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Database: UniProt/TrEMBL
Entry: B5YBK5_DICT6
LinkDB: B5YBK5_DICT6
Original site: B5YBK5_DICT6 
ID   B5YBK5_DICT6            Unreviewed;       342 AA.
AC   B5YBK5;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE            EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN   OrderedLocusNames=DICTH_0188 {ECO:0000313|EMBL:ACI18697.1};
OS   Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12).
OC   Bacteria; Dictyoglomota; Dictyoglomia; Dictyoglomales; Dictyoglomaceae;
OC   Dictyoglomus.
OX   NCBI_TaxID=309799 {ECO:0000313|EMBL:ACI18697.1, ECO:0000313|Proteomes:UP000001733};
RN   [1] {ECO:0000313|EMBL:ACI18697.1, ECO:0000313|Proteomes:UP000001733}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35947 / DSM 3960 / H-6-12
RC   {ECO:0000313|Proteomes:UP000001733};
RX   PubMed=24558247;
RA   Coil D.A., Badger J.H., Forberger H.C., Riggs F., Madupu R., Fedorova N.,
RA   Ward N., Robb F.T., Eisen J.A.;
RT   "Complete Genome Sequence of the Extreme Thermophile Dictyoglomus
RT   thermophilum H-6-12.";
RL   Genome Announc. 2:e00109-e00114(2014).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072}.
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DR   EMBL; CP001146; ACI18697.1; -; Genomic_DNA.
DR   RefSeq; WP_012547329.1; NC_011297.1.
DR   AlphaFoldDB; B5YBK5; -.
DR   STRING; 309799.DICTH_0188; -.
DR   PaxDb; 309799-DICTH_0188; -.
DR   KEGG; dth:DICTH_0188; -.
DR   eggNOG; COG1064; Bacteria.
DR   HOGENOM; CLU_026673_20_7_0; -.
DR   OrthoDB; 9771084at2; -.
DR   Proteomes; UP000001733; Chromosome.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   CDD; cd08298; CAD2; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR014187; ADH_Zn_typ-2.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   NCBIfam; TIGR02822; adh_fam_2; 1.
DR   PANTHER; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR   PANTHER; PTHR42940:SF8; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000313|EMBL:ACI18697.1}.
FT   DOMAIN          17..339
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   342 AA;  38411 MW;  65F7B6265A04988E CRC64;
     MKAMLLREVK DLTVWQDPLS LEEVSIPIPK EKEILIKVSA CGVCRTDLDI VEGRLPPTKL
     PLILGHQIVG TVVDKGKDAN KFQIGDRVGV AWINHSCGVC RFCRSGQENL CDDFKATGKD
     VDGGYAEYTV VSEDYAYKIP QNYSDEEAAP LLCAGAIGYR SVKLSNIKNG DNIGLSGFGA
     SGHLVLKIIK YLYPDSKIFV FARSEREREL AKELGSYWTG DFGEVTPFKL NAIIDTTPVW
     KTIVLVLRNL EKGGRLVINA IRKENQDKDF LINLNYERDL WMEKEIKSVA NITRRDVEEF
     LTLAEKVDLK PVVEVYKLEE ANKALRDLKE GRIRGAKVLK MS
//
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