LVR_LEIAQ
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 03-AUG-2022, entry version 86.
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; Micrococcales; Microbacteriaceae; Leifsonia.
OX NCBI_TaxID=144185;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M-13;
RX 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 gene
RT 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 PubMed=10508066; DOI=10.1128/aem.65.10.4399-4403.1999;
RA Wada M., Yoshizumi A., Nakamori S., Shimizu S.;
RT "Purification and characterization of monovalent cation-activated levodione
RT 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 INHIBITOR,
RP 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., Takagi H.,
RA Nakamori S., Wada M.;
RT "The crystal structure and stereospecificity of levodione reductase from
RT 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:
CC Reaction=(4R)-hydroxy-(6R)-2,2,6-trimethylcyclohexanone + NAD(+) =
CC (6R)-2,2,6-trimethyl-1,4-cyclohexanedione + H(+) + NADH;
CC Xref=Rhea:RHEA:46676, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:86399, ChEBI:CHEBI:86400;
CC -!- ACTIVITY REGULATION: Strongly activated by monovalent cations, such as
CC K(+), Na(+), and NH4(+).
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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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 AlphaFoldDB; Q9LBG2; -.
DR SMR; Q9LBG2; -.
DR BioCyc; MetaCyc:MON-20560; -.
DR EvolutionaryTrace; Q9LBG2; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NAD; Oxidoreductase.
FT CHAIN 1..267
FT /note="Levodione reductase"
FT /id="PRO_0000054721"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT BINDING 17..42
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12621044"
FT BINDING 152
FT /ligand="substrate"
FT SITE 103
FT /note="Role in the determination of stereospecificity"
FT MUTAGEN 103
FT /note="E->A,D,N,Q: 26-fold increase in Km and a much lower
FT enantiomeric excess of the reaction products."
FT /evidence="ECO:0000269|PubMed:12621044"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:1IY8"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:1IY8"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:1IY8"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:1IY8"
FT HELIX 47..60
FT /evidence="ECO:0007829|PDB:1IY8"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:1IY8"
FT HELIX 76..90
FT /evidence="ECO:0007829|PDB:1IY8"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:1IY8"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:1IY8"
FT HELIX 114..124
FT /evidence="ECO:0007829|PDB:1IY8"
FT HELIX 126..142
FT /evidence="ECO:0007829|PDB:1IY8"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:1IY8"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1IY8"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:1IY8"
FT HELIX 163..183
FT /evidence="ECO:0007829|PDB:1IY8"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:1IY8"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:1IY8"
FT HELIX 201..210
FT /evidence="ECO:0007829|PDB:1IY8"
FT HELIX 215..223
FT /evidence="ECO:0007829|PDB:1IY8"
FT HELIX 234..244
FT /evidence="ECO:0007829|PDB:1IY8"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:1IY8"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:1IY8"
FT TURN 261..265
FT /evidence="ECO:0007829|PDB:1IY8"
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
