ID   A0A0H4NX81_9BACI        Unreviewed;       350 AA.
AC   A0A0H4NX81;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=2,3-butanediol dehydrogenaseR-alcohol forming R and S-acetoin-specific {ECO:0000313|EMBL:AKP46451.1};
DE            EC=1.1.1.4 {ECO:0000313|EMBL:AKP46451.1};
GN   ORFNames=BSM4216_1151 {ECO:0000313|EMBL:AKP46451.1};
OS   Bacillus smithii.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1479 {ECO:0000313|EMBL:AKP46451.1, ECO:0000313|Proteomes:UP000036353};
RN   [1] {ECO:0000313|EMBL:AKP46451.1, ECO:0000313|Proteomes:UP000036353}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4216 {ECO:0000313|EMBL:AKP46451.1,
RC   ECO:0000313|Proteomes:UP000036353};
RA   Bosma E.F., Koehorst J.J., van Hijum S.A.F.T., Renckens B., Vriesendorp B.,
RA   van de Weijer A.H.P., Schaap P.J., de Vos W.M., van der Oost J.,
RA   van Kranenburg R.;
RT   "Complete genome sequence of thermophilic Bacillus smithii type strain DSM
RT   4216T.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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; CP012024; AKP46451.1; -; Genomic_DNA.
DR   RefSeq; WP_048622912.1; NZ_CP012024.1.
DR   AlphaFoldDB; A0A0H4NX81; -.
DR   STRING; 1479.BSM4216_1151; -.
DR   KEGG; bsm:BSM4216_1151; -.
DR   eggNOG; COG1063; Bacteria.
DR   OrthoDB; 9770238at2; -.
DR   Proteomes; UP000036353; Chromosome.
DR   GO; GO:0000721; F:(R,R)-butanediol dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08233; butanediol_DH_like; 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; PTHR43161:SF23; (R,R)-BUTANEDIOL DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 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|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AKP46451.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          7..347
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   350 AA;  37995 MW;  D84C54B3B33D0410 CRC64;
     MKGARWHNVR DIRVEEVEEP KVEKGKVKIQ VEWAGICGSD LHEYVAGPIF IPVKEPHPIS
     KDVAPIIMGH EFSGRVVEVG EGVTKVKVGD PVVVEPILRC GKCPACKQGK YNLCENLGFH
     GLAGGGGGFS EYTVVDEYMV HKMPEGLSFE QGALVEPAAV ALHAVRSSKI KAGDKAAVFG
     TGPIGLLVIE ALKAAGASEI YAVEVSEERL QKALELGATV VINPKNEDPV QKLLELTDGG
     VDVSFEVTGV PAVLQQAVDS TAFEGETVIV SIWEKEANLL PNNIVLKERN VKGVIAYRDI
     FPAVMNLMKQ GYFPAEKLVT KKIKLDQIVE EGFEKLIKEK DQVKILVKPE
//