ID   G8N731_GEOTH            Unreviewed;       336 AA.
AC   G8N731;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=Alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00016352};
DE            EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN   ORFNames=GTCCBUS3UF5_8140 {ECO:0000313|EMBL:AEV18137.1};
OS   Geobacillus thermoleovorans CCB_US3_UF5.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=1111068 {ECO:0000313|EMBL:AEV18137.1, ECO:0000313|Proteomes:UP000005636};
RN   [1] {ECO:0000313|EMBL:AEV18137.1, ECO:0000313|Proteomes:UP000005636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCB_US3_UF5 {ECO:0000313|EMBL:AEV18137.1,
RC   ECO:0000313|Proteomes:UP000005636};
RA   Muhd Sakaff M.K.L., Abdul Rahman A.Y., Saito J.A., Hou S., Alam M.;
RT   "Complete genome sequence of thermophilic Geobacillus thermoleovorans
RT   CCB_US3_UF5.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC         Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001146};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC         Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC         ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000781};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; CP003125; AEV18137.1; -; Genomic_DNA.
DR   RefSeq; WP_011230234.1; NC_016593.1.
DR   AlphaFoldDB; G8N731; -.
DR   KEGG; gte:GTCCBUS3UF5_8140; -.
DR   PATRIC; fig|1111068.3.peg.787; -.
DR   HOGENOM; CLU_026673_20_1_9; -.
DR   Proteomes; UP000005636; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08297; CAD3; 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; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
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; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          10..334
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   336 AA;  35951 MW;  D81E53107D29D6D7 CRC64;
     MKAAVVHKFK QKLQIEEVEK PKLGYGEVLV KIEACGVCHT DLHAAHGDWP VKPKLPLIPG
     HEGVGIVVEI GEGVKSIQIG DRVGIPWLYS ACGECEYCLS GQETLCPHQL NGGYSVDGSY
     AEYCKAPANY VARIPKNLDP VQVAPILCAG VTTYKALKVS NAKPGEWVAI YGIGGLGHIA
     LQYAKAMGLN VVAVDISDEK AELAAKLGAD ITINGLQEDP VAAIREKVGG VQAAISVAVT
     KKAFEQAYQS VRRGGCLVIV GLPHDELPIP IFDTVLNGVT IKGSIVGTRK DMQEALDFAA
     RGKVRPIVEA VPLEKINEVF ERMEKGQING RVVLTM
//