ID   FMDC_METTH              Reviewed;         400 AA.
AC   O27002;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 68.
DE   RecName: Full=Molybdenum-containing formylmethanofuran dehydrogenase 1 subunit C;
DE            EC=1.2.99.5;
DE   AltName: Full=Molybdenum-containing formylmethanofuran dehydrogenase I subunit C;
GN   Name=fmdC; OrderedLocusNames=MTH_918;
OS   Methanobacterium thermoautotrophicum.
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Delta H;
RX   MEDLINE=98037514; PubMed=9371463;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K.,
RA   Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D.,
RA   Spadafora R., Vicare R., Wang Y., Wierzbowski J., Gibson R.,
RA   Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S.,
RA   McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M.,
RA   Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum
RT   deltaH: functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of CO(2) and
CC       methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). Can only
CC       oxidize formylmethanofuran. This enzyme is oxygen-labile.
CC   -!- CATALYTIC ACTIVITY: Formylmethanofuran + H(2)O + acceptor = CO(2)
CC       + methanofuran + reduced acceptor.
CC   -!- COFACTOR: Molybdenum.
CC   -!- ENZYME REGULATION: Inactivated by cyanide.
CC   -!- PATHWAY: One-carbon metabolism; methanogenesis from carbone
CC       dioxide; 5,10-methenyl-H(4)MPT from CO(2): step 1/3.
CC   -!- SUBUNIT: Consists of five subunits; fmdA, fmdB, fmdC, fmdD, and
CC       fmdE.
CC   -!- INDUCTION: By growth on molybdenum, under anaerobic conditions.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the fwdC/fmdC
CC       family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the molybdenum
CC       dinucleotide binding protein family.
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DR   EMBL; AE000666; AAB85416.1; -; Genomic_DNA.
DR   PIR; H69222; H69222.
DR   RefSeq; NP_276055.1; -.
DR   GeneID; 1471326; -.
DR   GenomeReviews; AE000666_GR; MTH_918.
DR   KEGG; mth:MTH918; -.
DR   NMPDR; fig|187420.1.peg.910; -.
DR   HOGENOM; O27002; -.
DR   OMA; O27002; LECEVIT.
DR   BioCyc; MetaCyc:FMDCMAUTO-MON; -.
DR   BioCyc; MTHE187420:MTH918-MON; -.
DR   BRENDA; 1.2.99.5; 270.
DR   GO; GO:0018493; F:formylmethanofuran dehydrogenase activity; IEA:EC.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR012048; Formylmethanofuran_DH_csu/dsu.
DR   InterPro; IPR017550; Formylmethanofuran_DH_suC.
DR   InterPro; IPR002489; Glu_synthase_C.
DR   InterPro; IPR006657; MPT_dinuc_bd.
DR   Gene3D; G3DSA:2.160.20.60; Glu_synthase_C; 1.
DR   Pfam; PF01493; GXGXG; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   PIRSF; PIRSF036633; FmdC_D; 1.
DR   TIGRFAMs; TIGR03122; one_C_dehyd_C; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Methanogenesis; Molybdenum; Oxidoreductase; Repeat.
FT   CHAIN         1    400       Molybdenum-containing formylmethanofuran
FT                                dehydrogenase 1 subunit C.
FT                                /FTId=PRO_0000144192.
FT   REPEAT       76     88       1.
FT   REPEAT       95    107       2.
FT   REPEAT      114    126       3.
FT   REPEAT      140    152       4.
FT   REPEAT      159    171       5.
FT   REPEAT      178    190       6.
FT   REPEAT      197    209       7.
FT   REGION       76    209       7 X 13 AA repeats of [GW]-X-X-M-X-X-G-X-
FT                                I-X-[IV]-X-G.
SQ   SEQUENCE   400 AA;  43288 MW;  DBC32FF73A5DDF05 CRC64;
     MGFVLVPKSD FQIPLEADTI RPDLFEGLDL DEIRSLQVYE GNIKRPLGEF FEIAETPHAD
     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
//