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Database: UniProt
Entry: Q8TSG2_METAC
LinkDB: Q8TSG2_METAC
Original site: Q8TSG2_METAC 
ID   Q8TSG2_METAC            Unreviewed;       434 AA.
AC   Q8TSG2;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   24-JAN-2024, entry version 101.
DE   RecName: Full=Tungsten-containing formylmethanofuran dehydrogenase 2 subunit B {ECO:0000256|PIRNR:PIRNR005646};
DE            EC=1.2.7.12 {ECO:0000256|PIRNR:PIRNR005646};
DE   AltName: Full=Tungsten-containing formylmethanofuran dehydrogenase II subunit B {ECO:0000256|PIRNR:PIRNR005646};
GN   Name=fwdB {ECO:0000313|EMBL:AAM04273.1};
GN   OrderedLocusNames=MA_0834 {ECO:0000313|EMBL:AAM04273.1};
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937 {ECO:0000313|EMBL:AAM04273.1, ECO:0000313|Proteomes:UP000002487};
RN   [1] {ECO:0000313|EMBL:AAM04273.1, ECO:0000313|Proteomes:UP000002487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A
RC   {ECO:0000313|Proteomes:UP000002487};
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A., Hedderich R., Ingram-Smith C.,
RA   Kuettner C.H., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B.,
RA   Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H.,
RA   de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L.,
RA   Paulsen I., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H.,
RA   Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
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:0000256|PIRNR:PIRNR005646}.
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; Evidence={ECO:0000256|PIRNR:PIRNR005646};
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       {ECO:0000256|PIRNR:PIRNR005646}.
CC   -!- SUBUNIT: This enzyme is composed of six subunits FwdA, FwdC, FwdD,
CC       FwdE, FwdF and FwdG. {ECO:0000256|PIRNR:PIRNR005646}.
CC   -!- SIMILARITY: Belongs to the FwdB family.
CC       {ECO:0000256|PIRNR:PIRNR005646}.
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DR   EMBL; AE010299; AAM04273.1; -; Genomic_DNA.
DR   RefSeq; WP_011020878.1; NC_003552.1.
DR   AlphaFoldDB; Q8TSG2; -.
DR   STRING; 188937.MA_0834; -.
DR   EnsemblBacteria; AAM04273; AAM04273; MA_0834.
DR   GeneID; 1472726; -.
DR   KEGG; mac:MA_0834; -.
DR   HOGENOM; CLU_034348_0_0_2; -.
DR   InParanoid; Q8TSG2; -.
DR   OMA; VCIDPHE; -.
DR   OrthoDB; 23466at2157; -.
DR   PhylomeDB; Q8TSG2; -.
DR   Proteomes; UP000002487; Chromosome.
DR   GO; GO:0018493; F:formylmethanofuran dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045333; P:cellular respiration; IBA:GO_Central.
DR   GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniRule.
DR   CDD; cd02761; MopB_FmdB-FwdB; 1.
DR   Gene3D; 3.30.200.210; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
DR   InterPro; IPR016457; Formylmethanofuran_DH_bsu.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   NCBIfam; TIGR03129; one_C_dehyd_B; 1.
DR   PANTHER; PTHR43105:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   PIRSF; PIRSF005646; FwdB; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
PE   3: Inferred from homology;
KW   Methanogenesis {ECO:0000256|PIRNR:PIRNR005646};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR005646};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002487};
KW   Selenocysteine {ECO:0000256|PIRNR:PIRNR005646};
KW   Tungsten {ECO:0000256|PIRNR:PIRNR005646}.
FT   DOMAIN          50..423
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
SQ   SEQUENCE   434 AA;  47163 MW;  D56F12A1DFE2B81F CRC64;
     MPVIKDAVCS LCGSLCDDIT VTVEDNKITK IENACILGHS KFVGMFEHDR IETPMIRKDG
     ELVPVSYEEA IEAAAKILVN SRRILSYGWC STSCEAVSGA IELAEETGSV IDSTANVCHG
     PSALAAQEKG SPSASLGEIK NRADVIVFWG CNPVHAHPRH MSRYSSFSKG FFTEKGRKGR
     TMVVIDVRKT DTAKLADNYV EIEQGSDLLL ITALRSIVNG HEDVVPETVA GVPKAEVLEL
     AETLKNAKFV CIFFGMGVTQ SRSKYKNGDA VSSLISDLNQ HTKAVMIGMR GHYNVTGFGQ
     VATWETGFPM AIDFARGYPY YNPGETGAND LLVREEPDAA IIAAADPGAH FPQKAVRHLA
     KIPVIQIDPY ANPTTEIADV VIPSAIVGIE AEGTAYRMDA ISLRMKKLID TRFKTDEEIV
     KDLTAKVREL KRGA
//
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