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   27-MAR-2024, entry version 144.
DE   RecName: Full=Fumarate reductase iron-sulfur subunit;
DE            EC=1.3.5.1 {ECO:0000250|UniProtKB:P17596};
DE   AltName: Full=Quinol-fumarate reductase iron-sulfur subunit;
DE            Short=QFR iron-sulfur subunit;
GN   Name=frdB; OrderedLocusNames=jhp_0177;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Campylobacterota; 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., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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=1.3.5.1;
CC         Evidence={ECO:0000250|UniProtKB:P17596};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000250|UniProtKB:P17596};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250|UniProtKB:P17596};
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000250|UniProtKB:P17596};
CC       Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250|UniProtKB:P17596};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:P17596};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P17596};
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:0000250|UniProtKB:P17596}.
CC   -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase
CC       iron-sulfur protein family. {ECO:0000305}.
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DR   EMBL; AE001439; AAD05761.1; -; Genomic_DNA.
DR   PIR; F71963; F71963.
DR   RefSeq; WP_001282415.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZMP1; -.
DR   SMR; Q9ZMP1; -.
DR   IntAct; Q9ZMP1; 1.
DR   KEGG; hpj:jhp_0177; -.
DR   PATRIC; fig|85963.30.peg.844; -.
DR   eggNOG; COG0479; Bacteria.
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:0102040; F:fumarate reductase (menaquinone); IEA:RHEA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 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   NCBIfam; TIGR00384; dhsB; 1.
DR   PANTHER; PTHR11921:SF36; FUMARATE REDUCTASE IRON-SULFUR SUBUNIT; 1.
DR   PANTHER; PTHR11921; SUCCINATE DEHYDROGENASE IRON-SULFUR PROTEIN; 1.
DR   Pfam; PF13085; Fer2_3; 1.
DR   Pfam; PF13183; Fer4_8; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 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; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; Oxidoreductase; Transport; Tricarboxylic acid cycle.
FT   CHAIN           1..245
FT                   /note="Fumarate reductase iron-sulfur subunit"
FT                   /id="PRO_0000158704"
FT   DOMAIN          17..98
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   DOMAIN          145..174
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         60
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250|UniProtKB:P17596"
FT   BINDING         65
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250|UniProtKB:P17596"
FT   BINDING         68
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250|UniProtKB:P17596"
FT   BINDING         80
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250|UniProtKB:P17596"
FT   BINDING         154
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P17596"
FT   BINDING         157
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P17596"
FT   BINDING         160
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P17596"
FT   BINDING         164
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250|UniProtKB:P17596"
FT   BINDING         211
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250|UniProtKB:P17596"
FT   BINDING         217
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250|UniProtKB:P17596"
FT   BINDING         221
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P17596"
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
//