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Database: UniProt
Entry: O06914
LinkDB: O06914
Original site: O06914 
ID   FRDB_HELPY              Reviewed;         245 AA.
AC   O06914;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   10-APR-2019, entry version 129.
DE   RecName: Full=Fumarate reductase iron-sulfur subunit;
DE            EC=1.3.5.1;
GN   Name=frdB; OrderedLocusNames=HP_0191;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter
OS   pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43629 / JCM 7656 / NCTC 11639 / UA802;
RX   PubMed=9434188; DOI=10.1016/S0378-1119(97)00550-7;
RA   Ge Z., Jiang Q., Kalisiak M.S., Taylor D.E.;
RT   "Cloning and functional characterization of Helicobacter pylori
RT   fumarate reductase operon comprising three structural genes coding for
RT   subunits C, A and B.";
RL   Gene 204:227-234(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R.,
RA   Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F.,
RA   Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G.,
RA   Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D.,
RA   Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D.,
RA   Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C.,
RA   Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D.,
RA   Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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=1.3.5.1;
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC   -!- SUBUNIT: Part of an enzyme complex containing three subunits: a
CC       flavoprotein, an iron-sulfur, and cytochrome b-556. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate
CC       reductase iron-sulfur protein family. {ECO:0000305}.
DR   EMBL; U78101; AAC46065.1; -; Genomic_DNA.
DR   EMBL; AE000511; AAD07258.1; -; Genomic_DNA.
DR   PIR; G64543; G64543.
DR   RefSeq; NP_206990.1; NC_000915.1.
DR   RefSeq; WP_001282439.1; NC_018939.1.
DR   ProteinModelPortal; O06914; -.
DR   SMR; O06914; -.
DR   IntAct; O06914; 13.
DR   STRING; 85962.C694_00950; -.
DR   PaxDb; O06914; -.
DR   EnsemblBacteria; AAD07258; AAD07258; HP_0191.
DR   GeneID; 899155; -.
DR   KEGG; heo:C694_00950; -.
DR   KEGG; hpy:HP0191; -.
DR   PATRIC; fig|85962.47.peg.206; -.
DR   eggNOG; ENOG4105E33; Bacteria.
DR   eggNOG; COG0479; LUCA.
DR   KO; K00245; -.
DR   OMA; CPKGISL; -.
DR   BioCyc; HPY:HP0191-MONOMER; -.
DR   BioCyc; MetaCyc:HP0191-MONOMER; -.
DR   Proteomes; UP000000429; Chromosome.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR   GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
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; SSF46548; SSF46548; 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   3: Inferred from homology;
KW   2Fe-2S; 3Fe-4S; 4Fe-4S; Complete proteome; Electron transport; Iron;
KW   Iron-sulfur; Metal-binding; Oxidoreductase; Reference proteome;
KW   Transport; Tricarboxylic acid cycle.
FT   CHAIN         1    245       Fumarate reductase iron-sulfur subunit.
FT                                /FTId=PRO_0000158703.
FT   DOMAIN       17     98       2Fe-2S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00465}.
FT   DOMAIN      145    174       4Fe-4S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        60     60       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL        65     65       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL        68     68       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL        80     80       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL       154    154       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       157    157       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       160    160       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       164    164       Iron-sulfur 3 (3Fe-4S). {ECO:0000250}.
FT   METAL       211    211       Iron-sulfur 3 (3Fe-4S). {ECO:0000250}.
FT   METAL       217    217       Iron-sulfur 3 (3Fe-4S). {ECO:0000250}.
FT   METAL       221    221       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   CONFLICT    140    140       V -> I (in Ref. 1; AAC46065).
FT                                {ECO:0000305}.
FT   CONFLICT    194    194       N -> S (in Ref. 1; AAC46065).
FT                                {ECO:0000305}.
SQ   SEQUENCE   245 AA;  27652 MW;  D54447471FB4C499 CRC64;
     MSDNERTIVV RVLKFDPQSA VSKPHFKEYQ LKETPSMTLF IALNLIREHQ DPDLSFDFVC
     RAGICGSCAM MVNGRPRLAC KTLTSSFESG VITLMPMPSF TLIKDLSVNT GDWFLDMTKR
     VESWAHSKEE VDITRPEKRV EPDEAQEVFE LDRCIECGCC IASCGTKLMR PNFIGAAGMN
     RAMRFMIDSH DERNDDDFYE LVGDDDGVFG CMSLIACHDT CPKELPLQSS IATLRNRMLK
     VGKSR
//
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