ID   E2EA39_9ZZZZ            Unreviewed;       605 AA.
AC   E2EA39;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Formate dehydrogenase H {ECO:0000313|EMBL:ADN27362.1};
DE   Flags: Fragment;
GN   Name=fdhF {ECO:0000313|EMBL:ADN27362.1};
OS   uncultured prokaryote.
OC   unclassified sequences; environmental samples.
OX   NCBI_TaxID=198431 {ECO:0000313|EMBL:ADN27362.1};
RN   [1] {ECO:0000313|EMBL:ADN27362.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20819103; DOI=10.1111/j.1462-2920.2010.02330.x;
RA   Zhang X., Matson E.G., Leadbetter J.R.;
RT   "Genes for selenium dependent and independent formate dehydrogenase in the
RT   gut microbial communities of three lower, wood-feeding termites and a wood-
RT   feeding roach.";
RL   Environ. Microbiol. 13:307-323(2011).
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
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DR   EMBL; GU563446; ADN27362.1; -; Genomic_DNA.
DR   GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
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; cd02753; MopB_Formate-Dh-H; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 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   NCBIfam; TIGR01591; Fdh-alpha; 1.
DR   PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Selenium {ECO:0000313|EMBL:ADN27362.1};
KW   Selenocysteine {ECO:0000313|EMBL:ADN27362.1}.
FT   DOMAIN          10..440
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          529..605
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
FT   NON_STD         90
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000313|EMBL:ADN27362.1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADN27362.1"
FT   NON_TER         605
FT                   /evidence="ECO:0000313|EMBL:ADN27362.1"
SQ   SEQUENCE   605 AA;  67157 MW;  107ACC994991431B CRC64;
     LNDPQILTRR LTKPMIRKGG KHSPLEEVEW DEAITYTADR LSAIKKEFGP DAIMGTGSAR
     GPGNEANYIM QKFMRAVIGT NNIDHCARIU HAPSVAGLLY SLGSGAMSMG VPEIEDAALL
     FVFGYNGADS HPIVARRIVR AKQKGATIVC TDPRRTETAR IADIHLQLKG GSNLALVNAI
     ANTLIEEDLC DYKFIAEHST GFDEFKEVVK KYTPENTAAT TGLDPELVRR ATRLYAASGR
     SMILYGMGVC QFSQAVDVVK SLANLAIMTG NFGRPSTGIG PVRGQNNVQG ACDMGALPNS
     YPGYQNVTVP EVRTKFEKAW GVPLSDKVGI TLTKVPHHVL HEKGAKKIHA YYIMGEDPAQ
     SDPDLAEVRE GLEKCDFVIF QDIYMNKTGQ FADVVLPATG WCEHEGVYSC CDRGFQRFKK
     LIEPQGDLKK DWEIISLLAT AMGYPMKYNN TEEIWNEVID LCPGFKGATY EKIEKYGSIQ
     WPCRSTDMED KGTVYLHKDG KFAHPDGKAK FFATEWHPPT ELESPEFPLA LSTVREVGHY
     SSRSMTGNCR MLRNLEDEPG WIQMNPRDCR RLGDIKEGEL VKVLSPRGWC LTRCLPTDRV
     KKGAV
//