ID   LVR_LEIAQ               Reviewed;         267 AA.
AC   Q9LBG2;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   16-JUN-2009, entry version 46.
DE   RecName: Full=Levodione reductase;
DE            EC=1.1.1.-;
DE   AltName: Full=(6R)-2,2,6-trimethyl-1,4-cyclohexanedione reductase;
GN   Name=lvr;
OS   Leifsonia aquatica (Corynebacterium aquaticum).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Microbacteriaceae; Leifsonia.
OX   NCBI_TaxID=144185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=M-13;
RX   MEDLINE=21281640; PubMed=11388460; DOI=10.1271/bbb.65.830;
RA   Yoshisumi A., Wada M., Takagi H., Shimizu S., Nakamori S.;
RT   "Cloning, sequence analysis, and expression in Escherichia coli of the
RT   gene encoding monovalent cation-activated levodione reductase from
RT   Corynebacterium aquaticum M-13.";
RL   Biosci. Biotechnol. Biochem. 65:830-836(2001).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC   STRAIN=M-13;
RX   MEDLINE=99437825; PubMed=10508066;
RA   Wada M., Yoshizumi A., Nakamori S., Shimizu S.;
RT   "Purification and characterization of monovalent cation-activated
RT   levodione reductase from Corynebacterium aquaticum M-13.";
RL   Appl. Environ. Microbiol. 65:4399-4403(1999).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH NAD AND
RP   INHIBITOR, AND MUTAGENESIS OF GLU-103.
RC   STRAIN=M-13;
RX   PubMed=12621044; DOI=10.1074/jbc.M208146200;
RA   Sogabe S., Yoshizumi A., Fukami T.A., Shiratori Y., Shimizu S.,
RA   Takagi H., Nakamori S., Wada M.;
RT   "The crystal structure and stereospecificity of levodione reductase
RT   from Corynebacterium aquaticum M-13.";
RL   J. Biol. Chem. 278:19387-19395(2003).
CC   -!- FUNCTION: Catalyzes the regio- and stereoselective reversible NAD-
CC       dependent reduction of (6R)-2,2,6-trimethyl-1,4-cyclohexanedione
CC       (levodione) to (4R,6R)-4-hydroxy-2,2,6-trimethylcyclohexanone
CC       (actinol).
CC   -!- CATALYTIC ACTIVITY: (4R,6R)-4-hydroxy-2,2,6-trimethylcyclohexanone
CC       + NAD(+) = (6R)-2,2,6-trimethyl-1,4-cyclohexanedione + NADH.
CC   -!- ENZYME REGULATION: Strongly activated by monovalent cations, such
CC       as K(+), Na(+), and NH4(+).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family.
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DR   EMBL; AB042262; BAA95121.1; -; Genomic_DNA.
DR   PDB; 1IY8; X-ray; 1.60 A; A/B/C/D/E/F/G/H=1-267.
DR   PDBsum; 1IY8; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR   InterPro; IPR002347; Glc/ribitol_DH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR19410; ADH_short_C2; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; NAD; Oxidoreductase.
FT   CHAIN         1    267       Levodione reductase.
FT                                /FTId=PRO_0000054721.
FT   NP_BIND      17     42       NAD.
FT   ACT_SITE    165    165       Proton acceptor.
FT   BINDING     152    152       Substrate.
FT   SITE        103    103       Role in the determination of
FT                                stereospecificity.
FT   MUTAGEN     103    103       E->A,D,N,Q: 26-fold increase in Km and a
FT                                much lower enantiomeric excess of the
FT                                reaction products.
FT   STRAND       15     19
FT   TURN         20     22
FT   HELIX        24     35
FT   STRAND       39     45
FT   HELIX        47     60
FT   STRAND       66     70
FT   HELIX        76     90
FT   STRAND       94     98
FT   HELIX       109    111
FT   HELIX       114    124
FT   HELIX       126    142
FT   STRAND      146    150
FT   HELIX       153    155
FT   STRAND      160    162
FT   HELIX       163    183
FT   HELIX       184    186
FT   STRAND      189    195
FT   HELIX       201    210
FT   HELIX       215    223
FT   HELIX       234    244
FT   HELIX       247    249
FT   STRAND      256    260
FT   TURN        261    265
SQ   SEQUENCE   267 AA;  27920 MW;  6F05C89383500304 CRC64;
     MTATSSPTTR FTDRVVLITG GGSGLGRATA VRLAAEGAKL SLVDVSSEGL EASKAAVLET
     APDAEVLTTV ADVSDEAQVE AYVTATTERF GRIDGFFNNA GIEGKQNPTE SFTAAEFDKV
     VSINLRGVFL GLEKVLKIMR EQGSGMVVNT ASVGGIRGIG NQSGYAAAKH GVVGLTRNSA
     VEYGRYGIRI NAIAPGAIWT PMVENSMKQL DPENPRKAAE EFIQVNPSKR YGEAPEIAAV
     VAFLLSDDAS YVNATVVPID GGQSAAY
//