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   25-NOV-2008, entry version 21.
DE   RecName: Full=Tungsten-containing formylmethanofuran dehydrogenase 2 subunit B;
DE            EC=1.2.99.5;
DE   AltName: Full=Tungsten-containing formylmethanofuran dehydrogenase II subunit B;
GN   Name=fwdB; OrderedLocusNames=MJ1194;
OS   Methanocaldococcus jannaschii (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=2190;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   MEDLINE=96337999; PubMed=8688087;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D.,
RA   Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D.,
RA   Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I.,
RA   Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A.,
RA   Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D.,
RA   Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C.,
RA   Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M.,
RA   Klenk H.-P., 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
RT   of Methanococcus jannaschii probably directing selenocysteine
RT   insertion.";
RL   J. Mol. Biol. 266:637-641(1997).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of CO(2) and
CC       methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). This enzyme
CC       is oxygen-labile (By similarity).
CC   -!- CATALYTIC ACTIVITY: Formylmethanofuran + H(2)O + acceptor = CO(2)
CC       + methanofuran + reduced acceptor.
CC   -!- COFACTOR: Tungsten (By similarity).
CC   -!- PATHWAY: One-carbon metabolism; methanogenesis from carbone
CC       dioxide; 5,10-methenyl-H(4)MPT from CO(2): step 1/3.
CC   -!- SUBUNIT: This enzyme is composed of six subunits fwdA, fwdC, fwdD,
CC       fwdE, fwdF and fwdG (By similarity).
CC   -!- SIMILARITY: Belongs to the fwdB family.
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DR   EMBL; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   GenomeReviews; L77117_GR; MJ1194.
DR   TIGR; MJ1194; -.
DR   HOGENOM; P61154; -.
DR   GO; GO:0018493; F:formylmethanofuran dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0008430; F:selenium binding; IEA:UniProtKB-KW.
DR   GO; GO:0015948; P:methanogenesis; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
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   Complete proteome; Methanogenesis; Oxidoreductase; Selenium;
KW   Selenocysteine; Tungsten.
FT   CHAIN         1    435       Tungsten-containing formylmethanofuran
FT                                dehydrogenase 2 subunit B.
FT                                /FTId=PRO_0000087392.
FT   NON_STD     121    121       Selenocysteine (Probable).
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
//