ID   FMDC_METTM              Reviewed;         400 AA.
AC   P61937; P95294;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   25-NOV-2008, entry version 26.
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;
OS   Methanobacterium thermoautotrophicum (strain Marburg / DSM 2133).
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=79929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 242-253;
RP   275-290 AND 372-398.
RX   MEDLINE=97112485; PubMed=8954165;
RA   Hochheimer A., Linder D., Thauer R.K., Hedderich R.;
RT   "The molybdenum formylmethanofuran dehydrogenase operon and the
RT   tungsten formylmethanofuran dehydrogenase operon from Methanobacterium
RT   thermoautotrophicum. Structures and transcriptional regulation.";
RL   Eur. J. Biochem. 242:156-162(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-18.
RX   MEDLINE=96163477; PubMed=8575452;
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
RT   enzymes containing molybdopterin dinucleotide.";
RL   Eur. J. Biochem. 234:910-920(1995).
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; X97820; CAA66401.1; -; Genomic_DNA.
DR   GO; GO:0018493; F:formylmethanofuran dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0015948; P:methanogenesis; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR017550; Formylmethanofuran_DH_C.
DR   InterPro; IPR012048; Formylmethanofuran_DH_csu/dsu.
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.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Methanogenesis; Molybdenum; Oxidoreductase;
KW   Repeat.
FT   CHAIN         1    400       Molybdenum-containing formylmethanofuran
FT                                dehydrogenase 1 subunit C.
FT                                /FTId=PRO_0000144191.
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.
FT   CONFLICT     14     14       P -> G (in Ref. 2; AA sequence).
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
//