ID   FWDC_METTM              Reviewed;         270 AA.
AC   Q59579; D9PU55; O08493;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Tungsten-containing formylmethanofuran dehydrogenase 2 subunit C;
DE            EC=1.2.7.12 {ECO:0000250|UniProtKB:Q48943};
DE   AltName: Full=Tungsten-containing formylmethanofuran dehydrogenase II subunit C;
GN   Name=fwdC; OrderedLocusNames=MTBMA_c01440;
OS   Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS   14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS   thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=79929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=8575452; DOI=10.1111/j.1432-1033.1995.910_a.x;
RA   Hochheimer A., Schmitz R.A., Thauer R.K., Hedderich R.;
RT   "The tungsten formylmethanofuran dehydrogenase from Methanobacterium
RT   thermoautotrophicum contains sequence motifs characteristic for enzymes
RT   containing molybdopterin dinucleotide.";
RL   Eur. J. Biochem. 234:910-920(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=20802048; DOI=10.1128/jb.00844-10;
RA   Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA   Gottschalk G., Thauer R.K.;
RT   "Complete genome sequence of Methanothermobacter marburgensis, a
RT   methanoarchaeon model organism.";
RL   J. Bacteriol. 192:5850-5851(2010).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of CO(2) and methanofuran
CC       (MFR) to N-formylmethanofuran (CHO-MFR). Can only oxidize
CC       formylmethanofuran. This enzyme is oxygen-labile.
CC       {ECO:0000250|UniProtKB:Q48943}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-formylmethanofuran + 2 oxidized [2Fe-2S]-[ferredoxin]
CC         = CO2 + H(+) + methanofuran + 2 reduced [2Fe-2S]-[ferredoxin];
CC         Xref=Rhea:RHEA:19841, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57727,
CC         ChEBI:CHEBI:58151; EC=1.2.7.12;
CC         Evidence={ECO:0000250|UniProtKB:Q48943};
CC   -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); 5,10-
CC       methenyl-5,6,7,8-tetrahydromethanopterin from CO(2): step 1/3.
CC   -!- SUBUNIT: This enzyme is composed of seven subunits FwdA (65 kDa), FwdB
CC       (53 kDa), FwdC (31 kDa), FwdD (15 kDa), FwdE, FwdF and FwdG.
CC       {ECO:0000250}.
CC   -!- INDUCTION: By growth on tungsten or molybdenum under anaerobic
CC       conditions.
CC   -!- SIMILARITY: Belongs to the FwdC/FmdC family. {ECO:0000305}.
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DR   EMBL; X87970; CAA61214.1; -; Genomic_DNA.
DR   EMBL; CP001710; ADL57753.1; -; Genomic_DNA.
DR   RefSeq; WP_013294981.1; NC_014408.1.
DR   AlphaFoldDB; Q59579; -.
DR   SMR; Q59579; -.
DR   STRING; 79929.MTBMA_c01440; -.
DR   TCDB; 3.D.8.1.1; the na(+)- or h(+)-pumping formyl methanofuran dehydrogenase (fmf-dh) family.
DR   EnsemblBacteria; ADL57753; ADL57753; MTBMA_c01440.
DR   GeneID; 9703849; -.
DR   KEGG; mmg:MTBMA_c01440; -.
DR   PATRIC; fig|79929.8.peg.140; -.
DR   HOGENOM; CLU_072248_0_0_2; -.
DR   OMA; VNGDAGM; -.
DR   OrthoDB; 72252at2157; -.
DR   UniPathway; UPA00640; UER00692.
DR   Proteomes; UP000000345; Chromosome.
DR   GO; GO:0018493; F:formylmethanofuran dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR   GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway.
DR   CDD; cd00980; FwdC/FmdC; 1.
DR   Gene3D; 2.160.20.60; -; 2.
DR   InterPro; IPR017550; Formylmethanofuran_DH_suC.
DR   InterPro; IPR036485; Glu_synth_asu_C_sf.
DR   SUPFAM; SSF69336; SSF69336; 1.
DR   TIGRFAMs; TIGR03122; one_C_dehyd_C; 1.
PE   2: Evidence at transcript level;
KW   Methanogenesis; Oxidoreductase; Repeat.
FT   CHAIN           1..270
FT                   /note="Tungsten-containing formylmethanofuran dehydrogenase
FT                   2 subunit C"
FT                   /id="PRO_0000144197"
FT   REPEAT          80..92
FT                   /note="1"
FT   REPEAT          99..111
FT                   /note="2"
FT   REPEAT          118..130
FT                   /note="3"
FT   REPEAT          144..156
FT                   /note="4"
FT   REPEAT          163..175
FT                   /note="5"
FT   REPEAT          182..194
FT                   /note="6"
FT   REPEAT          201..213
FT                   /note="7"
FT   REGION          80..213
FT                   /note="7 X 13 AA repeats of [GW]-X-X-M-X-X-G-X-[IL]-X-[IV]-
FT                   X-G"
FT   CONFLICT        223
FT                   /note="K -> T (in Ref. 1; CAA61214)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   270 AA;  28582 MW;  DBCEC802ACFEC476 CRC64;
     MSEIILTPKE QPEVPLEAPN IKPDVFAGKS IDEIKNIQIM YGNEVVKLGD FFEVSGEPAD
     AASDIKIIID GDVYNTKRIG QEMTAGEILV KGNVNMYVGA GMKGGRITVE GNAASWAGQD
     MRGGELEILG NAADYVGSSY RGDWRGMSGG VITVHGNAGN EIGEYMNGGK IIIKGDVNIM
     PGIHMNNGLI IIEGNAVARV GGEMAGGTII VKGMIQEFLP GFKYLGVEKD IEVNGETFPG
     AFYKFEGDHA IKGAKGIVYA AVGCNGHIEP