ID   FMDC_METWO              Reviewed;         400 AA.
AC   P61938; P95294;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Molybdenum-containing formylmethanofuran dehydrogenase 1 subunit C;
DE            EC=1.2.7.12 {ECO:0000250|UniProtKB:Q48943};
DE   AltName: Full=Molybdenum-containing formylmethanofuran dehydrogenase I subunit C;
GN   Name=fmdC;
OS   Methanothermobacter wolfeii (Methanobacterium wolfei).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=145261;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9818358; DOI=10.1007/s002030050658;
RA   Hochheimer A., Hedderich R., Thauer R.K.;
RT   "The formylmethanofuran dehydrogenase isoenzymes in Methanobacterium wolfei
RT   and Methanobacterium thermoautotrophicum: induction of the molybdenum
RT   isoenzyme by molybdate and constitutive synthesis of the tungsten
RT   isoenzyme.";
RL   Arch. Microbiol. 170:389-393(1998).
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: Consists of five subunits; FmdA, FmdB, FmdC, FmdD, and FmdE.
CC   -!- INDUCTION: By growth on molybdenum, under anaerobic conditions.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the FwdC/FmdC family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the molybdenum
CC       dinucleotide binding protein family. {ECO:0000305}.
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DR   EMBL; AJ009689; CAA08787.1; -; Genomic_DNA.
DR   AlphaFoldDB; P61938; -.
DR   SMR; P61938; -.
DR   STRING; 145261.MWSIV6_1311; -.
DR   UniPathway; UPA00640; UER00692.
DR   GO; GO:0018493; F:formylmethanofuran dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway.
DR   CDD; cd00980; FwdC/FmdC; 1.
DR   CDD; cd02789; MopB_CT_FmdC-FwdD; 1.
DR   Gene3D; 2.160.20.60; -; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR041717; FmdC/FwdD_MopB-bd.
DR   InterPro; IPR012048; Formylmethanofuran_DH_csu/dsu.
DR   InterPro; IPR017550; Formylmethanofuran_DH_suC.
DR   InterPro; IPR036485; Glu_synth_asu_C_sf.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   PIRSF; PIRSF036633; FmdC_D; 1.
DR   SUPFAM; SSF50692; SSF50692; 1.
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..400
FT                   /note="Molybdenum-containing formylmethanofuran
FT                   dehydrogenase 1 subunit C"
FT                   /id="PRO_0000144193"
FT   REPEAT          76..88
FT                   /note="1"
FT   REPEAT          95..107
FT                   /note="2"
FT   REPEAT          114..126
FT                   /note="3"
FT   REPEAT          140..152
FT                   /note="4"
FT   REPEAT          159..171
FT                   /note="5"
FT   REPEAT          178..190
FT                   /note="6"
FT   REPEAT          197..209
FT                   /note="7"
FT   REGION          76..209
FT                   /note="7 X 13 AA repeats of [GW]-X-X-M-X-X-G-X-I-X-[IV]-X-
FT                   G"
SQ   SEQUENCE   400 AA;  43321 MW;  41F1C21A25CFBBC3 CRC64;
     MGFVLVPKSD FQIPLEADTI DPICLKGWDL DEIRSLQVYE GNIKRPLGEF FEIAETSHED
     QLIRIDGDVS RVKYIGSGMK SGKIIINGDV GLQLGCEMKG GEIEVNGNVS SWIGMEMHGG
     TIKINGNAGD YVGCAYRGEW RGMKGGKIII QGNAGNNIGG GMMAGEIYIG GDAGNFCGIR
     MNGGEITVRG DAGRAPGAEM VSGIIKIHGR ISSLLPGFKE ISTFKEDGSL MILFKGDLSE
     KNPEGNLYIN YNKNLHILEN ETDEGRVITK KGIKVIYNSG STIREGQIIK GGNKLTDDYI
     DECARCCISP EDYKLLGEPE NVVVSSHGNE VVLRAVEDPG IQMGTIFIPR GIWANVLTPP
     YTESTGSPMY KGVPVYLRKA SQGERILSAE ELVEEYGVGK