FRDC_WOLSU
ID FRDC_WOLSU Reviewed; 256 AA.
AC P17413;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Fumarate reductase cytochrome b subunit;
DE AltName: Full=Quinol-fumarate reductase cytochrome b subunit {ECO:0000303|PubMed:10586875};
DE Short=QFR cytochrome b subunit {ECO:0000303|PubMed:10586875};
GN Name=frdC; OrderedLocusNames=WS0832;
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], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2388563; DOI=10.1111/j.1365-2958.1990.tb00657.x;
RA Koertner C., Lauterbach F., Tripier D., Unden G., Kroeger A.;
RT "Wolinella succinogenes fumarate reductase contains a dihaem cytochrome
RT b.";
RL Mol. Microbiol. 4:855-860(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF HIS-44;
RP HIS-93; HIS-114; HIS-120; HIS-143 AND HIS-182.
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 205-256.
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 [5] {ECO:0007744|PDB:1QLB}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH HEME, COFACTOR,
RP SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
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 [6] {ECO:0007744|PDB:1E7P}
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH HEME, FUNCTION,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
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).
RN [7]
RP REVIEW.
RX PubMed=11532445; DOI=10.1016/s0014-5793(01)02706-5;
RA Lancaster C.R.D.;
RT "Succinate:quinone oxidoreductases -- what can we learn from Wolinella
RT succinogenes quinol:fumarate reductase?";
RL FEBS Lett. 504:133-141(2001).
CC -!- FUNCTION: The fumarate reductase enzyme complex is required for
CC fumarate respiration using formate or sulfide as electron donor. This
CC subunit anchors the complex in the membrane and binds a diheme
CC cytochrome b. {ECO:0000269|PubMed:11248702,
CC ECO:0000269|PubMed:9492313}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:10586875, ECO:0000269|PubMed:11248702};
CC Note=Binds 2 heme b molecules per subunit, called the proximal (bP) and
CC distal (bD) hemes. {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}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:10586875,
CC ECO:0000269|PubMed:11248702}.
CC -!- SIMILARITY: Belongs to the diheme cytochrome b FrdC family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ000662; CAA04213.1; -; Genomic_DNA.
DR EMBL; BX571659; CAE09943.1; -; Genomic_DNA.
DR PIR; S10164; S10164.
DR RefSeq; WP_011138740.1; NC_005090.1.
DR PDB; 1E7P; X-ray; 3.10 A; C/F/I/L=1-256.
DR PDB; 1QLB; X-ray; 2.33 A; C/F=1-256.
DR PDB; 2BS2; X-ray; 1.78 A; C/F=1-254.
DR PDB; 2BS3; X-ray; 2.19 A; C/F=1-256.
DR PDB; 2BS4; X-ray; 2.76 A; C/F=1-256.
DR PDBsum; 1E7P; -.
DR PDBsum; 1QLB; -.
DR PDBsum; 2BS2; -.
DR PDBsum; 2BS3; -.
DR PDBsum; 2BS4; -.
DR AlphaFoldDB; P17413; -.
DR SMR; P17413; -.
DR STRING; 273121.WS0832; -.
DR DrugBank; DB07669; 2,3-Dimethyl-1,4-naphthoquinone.
DR TCDB; 3.D.10.1.3; the prokaryotic succinate dehydrogenase (sdh) family.
DR EnsemblBacteria; CAE09943; CAE09943; WS0832.
DR KEGG; wsu:WS0832; -.
DR eggNOG; ENOG5031HUY; Bacteria.
DR HOGENOM; CLU_075821_0_0_7; -.
DR OMA; LLAHLHF; -.
DR OrthoDB; 1073274at2; -.
DR BRENDA; 1.3.5.4; 6642.
DR EvolutionaryTrace; P17413; -.
DR Proteomes; UP000000422; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd00581; QFR_TypeB_TM; 1.
DR Gene3D; 1.20.1300.10; -; 1.
DR InterPro; IPR004224; Fum_red_B_TM.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR Pfam; PF01127; Sdh_cyt; 1.
DR PIRSF; PIRSF000177; Fumar_rd_cyt_b; 1.
DR SUPFAM; SSF81343; SSF81343; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Reference proteome; Respiratory chain; Transmembrane;
KW Transmembrane helix; Transport; Tricarboxylic acid cycle.
FT CHAIN 1..256
FT /note="Fumarate reductase cytochrome b subunit"
FT /id="PRO_0000158685"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10586875"
FT TRANSMEM 31..52
FT /note="Helical"
FT TOPO_DOM 53..76
FT /note="Periplasmic"
FT TRANSMEM 77..98
FT /note="Helical"
FT TOPO_DOM 99..124
FT /note="Cytoplasmic"
FT TRANSMEM 125..149
FT /note="Helical"
FT TOPO_DOM 150..165
FT /note="Periplasmic"
FT TRANSMEM 166..188
FT /note="Helical"
FT TOPO_DOM 189..206
FT /note="Cytoplasmic"
FT TRANSMEM 207..230
FT /note="Helical"
FT TOPO_DOM 231..256
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:10586875"
FT BINDING 44
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="bD"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
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 93
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="bP"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
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 143
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="bD"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
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 182
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="bP"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
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 MUTAGEN 44
FT /note="H->A: Loss of fumarate reductase activity."
FT /evidence="ECO:0000269|PubMed:9492313"
FT MUTAGEN 93
FT /note="H->A: Loss of fumarate reductase activity."
FT /evidence="ECO:0000269|PubMed:9492313"
FT MUTAGEN 114
FT /note="H->A: Slight reduction in fumarate reductase
FT activity."
FT /evidence="ECO:0000269|PubMed:9492313"
FT MUTAGEN 120
FT /note="H->A: Reduction in fumarate reductase activity."
FT /evidence="ECO:0000269|PubMed:9492313"
FT MUTAGEN 143
FT /note="H->A,M,K: Loss of fumarate reductase activity."
FT /evidence="ECO:0000269|PubMed:9492313"
FT MUTAGEN 182
FT /note="H->A: Loss of fumarate reductase activity."
FT /evidence="ECO:0000269|PubMed:9492313"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 22..48
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 55..64
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1QLB"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 77..97
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 105..118
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 121..149
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 158..164
FT /evidence="ECO:0007829|PDB:2BS2"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:1QLB"
FT HELIX 169..194
FT /evidence="ECO:0007829|PDB:2BS2"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 202..235
FT /evidence="ECO:0007829|PDB:2BS2"
FT TURN 246..252
FT /evidence="ECO:0007829|PDB:2BS2"
SQ SEQUENCE 256 AA; 29723 MW; E8459B884BA9E20B CRC64;
MTNESILESY SGVTPERKKS RMPAKLDWWQ SATGLFLGLF MIGHMFFVST ILLGDNVMLW
VTKKFELDFI FEGGKPIVVS FLAAFVFAVF IAHAFLAMRK FPINYRQYLT FKTHKDLMRH
GDTTLWWIQA MTGFAMFFLG SVHLYIMMTQ PQTIGPVSSS FRMVSEWMWP LYLVLLFAVE
LHGSVGLYRL AVKWGWFDGE TPDKTRANLK KLKTLMSAFL IVLGLLTFGA YVKKGLEQTD
PNIDYKYFDY KRTHHR
