FWDC_METWO
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 25-MAY-2022, entry version 81.
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;
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). 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 six subunits FwdA, FwdB, FwdC,
CC FwdD, FwdF and FwdG. {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; AJ009688; CAA08784.1; -; Genomic_DNA.
DR PDB; 5T5I; X-ray; 1.90 A; C/K=1-270.
DR PDB; 5T5M; X-ray; 2.50 A; C=1-270.
DR PDBsum; 5T5I; -.
DR PDBsum; 5T5M; -.
DR AlphaFoldDB; O74031; -.
DR SMR; O74031; -.
DR STRING; 145261.MWSIV6_0099; -.
DR UniPathway; UPA00640; UER00692.
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; -; 1.
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 1: Evidence at protein level;
KW 3D-structure; Methanogenesis; Oxidoreductase; Repeat.
FT CHAIN 1..270
FT /note="Tungsten-containing formylmethanofuran dehydrogenase
FT 2 subunit C"
FT /id="PRO_0000144198"
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 STRAND 3..8
FT /evidence="ECO:0007829|PDB:5T5I"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:5T5I"
FT HELIX 31..35
FT /evidence="ECO:0007829|PDB:5T5I"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:5T5I"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:5T5I"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:5T5I"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:5T5I"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:5T5I"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:5T5I"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:5T5I"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:5T5I"
FT TURN 98..101
FT /evidence="ECO:0007829|PDB:5T5I"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:5T5I"
FT TURN 115..120
FT /evidence="ECO:0007829|PDB:5T5I"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:5T5I"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:5T5I"
FT TURN 162..165
FT /evidence="ECO:0007829|PDB:5T5I"
FT STRAND 167..175
FT /evidence="ECO:0007829|PDB:5T5I"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:5T5I"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:5T5I"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:5T5I"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:5T5I"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:5T5I"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:5T5I"
FT STRAND 223..233
FT /evidence="ECO:0007829|PDB:5T5I"
FT STRAND 236..247
FT /evidence="ECO:0007829|PDB:5T5I"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:5T5I"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:5T5I"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:5T5I"
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
