ID   FWDB_METJA              Reviewed;         435 AA.
AC   P61154;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   11-DEC-2019, entry version 66.
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=MJ1194;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   PROBABLE SELENOCYSTEINE AT SEC-121.
RX   PubMed=9102456; DOI=10.1006/jmbi.1996.0812;
RA   Wilting R., Schorling S., Persson B.C., Boeck A.;
RT   "Selenoprotein synthesis in archaea: identification of an mRNA element of
RT   Methanococcus jannaschii probably directing selenocysteine insertion.";
RL   J. Mol. Biol. 266:637-641(1997).
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; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   InParanoid; P61154; -.
DR   OMA; VCIDPHE; -.
DR   PhylomeDB; P61154; -.
DR   UniPathway; UPA00640; UER00692.
DR   Proteomes; UP000000805; 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..435
FT                   /note="Tungsten-containing formylmethanofuran dehydrogenase
FT                   2 subunit B"
FT                   /id="PRO_0000087392"
FT   NON_STD         121
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   435 AA;  48718 MW;  C1652D23FFC20970 CRC64;
     MVKVVRNVVC PFCGTLCDDL EILVEDNHIV GTRHACRIGN AKFMHFEGAV RYTEPLMREN
     KKDDFKKVDY ETAIEETARL LTEATLPLIY GWSATECHAH MYGVELAELV GAVIDNTASV
     UHGPSLLAVQ DVGYPVCTLG EVKNRADVII FWGSNPMHAH PRHMSRYSVF ARGFFRERGR
     EDRTLIVVDP RETDTAKLAD IHLQVEPHKD YELVSAMRAV LKGFELQVDK VAGVPADLIY
     EAVEVCKNAQ FGELFFAMGV TMTRGKHRNI DNAIQLVIDL NAYTKFGLMP MRGHYNVNGF
     NQVLTWVTGY PFGVDFSRGY PRYNPGETTA NDLLQRGETD MMLNIASDPG AHFPQKAVQH
     MAKIPLVCID PHETPTTQLA NIIIPPAIAG VEVEGTAYRM DGVPIQLRKV IDPPEGVLPD
     REILKILIKK VKEML