ID E2DDE4_9ZZZZ Unreviewed; 605 AA.
AC E2DDE4;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Formate dehydrogenase H {ECO:0000313|EMBL:ADN27272.1};
DE Flags: Fragment;
GN Name=fdhF {ECO:0000313|EMBL:ADN27272.1};
OS uncultured prokaryote.
OC unclassified sequences; environmental samples.
OX NCBI_TaxID=198431 {ECO:0000313|EMBL:ADN27272.1};
RN [1] {ECO:0000313|EMBL:ADN27272.1}
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; GQ922385; ADN27272.1; -; 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 InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
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.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Selenium {ECO:0000313|EMBL:ADN27272.1};
KW Selenocysteine {ECO:0000313|EMBL:ADN27272.1}.
FT DOMAIN 10..441
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 530..605
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
FT NON_STD 90
FT /note="Selenocysteine"
FT /evidence="ECO:0000313|EMBL:ADN27272.1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADN27272.1"
FT NON_TER 605
FT /evidence="ECO:0000313|EMBL:ADN27272.1"
SQ SEQUENCE 605 AA; 66422 MW; 4501D0FE57AEF14B CRC64;
LNDPQILSKR LRKPMIRKGG KGSALEEVEW DEAIAYTAGR LKEIKEKHGP NAIMCTGSAR
GPGNEANYIM QKFARAAVGT NNVDHCARIU HAPSVAGLQY SFGSGAMTMG VPEIEDAALL
FVFGYNGADS HPIVARRIVR AKQKGAKIIC ADPRIIETAR IADMHLQLKG GTNLLLVNAI
ANTILEEGLC DNAFIAEHSN GFDEFKEIIK KYTPEGVSAQ VGISAADIRK AARMYATSGR
SMILYGMGVC QFGQAVDVVK ALANLTIMTG NLGRPSTGIG PVRGQNNVQG ACDMGALPNV
FPGYQAVTNA EIRAKFEKAW GVKLPDQNGI TLTVVPHQVL HETDPAKKIH GYYIMGEDPV
QSDPDSAEAR ESLEKCDFVV MQDIFMNKTG QYADVILPAT SWCEHEGVYS CCDRGFQRVR
KILEPVGDLK TDWQIISELS TAMGYPMKYT KTEEIWNELI ELCPNFAGAT YAKIEKQGSV
QWPCRDKADS DTGTVYLHKG GKCSNPDGKA NFFATDWRPP QELENKDYPL TLCTVREVGH
YSVRTMSGNC RMLRNLEDEP GWLQISPRDA EALGIRHKEL VRVSSIRGSV ITRANVTERV
KKGAV
//
