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Database: UniProt
Entry: Q5JHW0_THEKO
LinkDB: Q5JHW0_THEKO
Original site: Q5JHW0_THEKO 
ID   Q5JHW0_THEKO            Unreviewed;       721 AA.
AC   Q5JHW0;
DT   15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   SubName: Full=Probable formate dehydrogenase, alpha subunit {ECO:0000313|EMBL:BAD86265.1};
GN   OrderedLocusNames=TK2076 {ECO:0000313|EMBL:BAD86265.1};
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014 {ECO:0000313|EMBL:BAD86265.1, ECO:0000313|Proteomes:UP000000536};
RN   [1] {ECO:0000313|EMBL:BAD86265.1, ECO:0000313|Proteomes:UP000000536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1
RC   {ECO:0000313|Proteomes:UP000000536};
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR   EMBL; AP006878; BAD86265.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5JHW0; -.
DR   STRING; 69014.TK2076; -.
DR   EnsemblBacteria; BAD86265; BAD86265; TK2076.
DR   KEGG; tko:TK2076; -.
DR   PATRIC; fig|69014.16.peg.2031; -.
DR   eggNOG; arCOG01491; Archaea.
DR   HOGENOM; CLU_000422_4_0_2; -.
DR   InParanoid; Q5JHW0; -.
DR   PhylomeDB; Q5JHW0; -.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0015942; P:formate metabolic process; IEA:InterPro.
DR   CDD; cd00508; MopB_CT_Fdh-Nap-like; 1.
DR   CDD; cd02753; MopB_Formate-Dh-H; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 2.20.25.90; ADC-like domains; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR041924; Formate_Dh-H_N.
DR   InterPro; IPR006478; Formate_DH_asu.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   NCBIfam; TIGR01591; Fdh-alpha; 1.
DR   PANTHER; PTHR43598:SF5; DMSO REDUCTASE CHAIN A; 1.
DR   PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   PIRSF; PIRSF000144; CbbBc; 2.
DR   SMART; SM00926; Molybdop_Fe4S4; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000536}.
FT   DOMAIN          14..73
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   721 AA;  80097 MW;  335B4A6847A3B63B CRC64;
     MMYSAMMEVL RMDEKLVPVV CPYCGVGCRL YIRSSDGHPL GIEYANDIPG ISNENGKLCP
     KGNAVLEYVL ARDRLKKPLK AKEQGKFVEI SWSQAIKEVA ERLKEYSKDD PNSMMFFGSA
     KTFNEPNYLI QKLARMLGTN NVDHCARLCH ASTVSGLKAV FGAGAMTNTY RDIEEANVIF
     IIGHNFAETH PVGFRYVLKA KERGAKVIVA DPRFTRTAWF ADIYLQHYPG TDIALINGLI
     HVIIEERLYD EKFVRERCTG FDELAKTVEK FTPGYVEKIT GVPADLIVQA ARTFATGGKG
     VITWAMGITQ HTHGHDNVRL LATLSAICGY QGREGCGVSP MRGQNNVQGA CDLGVLPNVF
     PGYKAVSDPE GRKFFEEFWG TELSGEVGLT VIEAAHAIEK GKVRAYYVMG ENPVISDANT
     NHVIKALHKL EFMVVQDIVP TPTMEFADIV LPAAAMLENE GSLTNTERRV QWSFQAINPP
     GEARPDWWIV SEIGKAAGFT GDGPKGFNYS GPEDILREVN ACTPQYRGIT PERLKANLAG
     IHWPCPSEDH PGTRVLYKER FLTSDGKAHL AAVEYRGPAE TPDEDYPFLL TTVRYVGHYH
     TLTMTGRSRA LVKRWPEPLA EIHPEDAERL GIKTGDWVKI VTRRGEYPIR AKVTRTVKKG
     VIAVPWHWGA NVVTNDALDP VAKIPETKAC ACKVVKITEE EARELMKKVP PVIPEIEIVR
     G
//
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