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Database: UniProt
Entry: Q49611
LinkDB: Q49611
Original site: Q49611 
ID   FWDG_METKA              Reviewed;          79 AA.
AC   Q49611;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   10-APR-2019, entry version 111.
DE   RecName: Full=Tungsten-containing formylmethanofuran dehydrogenase 2 subunit G;
DE            EC=1.2.7.12 {ECO:0000250|UniProtKB:Q48943};
DE   AltName: Full=Tungsten-containing formylmethanofuran dehydrogenase II subunit G;
GN   Name=fwdG; Synonyms=fudG; OrderedLocusNames=MK1525;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC
OS   100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=9076739; DOI=10.1046/j.1365-2958.1997.2931653.x;
RA   Vorholt J.A., Vaupel M., Thauer R.K.;
RT   "A selenium-dependent and a selenium-independent formylmethanofuran
RT   dehydrogenase and their transcriptional regulation in the
RT   hyperthermophilic Methanopyrus kandleri.";
RL   Mol. Microbiol. 23:1033-1042(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L.,
RA   Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O.,
RA   Malykh A.G., Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19
RT   and monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of CO(2) and
CC       methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). This enzyme
CC       is oxygen-labile. May function as an electron transfer protein.
CC       {ECO:0000250|UniProtKB:Q48943}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-formylmethanofuran + 2 oxidized [2Fe-2S]-
CC         [ferredoxin] = CO2 + H(+) + methanofuran + 2 reduced [2Fe-2S]-
CC         [ferredoxin]; Xref=Rhea:RHEA:19841, Rhea:RHEA-COMP:10000,
CC         Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:57727, ChEBI:CHEBI:58151; EC=1.2.7.12;
CC         Evidence={ECO:0000250|UniProtKB:Q48943};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000305};
CC       Note=Binds 2 [4Fe-4S] clusters. {ECO:0000305};
CC   -!- ACTIVITY REGULATION: Not inactivated by cyanide. {ECO:0000250}.
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   -!- INDUCTION: By growth on tungsten or molybdenum under anaerobic
CC       conditions.
DR   EMBL; X98917; CAA67417.1; -; Genomic_DNA.
DR   EMBL; AE009439; AAM02738.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q49611; -.
DR   SMR; Q49611; -.
DR   EnsemblBacteria; AAM02738; AAM02738; MK1525.
DR   KEGG; mka:MK1525; -.
DR   PATRIC; fig|190192.8.peg.1685; -.
DR   eggNOG; arCOG00292; Archaea.
DR   eggNOG; ENOG4111IC0; LUCA.
DR   HOGENOM; HOG000044611; -.
DR   KO; K11260; -.
DR   OMA; ETWGGKG; -.
DR   UniPathway; UPA00640; UER00692.
DR   Proteomes; UP000001826; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   Pfam; PF00037; Fer4; 2.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   2: Evidence at transcript level;
KW   4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; Methanogenesis; Oxidoreductase; Reference proteome;
KW   Repeat; Transport.
FT   CHAIN         1     79       Tungsten-containing formylmethanofuran
FT                                dehydrogenase 2 subunit G.
FT                                /FTId=PRO_0000159254.
FT   DOMAIN        2     31       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       51     79       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        11     11       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        14     14       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        17     17       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        21     21       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        60     60       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        63     63       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        66     66       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        70     70       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
SQ   SEQUENCE   79 AA;  8345 MW;  0EFD1B298A8BBA67 CRC64;
     MVKIVIHEER CHGCGNCVIA CPVNACNSPN VWGGKGPEDG EDVVIKVVNG TVSVINEDLC
     EACMTCELAC PVDAIEIKT
//
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