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Database: UniProt
Entry: D7DTE1_METV3
LinkDB: D7DTE1_METV3
Original site: D7DTE1_METV3 
ID   D7DTE1_METV3            Unreviewed;       425 AA.
AC   D7DTE1;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=formylmethanofuran dehydrogenase {ECO:0000256|ARBA:ARBA00012692};
DE            EC=1.2.7.12 {ECO:0000256|ARBA:ARBA00012692};
GN   OrderedLocusNames=Mvol_0742 {ECO:0000313|EMBL:ADI36401.1};
OS   Methanococcus voltae (strain ATCC BAA-1334 / A3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=456320 {ECO:0000313|EMBL:ADI36401.1, ECO:0000313|Proteomes:UP000007722};
RN   [1] {ECO:0000313|EMBL:ADI36401.1, ECO:0000313|Proteomes:UP000007722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1334 / A3 {ECO:0000313|Proteomes:UP000007722};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Lowry S., Clum A., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Whitman W.B., Woyke T.;
RT   "Complete sequence of Methanococcus voltae A3.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000989};
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|ARBA:ARBA00004830}.
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DR   EMBL; CP002057; ADI36401.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7DTE1; -.
DR   STRING; 456320.Mvol_0742; -.
DR   KEGG; mvo:Mvol_0742; -.
DR   eggNOG; arCOG00097; Archaea.
DR   eggNOG; arCOG02674; Archaea.
DR   HOGENOM; CLU_661592_0_0_2; -.
DR   InParanoid; D7DTE1; -.
DR   OrthoDB; 106216at2157; -.
DR   UniPathway; UPA00640; UER00692.
DR   Proteomes; UP000007722; Chromosome.
DR   GO; GO:0018493; F:formylmethanofuran dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR   GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway.
DR   CDD; cd00980; FwdC/FmdC; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 2.160.20.60; Glutamate synthase, alpha subunit, C-terminal domain; 2.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR017550; Formylmethanofuran_DH_suC.
DR   InterPro; IPR036485; Glu_synth_asu_C_sf.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   NCBIfam; TIGR03122; one_C_dehyd_C; 1.
DR   PANTHER; PTHR39673; TUNGSTEN FORMYLMETHANOFURAN DEHYDROGENASE, SUBUNIT C (FWDC); 1.
DR   PANTHER; PTHR39673:SF7; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT C; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF69336; Alpha subunit of glutamate synthase, C-terminal domain; 1.
PE   4: Predicted;
KW   Methanogenesis {ECO:0000256|ARBA:ARBA00022994};
KW   Oxidoreductase {ECO:0000313|EMBL:ADI36401.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007722};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          303..395
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   425 AA;  46442 MW;  E420E1B4E6236961 CRC64;
     MGEIILTPKY DDRFPVECDM ITPDNFFGKS NEEIQAVKLW KSSVQYPLSE FFDVKGDGQG
     TESAADIHII IDGTVPKMKL IGYSMTTGKI TVNGDVNYHV GCEMKGGEIE VNGNAGSWAG
     REMEGGTIII HGNAGDHIGG SYRGKWEGML GGRIVIDGNA GSSVGDGLVK GTIIVKGNVE
     AFCGIRQSGG LIYVGGDVLR TIGVEMKKGT IIVEGNIKNF SPGFFEQTLL KSNEVPSELY
     DEILPYGANL YSKSYIEYKG DHAFFNKPKG KMYVSANNNE YLLSCEGSTD RPIEFKGEAL
     KVILNTGSTI EQGRIIKGGD KYSPEYKDVC AVCHIHPDDY QLLGKPEKVK VSSPDGNRSV
     VVRAEMKDNV QRRNIFIPRS VWANVIVDAQ SVNSGAPIYK GGEAYVQPTD DEILEAPYII
     EQQYK
//
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