ID FRDB_MYCTU Reviewed; 247 AA. AC Q10761; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 25-NOV-2008, entry version 67. DE RecName: Full=Fumarate reductase iron-sulfur subunit; DE EC=1.3.99.1; GN Name=frdB; OrderedLocusNames=Rv1553, MT1604; ORFNames=MTCY48.12c; OS Mycobacterium tuberculosis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=1773; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv; RX MEDLINE=98295987; PubMed=9634230; DOI=10.1038/31159; RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., RA Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, RA Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., RA Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., RA Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., RA Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., RA Sulston J.E., Taylor K., Whitehead S., Barrell B.G.; RT "Deciphering the biology of Mycobacterium tuberculosis from the RT complete genome sequence."; RL Nature 393:537-544(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC 1551 / Oshkosh; RX MEDLINE=22206494; PubMed=12218036; RX 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., RA Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., RA Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., RA Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., RA 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: Succinate + acceptor = fumarate + reduced CC acceptor. CC -!- COFACTOR: Binds 1 2Fe-2S cluster (By similarity). CC -!- COFACTOR: Binds 1 3Fe-4S cluster (By similarity). CC -!- COFACTOR: Binds 1 4Fe-4S cluster (By similarity). 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 (By similarity). CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate CC reductase iron-sulfur protein family. CC -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain. CC -!- SIMILARITY: Contains 1 4Fe-4S ferredoxin-type domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX842577; CAA98310.1; -; Genomic_DNA. DR EMBL; AE000516; AAK45871.1; -; Genomic_DNA. DR PIR; F70762; F70762. DR RefSeq; NP_216069.1; -. DR RefSeq; NP_336057.1; -. DR HSSP; P00364; 1KF6. DR GeneID; 886378; -. DR GeneID; 924333; -. DR GenomeReviews; AE000516_GR; MT1604. DR GenomeReviews; AL123456_GR; Rv1553. DR KEGG; mtc:MT1604; -. DR KEGG; mtu:Rv1553; -. DR TIGR; MT1604; -. DR TubercuList; Rv1553; -. DR HOGENOM; Q10761; -. 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 carrier activity; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. DR GO; GO:0000104; F:succinate dehydrogenase activity; IEA:EC. DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR001450; 4Fe4S_Fe_S_bd. DR InterPro; IPR012675; b-grasp_ferredoxin-like. DR InterPro; IPR001041; Ferredoxin. DR InterPro; IPR012285; Fum_reductase_C. DR InterPro; IPR004489; Succ_DHase/fum_Rdtase_Fe-S. DR Gene3D; G3DSA:3.10.20.30; Ferredoxin_fold; 1. DR Gene3D; G3DSA:1.10.1060.10; Fum_reductase_C; 1. DR Pfam; PF00037; Fer4; 1. DR TIGRFAMs; TIGR00384; dhsB; 1. DR PROSITE; PS00197; 2FE2S_FER_1; FALSE_NEG. DR PROSITE; PS51085; 2FE2S_FER_2; FALSE_NEG. 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 1 247 Fumarate reductase iron-sulfur subunit. FT /FTId=PRO_0000158705. FT DOMAIN 14 94 2Fe-2S ferredoxin-type. FT DOMAIN 140 169 4Fe-4S ferredoxin-type. FT METAL 56 56 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 61 61 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 76 76 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 149 149 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 152 152 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 155 155 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 159 159 Iron-sulfur 3 (3Fe-4S) (By similarity). FT METAL 205 205 Iron-sulfur 3 (3Fe-4S) (By similarity). FT METAL 211 211 Iron-sulfur 3 (3Fe-4S) (By similarity). FT METAL 215 215 Iron-sulfur 2 (4Fe-4S) (By similarity). 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 //