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Database: UniProt
Entry: Q9ZMP1
LinkDB: Q9ZMP1
Original site: Q9ZMP1 
ID   FRDB_HELPJ              Reviewed;         245 AA.
AC   Q9ZMP1;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   10-APR-2019, entry version 127.
DE   RecName: Full=Fumarate reductase iron-sulfur subunit;
DE            EC=1.3.5.1;
GN   Name=frdB; OrderedLocusNames=jhp_0177;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori
OS   J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G.,
RA   Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C.,
RA   Gibson R., Merberg D., Mills S.D., Jiang Q., Taylor D.E., Vovis G.F.,
RA   Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human
RT   gastric pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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; AE001439; AAD05761.1; -; Genomic_DNA.
DR   PIR; F71963; F71963.
DR   RefSeq; WP_001282415.1; NZ_CP011330.1.
DR   ProteinModelPortal; Q9ZMP1; -.
DR   SMR; Q9ZMP1; -.
DR   IntAct; Q9ZMP1; 1.
DR   STRING; 85963.jhp_0177; -.
DR   EnsemblBacteria; AAD05761; AAD05761; jhp_0177.
DR   KEGG; hpj:jhp_0177; -.
DR   PATRIC; fig|85963.30.peg.844; -.
DR   eggNOG; ENOG4105E33; Bacteria.
DR   eggNOG; COG0479; LUCA.
DR   KO; K00245; -.
DR   OMA; CPKGISL; -.
DR   BioCyc; HPYL85963:G1G1A-198-MONOMER; -.
DR   Proteomes; UP000000804; 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: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; Transport;
KW   Tricarboxylic acid cycle.
FT   CHAIN         1    245       Fumarate reductase iron-sulfur subunit.
FT                                /FTId=PRO_0000158704.
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}.
SQ   SEQUENCE   245 AA;  27625 MW;  D400D302E279DB4B CRC64;
     MSDNERTIVV RVLKFDPQSA VNKPHFKEYQ LKETPSMTLF IALNLIREHQ DPDLSFDFVC
     RAGICGSCAM MVNGRPRLAC KTLTSSFENG VITLMPMPSF TLIKDLSVNT GDWFSDMTKR
     VESWAHSKEE VDITKPEKRV EPDEAQEVFE LDRCIECGCC IASCGTKLMR PNFIGAAGMN
     RAMRFMIDSH DERSDDDFYE LVGDDDGVFG CMSLIACHDT CPKELPLQSS IATLRNRMLK
     VGKSR
//
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