FWDC_METMP
ID FWDC_METMP Reviewed; 272 AA.
AC P0CW43; O31112;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 51.
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=MMP1249;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
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 seven subunits fwdA (65 kDa), fwdB
CC (53 kDa), fwdC (31 kDa), fwdD (15 kDa), fwdE, fwdF and fwdG.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FwdC/FmdC family. {ECO:0000305}.
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DR EMBL; BX950229; CAF30805.1; -; Genomic_DNA.
DR RefSeq; WP_011171193.1; NC_005791.1.
DR AlphaFoldDB; P0CW43; -.
DR SMR; P0CW43; -.
DR STRING; 267377.MMP1249; -.
DR EnsemblBacteria; CAF30805; CAF30805; MMP1249.
DR GeneID; 2762780; -.
DR KEGG; mmp:MMP1249; -.
DR PATRIC; fig|267377.15.peg.1282; -.
DR eggNOG; arCOG00097; Archaea.
DR HOGENOM; CLU_072248_0_0_2; -.
DR OMA; VNGDAGM; -.
DR OrthoDB; 72252at2157; -.
DR BioCyc; MMAR267377:MMP_RS06425-MON; -.
DR UniPathway; UPA00640; UER00692.
DR Proteomes; UP000000590; 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; -; 1.
DR InterPro; IPR017550; Formylmethanofuran_DH_suC.
DR InterPro; IPR002489; Glu_synth_asu_C.
DR InterPro; IPR036485; Glu_synth_asu_C_sf.
DR Pfam; PF01493; GXGXG; 1.
DR SUPFAM; SSF69336; SSF69336; 1.
DR TIGRFAMs; TIGR03122; one_C_dehyd_C; 1.
PE 3: Inferred from homology;
KW Methanogenesis; Oxidoreductase; Reference proteome; Repeat.
FT CHAIN 1..272
FT /note="Tungsten-containing formylmethanofuran dehydrogenase
FT 2 subunit C"
FT /id="PRO_0000408198"
FT REPEAT 77..89
FT /note="1"
FT REPEAT 96..108
FT /note="2"
FT REPEAT 115..127
FT /note="3"
FT REPEAT 141..153
FT /note="4"
FT REPEAT 160..172
FT /note="5"
FT REPEAT 179..191
FT /note="6"
FT REPEAT 198..210
FT /note="7"
FT REGION 77..210
FT /note="7 X 13 AA repeats of [GW]-X-X-[MLP]-X-X-G-X-[IL]-X-
FT [IV]-X-G"
SQ SEQUENCE 272 AA; 29187 MW; F87AA3DE97D34DC0 CRC64;
MNELILNLKG DVSVPVEMDK ILPEKIQEMS LEEISGIELI QGNKTAKVSE IFDVELKESD
VAKVTINNCC KKVKRIGEKM TSGEIVVNGD AGMYIGVEMK GGKITVNGDA ESWVGQNLKG
GEIIINGNAE NYVGSAYRGD WRGMSGGKIT ITGNAGSELG EYLKGGTIVI KGNTKIMPGI
HQNGGMIIIE GDIEGRAGGE MMKGAIVVYG KILEPLPSFK FEGIVEDPLV KLSKKDAGTQ
LKGTFIKFSG DYVNTKPKGQ LYAAIENNKN LI