ID   B2GIS5_KOCRD            Unreviewed;       358 AA.
AC   B2GIS5;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   SubName: Full=2,3-butanediol dehydrogenase {ECO:0000313|EMBL:BAG30602.1};
DE            EC=1.1.1.4 {ECO:0000313|EMBL:BAG30602.1};
GN   OrderedLocusNames=KRH_22550 {ECO:0000313|EMBL:BAG30602.1};
OS   Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=378753 {ECO:0000313|EMBL:BAG30602.1, ECO:0000313|Proteomes:UP000008838};
RN   [1] {ECO:0000313|EMBL:BAG30602.1, ECO:0000313|Proteomes:UP000008838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201
RC   {ECO:0000313|Proteomes:UP000008838};
RX   PubMed=18408034; DOI=10.1128/JB.01853-07;
RA   Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA   Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL   J. Bacteriol. 190:4139-4146(2008).
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; AP009152; BAG30602.1; -; Genomic_DNA.
DR   RefSeq; WP_012399323.1; NC_010617.1.
DR   AlphaFoldDB; B2GIS5; -.
DR   STRING; 378753.KRH_22550; -.
DR   KEGG; krh:KRH_22550; -.
DR   eggNOG; COG1063; Bacteria.
DR   HOGENOM; CLU_026673_11_0_11; -.
DR   OrthoDB; 9797931at2; -.
DR   Proteomes; UP000008838; 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:BAG30602.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008838};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          8..351
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   358 AA;  38112 MW;  074889738B704660 CRC64;
     MRAARYYGRN DIRIDELPEP EVGPGMVGID VAWCGICGTD LHEYLEGPIF CPTPDTPHPI
     SGETAPVTMG HEFSGVIYEL GDGVGDLRVG QHVVVEPYII GEDVDTGPES KDYHLSRDMN
     FIGLAGGGGG LGEKIAVRRR WVHPVSDVVP LDQAALIEPL SVGYHAAERS GAKAGDVAVV
     GGAGPIGLLT AAVLKALSVT VVVSELSPLR RQKALDTGVA DYALDPREVD VAQEVRRLTN
     GKGADVAFEC TSVQVVLDTL MDVLRPTGVL VVVSIWGKRA DFDMHKLVMK EIDLRGTIAY
     VNSHPATIEL VESGKIDLAP FITGKIGVDG LVEEGFETLI HRNETAVKIL VSPSGEGL
//