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Database: UniProt
Entry: P17413
LinkDB: P17413
Original site: P17413 
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   08-MAY-2019, entry version 134.
DE   RecName: Full=Fumarate reductase cytochrome b subunit;
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
RT   cytochrome b.";
RL   Mol. Microbiol. 4:855-860(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF
RP   HIS-44; 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 / LMG 7466 / NCTC 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]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
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]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
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
RT   reductase 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.
CC       {ECO:0000269|PubMed:9492313}.
CC   -!- SUBUNIT: Part of an enzyme complex containing three subunits: a
CC       flavoprotein, an iron-sulfur protein, and cytochrome b-556.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
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   SMR; P17413; -.
DR   STRING; 273121.WS0832; -.
DR   TCDB; 3.D.10.1.3; the prokaryotic succinate dehydrogenase (sdh) family.
DR   EnsemblBacteria; CAE09943; CAE09943; WS0832.
DR   KEGG; wsu:WS0832; -.
DR   eggNOG; ENOG4108S24; Bacteria.
DR   eggNOG; COG2009; LUCA.
DR   HOGENOM; HOG000286335; -.
DR   KO; K00246; -.
DR   OMA; LLAHLHF; -.
DR   OrthoDB; 1073274at2; -.
DR   BioCyc; WSUC273121:G1GTD-800-MONOMER; -.
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 membrane; Complete proteome;
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       Fumarate reductase cytochrome b subunit.
FT                                /FTId=PRO_0000158685.
FT   TOPO_DOM      1     30       Cytoplasmic.
FT   TRANSMEM     31     52       Helical.
FT   TOPO_DOM     53     76       Periplasmic.
FT   TRANSMEM     77     98       Helical.
FT   TOPO_DOM     99    124       Cytoplasmic.
FT   TRANSMEM    125    149       Helical.
FT   TOPO_DOM    150    165       Periplasmic.
FT   TRANSMEM    166    188       Helical.
FT   TOPO_DOM    189    206       Cytoplasmic.
FT   TRANSMEM    207    230       Helical.
FT   TOPO_DOM    231    256       Periplasmic.
FT   METAL        44     44       Iron (heme axial ligand).
FT   METAL        93     93       Iron (heme axial ligand).
FT   METAL       143    143       Iron (heme axial ligand).
FT   METAL       182    182       Iron (heme axial ligand).
FT   MUTAGEN      44     44       H->A: Loss of fumarate reductase
FT                                activity. {ECO:0000269|PubMed:9492313}.
FT   MUTAGEN      93     93       H->A: Loss of fumarate reductase
FT                                activity. {ECO:0000269|PubMed:9492313}.
FT   MUTAGEN     114    114       H->A: Slight reduction in fumarate
FT                                reductase activity.
FT                                {ECO:0000269|PubMed:9492313}.
FT   MUTAGEN     120    120       H->A: Reduction in fumarate reductase
FT                                activity. {ECO:0000269|PubMed:9492313}.
FT   MUTAGEN     143    143       H->A,M,K: Loss of fumarate reductase
FT                                activity. {ECO:0000269|PubMed:9492313}.
FT   MUTAGEN     182    182       H->A: Loss of fumarate reductase
FT                                activity. {ECO:0000269|PubMed:9492313}.
FT   HELIX         3     11       {ECO:0000244|PDB:2BS2}.
FT   HELIX        22     48       {ECO:0000244|PDB:2BS2}.
FT   HELIX        49     52       {ECO:0000244|PDB:2BS2}.
FT   HELIX        55     64       {ECO:0000244|PDB:2BS2}.
FT   STRAND       65     67       {ECO:0000244|PDB:1QLB}.
FT   TURN         68     70       {ECO:0000244|PDB:2BS2}.
FT   STRAND       71     73       {ECO:0000244|PDB:2BS2}.
FT   HELIX        77     97       {ECO:0000244|PDB:2BS2}.
FT   HELIX        98    100       {ECO:0000244|PDB:2BS2}.
FT   HELIX       105    118       {ECO:0000244|PDB:2BS2}.
FT   HELIX       121    149       {ECO:0000244|PDB:2BS2}.
FT   HELIX       151    153       {ECO:0000244|PDB:2BS2}.
FT   HELIX       158    164       {ECO:0000244|PDB:2BS2}.
FT   TURN        165    167       {ECO:0000244|PDB:1QLB}.
FT   HELIX       169    194       {ECO:0000244|PDB:2BS2}.
FT   TURN        195    197       {ECO:0000244|PDB:2BS2}.
FT   HELIX       202    235       {ECO:0000244|PDB:2BS2}.
FT   TURN        246    252       {ECO:0000244|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
//
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