ID   FWDB_METMP              Reviewed;         434 AA.
AC   Q6LWL8;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Tungsten-containing formylmethanofuran dehydrogenase 2 subunit B;
DE            EC=1.2.7.12 {ECO:0000250|UniProtKB:Q48943};
DE   AltName: Full=Tungsten-containing formylmethanofuran dehydrogenase II subunit B;
GN   Name=fwdB; OrderedLocusNames=MMP1691;
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   -!- COFACTOR:
CC       Name=W-bis(molybdopterin guanine dinucleotide); Xref=ChEBI:CHEBI:60537;
CC         Evidence={ECO:0000305};
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, FwdC, FwdD,
CC       FwdE, FwdF and FwdG. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FwdB family. {ECO:0000305}.
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DR   EMBL; BX950229; CAF31247.1; -; Genomic_DNA.
DR   STRING; 267377.MMP1691; -.
DR   KEGG; mmp:MMP1691; -.
DR   PATRIC; fig|267377.15.peg.1732; -.
DR   eggNOG; arCOG01499; Archaea.
DR   HOGENOM; CLU_034348_0_0_2; -.
DR   OMA; VCIDPHE; -.
DR   BioCyc; MMAR267377:MMP_RS08715-MON; -.
DR   UniPathway; UPA00640; UER00692.
DR   Proteomes; UP000000590; Chromosome.
DR   GO; GO:0018493; F:formylmethanofuran dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway.
DR   CDD; cd02761; MopB_FmdB-FwdB; 1.
DR   InterPro; IPR016457; Formylmethanofuran_DH_bsu.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   PIRSF; PIRSF005646; FwdB; 1.
DR   TIGRFAMs; TIGR03129; one_C_dehyd_B; 1.
PE   3: Inferred from homology;
KW   Methanogenesis; Oxidoreductase; Reference proteome; Selenocysteine;
KW   Tungsten.
FT   CHAIN           1..434
FT                   /note="Tungsten-containing formylmethanofuran dehydrogenase
FT                   2 subunit B"
FT                   /id="PRO_0000318645"
FT   NON_STD         120
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   434 AA;  48323 MW;  F7CBD9D17D4F8C06 CRC64;
     MEVFKNVVCP FCGTLCDDIE VLVENNHVVG TRNACRIGNA KFMHFEGAIR HESPLMRENK
     KDDFKKVDYE TATEETARLL VEAKLPLIYG WSSAECHAQQ LGVLLAEKTK AIVDNTASVU
     HGPSLLAVQD VGYPVSTLGE TKNRADVVLF WGSNPMHAHP RHMSRYSVFP RGFFRQRGKQ
     DRQMIVVDPR KTDTAKLADI HLQVEPHKDY ELVSALRAAA KGFNIEAEQV AGVPTETIYE
     AVDICKNAQF GSLFFAMGVT MSRGKHRIID NAIQFVIDMN AYTKFVLTPM RGHYNVNGFN
     QVSTWVTGYP YGVDFSRGYP RYNPGETASN DVLQRGDTDM MINVASDAGA HFPQKAVQHM
     AKIPLVCIDP HETPSSVISN IVLPPAITGL EVSGTAYRMD GVPIELRKVI KAPEGMLSDA
     EIMKMLIKKV DEMK