FWDC_METTH
ID FWDC_METTH Reviewed; 270 AA.
AC O27600;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 123.
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=MTH_1558;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
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., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
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 -!- ACTIVITY REGULATION: Not inactivated by cyanide.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000666; AAB86032.1; -; Genomic_DNA.
DR PIR; H69074; H69074.
DR RefSeq; WP_010877167.1; NC_000916.1.
DR AlphaFoldDB; O27600; -.
DR SMR; O27600; -.
DR IntAct; O27600; 2.
DR STRING; 187420.MTH_1558; -.
DR TCDB; 3.D.8.1.1; the na(+)- or h(+)-pumping formyl methanofuran dehydrogenase (fmf-dh) family.
DR EnsemblBacteria; AAB86032; AAB86032; MTH_1558.
DR GeneID; 1471827; -.
DR KEGG; mth:MTH_1558; -.
DR PATRIC; fig|187420.15.peg.1521; -.
DR HOGENOM; CLU_072248_0_0_2; -.
DR OMA; VNGDAGM; -.
DR UniPathway; UPA00640; UER00692.
DR Proteomes; UP000005223; 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; Reference proteome; Repeat.
FT CHAIN 1..270
FT /note="Tungsten-containing formylmethanofuran dehydrogenase
FT 2 subunit C"
FT /id="PRO_0000144196"
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"
SQ SEQUENCE 270 AA; 28641 MW; 043A9FFBBA554D36 CRC64;
MSEIILTPKE QPEVPLEAPN IKPDVFAGKS IDEIRNIQIM HGNEVVKLGD FFEVSGEPAD
SAADIKIIID GDVYNTKRIG QDMTAGEILV KGNVNMYVGA GMKGGKITVE GNAKSWAGQD
MRGGELEIFG DAGDYVGSSY RGDWRGMSGG VITVHGNAGN EIGEYMNGGK IIIKGDVNIM
PGIHMNNGLI IIEGNAVARV GGEMAGGTIV VKGMIEEFLP GFKYLGVEKD IEVNGETFPG
AYYKFEGDHA IKGAKGMVYA AVGCNGHIEP