FRDB_WOLSU
ID FRDB_WOLSU Reviewed; 239 AA.
AC P17596;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 166.
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:10586875};
DE Short=QFR iron-sulfur subunit {ECO:0000303|PubMed:10586875};
GN Name=frdB; OrderedLocusNames=WS0830;
OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS 11488 / FDC 602W) (Vibrio succinogenes).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Wolinella.
OX NCBI_TaxID=273121;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2244791; DOI=10.1007/bf00276536;
RA Lauterbach F., Koertner C., Albracht S.P., Unden G., Kroeger A.;
RT "The fumarate reductase operon of Wolinella succinogenes. Sequence and
RT expression of the frdA and frdB genes.";
RL Arch. Microbiol. 154:386-393(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=9492313; DOI=10.1046/j.1432-1327.1998.2510418.x;
RA Simon J., Gross R., Ringel M., Schmidt E., Kroeger A.;
RT "Deletion and site-directed mutagenesis of the Wolinella succinogenes
RT fumarate reductase operon.";
RL Eur. J. Biochem. 251:418-426(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC 11488 / FDC 602W;
RX PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA Meyer F., Lederer H., Schuster S.C.;
RT "Complete genome sequence and analysis of Wolinella succinogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
RN [4] {ECO:0007744|PDB:1QLB}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (2FE-2S);
RP IRON-SULFUR (3FE-4S) AND IRON-SULFUR (4FE-4S), SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10586875; DOI=10.1038/46483;
RA Lancaster C.R.D., Kroeger A., Auer M., Michel H.;
RT "Structure of fumarate reductase from Wolinella succinogenes at 2.2 A
RT resolution.";
RL Nature 402:377-385(1999).
RN [5] {ECO:0007744|PDB:1E7P}
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (2FE-2S);
RP IRON-SULFUR (3FE-4S) AND IRON-SULFUR (4FE-4S), AND FUNCTION.
RX PubMed=11248702; DOI=10.1046/j.1432-1033.2001.02053.x;
RA Lancaster C.R.D., Gross R., Simon J.;
RT "A third crystal form of Wolinella succinogenes quinol:fumarate reductase
RT reveals domain closure at the site of fumarate reduction.";
RL Eur. J. Biochem. 268:1820-1827(2001).
CC -!- FUNCTION: The fumarate reductase enzyme complex is required for
CC fumarate respiration using formate or sulfide as electron donor.
CC {ECO:0000269|PubMed:10586875, ECO:0000269|PubMed:11248702,
CC ECO:0000269|PubMed:9492313}.
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:0000250|UniProtKB:P0AC47};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:10586875, ECO:0000269|PubMed:11248702};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:10586875,
CC ECO:0000269|PubMed:11248702};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000269|PubMed:10586875, ECO:0000269|PubMed:11248702};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000269|PubMed:10586875,
CC ECO:0000269|PubMed:11248702};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:10586875, ECO:0000269|PubMed:11248702};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:10586875,
CC ECO:0000269|PubMed:11248702};
CC -!- SUBUNIT: Part of an enzyme complex containing three subunits: a
CC flavoprotein (frdA), an iron-sulfur protein (frdB), and diheme
CC cytochrome b (frdC). {ECO:0000269|PubMed:10586875}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305|PubMed:10586875}; Cytoplasmic side
CC {ECO:0000305|PubMed:10586875}.
CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase
CC iron-sulfur protein family. {ECO:0000305}.
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DR EMBL; AJ000662; CAA04215.1; -; Genomic_DNA.
DR EMBL; BX571659; CAE09941.1; -; Genomic_DNA.
DR PIR; C44954; C44954.
DR RefSeq; WP_011138738.1; NC_005090.1.
DR PDB; 1E7P; X-ray; 3.10 A; B/E/H/K=1-239.
DR PDB; 1QLB; X-ray; 2.33 A; B/E=1-239.
DR PDB; 2BS2; X-ray; 1.78 A; B/E=1-239.
DR PDB; 2BS3; X-ray; 2.19 A; B/E=1-239.
DR PDB; 2BS4; X-ray; 2.76 A; B/E=1-239.
DR PDBsum; 1E7P; -.
DR PDBsum; 1QLB; -.
DR PDBsum; 2BS2; -.
DR PDBsum; 2BS3; -.
DR PDBsum; 2BS4; -.
DR AlphaFoldDB; P17596; -.
DR SMR; P17596; -.
DR STRING; 273121.WS0830; -.
DR DrugBank; DB07669; 2,3-Dimethyl-1,4-naphthoquinone.
DR TCDB; 3.D.10.1.3; the prokaryotic succinate dehydrogenase (sdh) family.
DR EnsemblBacteria; CAE09941; CAE09941; WS0830.
DR KEGG; wsu:WS0830; -.
DR eggNOG; COG0479; Bacteria.
DR HOGENOM; CLU_044838_3_3_7; -.
DR OMA; KYDPLVW; -.
DR OrthoDB; 1605514at2; -.
DR BRENDA; 1.3.5.4; 6642.
DR EvolutionaryTrace; P17596; -.
DR Proteomes; UP000000422; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
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 Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Respiratory chain; Transport;
KW Tricarboxylic acid cycle.
FT CHAIN 1..239
FT /note="Fumarate reductase iron-sulfur subunit"
FT /id="PRO_0000158708"
FT DOMAIN 5..95
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 142..171
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 57
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:10586875,
FT ECO:0000269|PubMed:11248702, ECO:0007744|PDB:1E7P,
FT ECO:0007744|PDB:1QLB, ECO:0007744|PDB:2BS2,
FT ECO:0007744|PDB:2BS3, ECO:0007744|PDB:2BS4"
FT BINDING 62
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:10586875,
FT ECO:0000269|PubMed:11248702, ECO:0007744|PDB:1E7P,
FT ECO:0007744|PDB:1QLB, ECO:0007744|PDB:2BS2,
FT ECO:0007744|PDB:2BS3, ECO:0007744|PDB:2BS4"
FT BINDING 65
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:10586875,
FT ECO:0000269|PubMed:11248702, ECO:0007744|PDB:1E7P,
FT ECO:0007744|PDB:1QLB, ECO:0007744|PDB:2BS2,
FT ECO:0007744|PDB:2BS3, ECO:0007744|PDB:2BS4"
FT BINDING 77
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:10586875,
FT ECO:0000269|PubMed:11248702, ECO:0007744|PDB:1E7P,
FT ECO:0007744|PDB:1QLB, ECO:0007744|PDB:2BS2,
FT ECO:0007744|PDB:2BS3, ECO:0007744|PDB:2BS4"
FT BINDING 151
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:10586875,
FT ECO:0000269|PubMed:11248702, ECO:0007744|PDB:1E7P,
FT ECO:0007744|PDB:1QLB, ECO:0007744|PDB:2BS2,
FT ECO:0007744|PDB:2BS3, ECO:0007744|PDB:2BS4"
FT BINDING 154
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:10586875,
FT ECO:0000269|PubMed:11248702, ECO:0007744|PDB:1E7P,
FT ECO:0007744|PDB:1QLB, ECO:0007744|PDB:2BS2,
FT ECO:0007744|PDB:2BS3, ECO:0007744|PDB:2BS4"
FT BINDING 157
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:10586875,
FT ECO:0000269|PubMed:11248702, ECO:0007744|PDB:1E7P,
FT ECO:0007744|PDB:1QLB, ECO:0007744|PDB:2BS2,
FT ECO:0007744|PDB:2BS3, ECO:0007744|PDB:2BS4"
FT BINDING 161
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000269|PubMed:10586875,
FT ECO:0000269|PubMed:11248702, ECO:0007744|PDB:1E7P,
FT ECO:0007744|PDB:1QLB, ECO:0007744|PDB:2BS2,
FT ECO:0007744|PDB:2BS3, ECO:0007744|PDB:2BS4"
FT BINDING 208
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000269|PubMed:10586875,
FT ECO:0000269|PubMed:11248702, ECO:0007744|PDB:1E7P,
FT ECO:0007744|PDB:1QLB, ECO:0007744|PDB:2BS2,
FT ECO:0007744|PDB:2BS3, ECO:0007744|PDB:2BS4"
FT BINDING 214
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000269|PubMed:10586875,
FT ECO:0000269|PubMed:11248702, ECO:0007744|PDB:1E7P,
FT ECO:0007744|PDB:1QLB, ECO:0007744|PDB:2BS2,
FT ECO:0007744|PDB:2BS3, ECO:0007744|PDB:2BS4"
FT BINDING 218
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:10586875,
FT ECO:0000269|PubMed:11248702, ECO:0007744|PDB:1E7P,
FT ECO:0007744|PDB:1QLB, ECO:0007744|PDB:2BS2,
FT ECO:0007744|PDB:2BS3, ECO:0007744|PDB:2BS4"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 22..29
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:1E7P"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 162..166
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:2BS2"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 213..217
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 224..235
FT /evidence="ECO:0007829|PDB:2BS2"
SQ SEQUENCE 239 AA; 27165 MW; 24D1992489B8FFD1 CRC64;
MGRMLTIRVF KYDPQSAVSK PHFQEYKIEE APSMTIFIVL NMIRETYDPD LNFDFVCRAG
ICGSCGMMIN GRPSLACRTL TKDFEDGVIT LLPLPAFKLI KDLSVDTGNW FNGMSQRVES
WIHAQKEHDI SKLEERIEPE VAQEVFELDR CIECGCCIAA CGTKIMREDF VGAAGLNRVV
RFMIDPHDER TDEDYYELIG DDDGVFGCMT LLACHDVCPK NLPLQSKIAY LRRKMVSVN
