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 27-MAR-2024, entry version 149. 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=HP_0191; OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori). OC Bacteria; Campylobacterota; 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 fumarate RT reductase operon comprising three structural genes coding for subunits C, A RT 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., Dougherty B.A., RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A., RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., RA Borodovsky M., Karp P.D., 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 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}. 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; 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 AlphaFoldDB; O06914; -. DR SMR; O06914; -. DR IntAct; O06914; 13. DR STRING; 85962.HP_0191; -. DR PaxDb; 85962-C694_00950; -. DR EnsemblBacteria; AAD07258; AAD07258; HP_0191. DR KEGG; hpy:HP_0191; -. DR PATRIC; fig|85962.47.peg.206; -. DR eggNOG; COG0479; Bacteria. DR InParanoid; O06914; -. DR OrthoDB; 9804391at2; -. DR PhylomeDB; O06914; -. 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:0102040; F:fumarate reductase (menaquinone); IEA:RHEA. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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 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; Reference proteome; Transport; KW Tricarboxylic acid cycle. FT CHAIN 1..245 FT /note="Fumarate reductase iron-sulfur subunit" FT /id="PRO_0000158703" 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" FT CONFLICT 140 FT /note="V -> I (in Ref. 1; AAC46065)" FT /evidence="ECO:0000305" FT CONFLICT 194 FT /note="N -> S (in Ref. 1; AAC46065)" FT /evidence="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 //