ID FRDB_MYCTO Reviewed; 247 AA. AC P9WN88; L0T766; Q10761; DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot. DT 16-APR-2014, sequence version 1. DT 24-JAN-2024, entry version 46. DE RecName: Full=Fumarate reductase iron-sulfur subunit; DE EC=1.3.5.1 {ECO:0000250|UniProtKB:P0AC47}; DE AltName: Full=Quinol-fumarate reductase iron-sulfur subunit; DE Short=QFR iron-sulfur subunit; GN Name=frdB; OrderedLocusNames=MT1604; OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=83331; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC 1551 / Oshkosh; RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002; RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A., RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.; RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and RT laboratory strains."; RL J. Bacteriol. 184:5479-5490(2002). 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 Evidence={ECO:0000250|UniProtKB:P0AC47}; 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:P0AC47}; CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; CC Evidence={ECO:0000250|UniProtKB:P0AC47}; CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250|UniProtKB:P0AC47}; CC -!- COFACTOR: CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; CC Evidence={ECO:0000250|UniProtKB:P0AC47}; CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250|UniProtKB:P0AC47}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250|UniProtKB:P0AC47}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P0AC47}; CC -!- SUBUNIT: Fumarate dehydrogenase forms part of an enzyme complex CC containing four subunits: a flavoprotein, an iron-sulfur, and two CC hydrophobic anchor proteins. {ECO:0000250|UniProtKB:P0AC47}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P0AC47}; CC Peripheral membrane protein {ECO:0000250|UniProtKB:P0AC47}; Cytoplasmic CC side {ECO:0000250|UniProtKB:P0AC47}. 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; AE000516; AAK45871.1; -; Genomic_DNA. DR PIR; F70762; F70762. DR RefSeq; WP_003407767.1; NZ_KK341227.1. DR AlphaFoldDB; P9WN88; -. DR SMR; P9WN88; -. DR KEGG; mtc:MT1604; -. DR PATRIC; fig|83331.31.peg.1726; -. DR HOGENOM; CLU_044838_3_2_11; -. DR Proteomes; UP000001020; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 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; 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; PTHR43551; FUMARATE REDUCTASE IRON-SULFUR SUBUNIT; 1. DR PANTHER; PTHR43551:SF2; FUMARATE REDUCTASE IRON-SULFUR SUBUNIT; 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; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 1. PE 3: Inferred from homology; KW 2Fe-2S; 3Fe-4S; 4Fe-4S; Cell membrane; Electron transport; Iron; KW Iron-sulfur; Membrane; Metal-binding; Oxidoreductase; Reference proteome; KW Transport; Tricarboxylic acid cycle. FT CHAIN 1..247 FT /note="Fumarate reductase iron-sulfur subunit" FT /id="PRO_0000427169" FT DOMAIN 14..94 FT /note="2Fe-2S ferredoxin-type" FT DOMAIN 140..169 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 12 FT /ligand="a menaquinone" FT /ligand_id="ChEBI:CHEBI:16374" FT /evidence="ECO:0000250|UniProtKB:P0AC47" FT BINDING 56 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250|UniProtKB:P0AC47" FT BINDING 61 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250|UniProtKB:P0AC47" FT BINDING 76 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250|UniProtKB:P0AC47" FT BINDING 149 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250|UniProtKB:P0AC47" FT BINDING 152 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250|UniProtKB:P0AC47" FT BINDING 155 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250|UniProtKB:P0AC47" FT BINDING 159 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT /evidence="ECO:0000250|UniProtKB:P0AC47" FT BINDING 205 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT /evidence="ECO:0000250|UniProtKB:P0AC47" FT BINDING 211 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT /evidence="ECO:0000250|UniProtKB:P0AC47" FT BINDING 215 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250|UniProtKB:P0AC47" FT BINDING 226..229 FT /ligand="a menaquinone" FT /ligand_id="ChEBI:CHEBI:16374" FT /evidence="ECO:0000250|UniProtKB:P0AC47" SQ SEQUENCE 247 AA; 27234 MW; 15863DCCB2C82B0B CRC64; MMDRIVMEVS RYRPEIESAP TFQAYEVPLT REWAVLDGLT YIKDHLDGTL SFRWSCRMGI CGSSGMTING DPKLACATFL ADYLPGPVRV EPMRNFPVIR DLVVDISDFM AKLPSVKPWL VRHDEPPVED GEYRQTPAEL DAFKQFSMCI NCMLCYSACP VYALDPDFLG PAAIALGQRY NLDSRDQGAA DRRDVLAAAD GAWACTLVGE CSTACPKGVD PAGAIQRYKL TAATHALKKL LFPWGGG //