ID FWDG_METKA Reviewed; 79 AA. AC Q49611; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 05-MAY-2009, entry version 64. DE RecName: Full=Tungsten-containing formylmethanofuran dehydrogenase 2 subunit G; DE EC=1.2.99.5; DE AltName: Full=Tungsten-containing formylmethanofuran dehydrogenase II subunit G; GN Name=fwdG; Synonyms=fudG; OrderedLocusNames=MK1525; OS Methanopyrus kandleri. OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae; OC Methanopyrus. OX NCBI_TaxID=2320; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938; RX MEDLINE=97231344; PubMed=9076739; RX DOI=10.1046/j.1365-2958.1997.2931653.x; RA Vorholt J.A., Vaupel M., Thauer R.K.; RT "A selenium-dependent and a selenium-independent formylmethanofuran RT dehydrogenase and their transcriptional regulation in the RT hyperthermophilic Methanopyrus kandleri."; RL Mol. Microbiol. 23:1033-1042(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938; RX MEDLINE=21927647; PubMed=11930014; DOI=10.1073/pnas.032671499; RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., RA Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., RA Malykh A.G., Koonin E.V., Kozyavkin S.A.; RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 RT and monophyly of archaeal methanogens."; RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002). CC -!- FUNCTION: Catalyzes the reversible oxidation of CO(2) and CC methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). This enzyme CC is oxygen-labile. May function as an electron transfer protein (By CC similarity). CC -!- CATALYTIC ACTIVITY: Formylmethanofuran + H(2)O + acceptor = CO(2) CC + methanofuran + reduced acceptor. CC -!- COFACTOR: Binds 2 4Fe-4S clusters (Potential). CC -!- ENZYME REGULATION: Not inactivated by cyanide (By similarity). CC -!- PATHWAY: One-carbon metabolism; methanogenesis from carbone CC dioxide; 5,10-methenyl-H(4)MPT from CO(2): step 1/3. CC -!- INDUCTION: By growth on tungsten or molybdenum under anaerobic CC conditions. CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. 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; X98917; CAA67417.1; -; Genomic_DNA. DR EMBL; AE010442; AAM02738.1; -; Genomic_DNA. DR RefSeq; NP_614808.1; -. DR HSSP; P03942; 1H98. DR GeneID; 1478120; -. DR GenomeReviews; AE009439_GR; MK1525. DR KEGG; mka:MK1525; -. DR NMPDR; fig|190192.1.peg.1521; -. DR HOGENOM; Q49611; -. DR OMA; Q49611; CHGCGNC. DR BioCyc; MKAN190192:MK1525-MON; -. DR BRENDA; 1.2.99.5; 7577. 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:0018493; F:formylmethanofuran dehydrogenase activity; IEA:EC. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR001450; 4Fe4S_Fe_S_bd_subgr. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR Pfam; PF00037; Fer4; 2. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 2: Evidence at transcript level; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Methanogenesis; Oxidoreductase; Repeat; Transport. FT CHAIN 1 79 Tungsten-containing formylmethanofuran FT dehydrogenase 2 subunit G. FT /FTId=PRO_0000159254. FT DOMAIN 2 31 4Fe-4S ferredoxin-type 1. FT DOMAIN 51 79 4Fe-4S ferredoxin-type 2. FT METAL 11 11 Iron-sulfur 1 (4Fe-4S) (By similarity). FT METAL 14 14 Iron-sulfur 1 (4Fe-4S) (By similarity). FT METAL 17 17 Iron-sulfur 1 (4Fe-4S) (By similarity). FT METAL 21 21 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 60 60 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 63 63 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 66 66 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 70 70 Iron-sulfur 1 (4Fe-4S) (By similarity). SQ SEQUENCE 79 AA; 8345 MW; 0EFD1B298A8BBA67 CRC64; MVKIVIHEER CHGCGNCVIA CPVNACNSPN VWGGKGPEDG EDVVIKVVNG TVSVINEDLC EACMTCELAC PVDAIEIKT //