ID E2DDE1_9ZZZZ Unreviewed; 606 AA.
AC E2DDE1;
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:ADN27269.1};
DE Flags: Fragment;
GN Name=fdhF {ECO:0000313|EMBL:ADN27269.1};
OS uncultured prokaryote.
OC unclassified sequences; environmental samples.
OX NCBI_TaxID=198431 {ECO:0000313|EMBL:ADN27269.1};
RN [1] {ECO:0000313|EMBL:ADN27269.1}
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; GQ922382; ADN27269.1; -; 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:ADN27269.1};
KW Selenocysteine {ECO:0000313|EMBL:ADN27269.1}.
FT DOMAIN 10..442
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 531..606
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
FT NON_STD 90
FT /note="Selenocysteine"
FT /evidence="ECO:0000313|EMBL:ADN27269.1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADN27269.1"
FT NON_TER 606
FT /evidence="ECO:0000313|EMBL:ADN27269.1"
SQ SEQUENCE 606 AA; 66863 MW; 18B77F49EA512E20 CRC64;
LNDPQILSKR LRKPMIRKGG KGSALEEVEW DEAISYTAKR LMEIKEKHGP NAIMCTGSAR
GPGNEANYIM QKFARAAVGT NNVDHCARIU HAPSVAGLQY SFGSGAMTMG VPEIEDAALL
FVFGYNGADS HPIVARRIVR AKQKGAKIIC ADPRIIETAR IADMHLQLKG GTNLLLVNAI
ANTILEEGLC DNDFIAQHSN GFDEFKEIIK KYTPEGVSAQ VGIPAEDIRK AARMYATSGR
SMILYGMGVC QFGQAVDVVK ALANLTIMTG NLGRPSTGIG PVRGQNNVQG ACDMGALPNV
FPGYQAVTNP DIRAKFEKAW GVDKLPDQNG ITLTVVPHQV LHEKDPTKQI HGYYIMGEDP
VQSDPDSAEV RESLEKCDFV VMQDIFMNKT GQFADVILPA TSWCEHEGVY SCCDRGFQRV
RKILEPVGDL KTDWQIICEL STAMGYPMKY NKTEEIWNEL IELCPNFAGA TYAKIEKQGS
VQWPCRDKAD SDTGTVYLHK GGKCSNPDGK ANFFATDWRP PQELENKDYP LTLCTVREVG
HYSVRTMSGN CRMLRNLEDE PGWLQISPRD AEALGIRHKE LVRVSSKRGS VITRANVTER
VKKGAV
//
