ID FWDC_METWO Reviewed; 270 AA. AC O74031; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 16-JUN-2009, entry version 45. DE RecName: Full=Tungsten-containing formylmethanofuran dehydrogenase 2 subunit C; DE EC=1.2.99.5; DE AltName: Full=Tungsten-containing formylmethanofuran dehydrogenase II subunit C; GN Name=fwdC; OS Methanobacterium wolfei. OC Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales; OC Methanobacteriaceae; Methanothermobacter. OX NCBI_TaxID=145261; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=99035764; PubMed=9818358; DOI=10.1007/s002030050658; RA Hochheimer A., Hedderich R., Thauer R.K.; RT "The formylmethanofuran dehydrogenase isoenzymes in Methanobacterium RT wolfei and Methanobacterium thermoautotrophicum: induction of the RT molybdenum isoenzyme by molybdate and constitutive synthesis of the RT tungsten isoenzyme."; RL Arch. Microbiol. 170:389-393(1998). CC -!- FUNCTION: Catalyzes the reversible oxidation of CO(2) and CC methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). This enzyme CC is oxygen-labile (By similarity). CC -!- CATALYTIC ACTIVITY: Formylmethanofuran + H(2)O + acceptor = CO(2) CC + methanofuran + reduced acceptor. CC -!- COFACTOR: Tungsten. CC -!- PATHWAY: One-carbon metabolism; methanogenesis from carbone CC dioxide; 5,10-methenyl-H(4)MPT from CO(2): step 1/3. CC -!- SUBUNIT: This enzyme is composed of six subunits fwdA, fwdB, fwdC, CC fwdD, fwdF and fwdG (By similarity). CC -!- INDUCTION: By growth on tungsten or molybdenum under anaerobic CC conditions. CC -!- SIMILARITY: Belongs to the fwdC/fmdC family. 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; AJ009688; CAA08784.1; -; Genomic_DNA. DR BRENDA; 1.2.99.5; 7575. DR GO; GO:0018493; F:formylmethanofuran dehydrogenase activity; IEA:EC. DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro. DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR017550; Formylmethanofuran_DH_suC. DR InterPro; IPR002489; Glu_synthase_C. DR Gene3D; G3DSA:2.160.20.60; Glu_synthase_C; 1. DR Pfam; PF01493; GXGXG; 1. DR TIGRFAMs; TIGR03122; one_C_dehyd_C; 1. PE 2: Evidence at transcript level; KW Methanogenesis; Oxidoreductase; Repeat; Tungsten. FT CHAIN 1 270 Tungsten-containing formylmethanofuran FT dehydrogenase 2 subunit C. FT /FTId=PRO_0000144198. FT REPEAT 80 92 1. FT REPEAT 99 111 2. FT REPEAT 118 130 3. FT REPEAT 144 156 4. FT REPEAT 163 175 5. FT REPEAT 182 194 6. FT REPEAT 201 213 7. FT REGION 80 213 7 X 13 AA repeats of [GW]-X-X-M-X-X-G-X- FT [IL]-X-[IV]-X-G. SQ SEQUENCE 270 AA; 28660 MW; BB1061CBDF53061B CRC64; MSEIILTPKE QPEVPLEAPN IKPDVFAGKS IDEIKNIQIM HGNEVVKLGD FFEVSGEPAD APEDIKIIID GDVYNTKRIG QEMTAGEIIV RGNVNMYVGA GMKGGKITVE GNAGSWAGQD MRGGEIEILG DADDYVGSSY RGDWRGMSGG TITVHGNADN EIGEYMNGGK IIIKGDVNIM PGIHMNNGLI IIEGNVVARA GGEMAGGTIV VKGMMQEFLA GFKYLGVEKD IELMVKNSPG AFYKFEGDHA IKGAKGIVYA AVGCNGHIAP //