ID E2DDC0_9ZZZZ Unreviewed; 606 AA.
AC E2DDC0;
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:ADN27248.1};
DE Flags: Fragment;
GN Name=fdhF {ECO:0000313|EMBL:ADN27248.1};
OS uncultured prokaryote.
OC unclassified sequences; environmental samples.
OX NCBI_TaxID=198431 {ECO:0000313|EMBL:ADN27248.1};
RN [1] {ECO:0000313|EMBL:ADN27248.1}
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; GQ922361; ADN27248.1; -; 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:ADN27248.1};
KW Selenocysteine {ECO:0000313|EMBL:ADN27248.1}.
FT DOMAIN 10..442
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 532..606
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
FT NON_STD 90
FT /note="Selenocysteine"
FT /evidence="ECO:0000313|EMBL:ADN27248.1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADN27248.1"
FT NON_TER 606
FT /evidence="ECO:0000313|EMBL:ADN27248.1"
SQ SEQUENCE 606 AA; 67030 MW; 575F8D4C543674F2 CRC64;
LNDPQIISKR LRKPMIRKGG KGSPLVEVEW DEAISYTAGR LSEIKKKYGP NAIMGTGSAR
GPGNEANYIM QKFMRAAVGT NNVDHCARIU HAPSVAGLQY SFGSGAMTMG VPEIEDAALL
LVFGYNGADS HPIVARRIVR AKEKGAKIIC VDPRIIETAR IADVHLQLKG GTNLLLVNAL
ANVIIEEGLC DYDFIEKHSN DFDQFKEVIK KYTPESVAEQ TRIPAEDIRK AARMYATSGK
SMILYGMGVC QFGQAVDVVK GLANLTIMTG NLGRPSTGIG PVRGQNNVQG ACDMGALPNV
YPGYQSVTVP EIKAKFEKAW GVKQLSDQPG ITLTMVPHHV LHEKDPAKKI RAYYIMGEDP
AQSDPDLAEV RESLEKCEFV VFQDIYMNKT GQYADVILPA TGWCEHEGVY TCCDRGFQRI
RKIIEPTGDV KTDWDIISRI STAMGYPMKY NNTEEIWNEL IALCPGFAGA TYAKIEKQGC
VQWPCRDKGE QDTGTVYLHK DGKFANPDGK AKFFATDWRP PQELENKDYP ITLCTVREVD
HYSVRTMTGN CRTLRNLEDE PGWVQISPAD AAALGIKHRE LVRISSKRGS VITRANVTER
VKKGAV
//
