->S: Affects center 1 (2Fe-2S)."
FT /evidence="ECO:0000269|PubMed:2174169"
FT STRAND 5..13
FT /evidence="ECO:0007829|PDB:1KF6"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:1KF6"
FT STRAND 23..31
FT /evidence="ECO:0007829|PDB:1KF6"
FT HELIX 37..47
FT /evidence="ECO:0007829|PDB:1KF6"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:1KF6"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:1KF6"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:1KF6"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:1KF6"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:1KF6"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:1KF6"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1KF6"
FT HELIX 108..116
FT /evidence="ECO:0007829|PDB:1KF6"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:1KF6"
FT HELIX 137..141
FT /evidence="ECO:0007829|PDB:1KF6"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:1KF6"
FT HELIX 154..158
FT /evidence="ECO:0007829|PDB:1KF6"
FT HELIX 160..164
FT /evidence="ECO:0007829|PDB:1KF6"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:3P4S"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:1KF6"
FT HELIX 190..197
FT /evidence="ECO:0007829|PDB:1KF6"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:1KF6"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:1KF6"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:1KF6"
FT HELIX 221..240
FT /evidence="ECO:0007829|PDB:1KF6"
SQ SEQUENCE 244 AA; 27123 MW; AC1D7A73244D7AC0 CRC64;
MAEMKNLKIE VVRYNPEVDT APHSAFYEVP YDATTSLLDA LGYIKDNLAP DLSYRWSCRM
AICGSCGMMV NNVPKLACKT FLRDYTDGMK VEALANFPIE RDLVVDMTHF IESLEAIKPY
IIGNSRTADQ GTNIQTPAQM AKYHQFSGCI NCGLCYAACP QFGLNPEFIG PAAITLAHRY
NEDSRDHGKK ERMAQLNSQN GVWSCTFVGY CSEVCPKHVD PAAAIQQGKV ESSKDFLIAT
LKPR
