[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=M-13; DOI=10.1271/bbb.65.830; PubMed=11388460 [NCBI, ExPASy, EBI, Israel, Japan] Yoshisumi A., Wada M., Takagi H., Shimizu S., Nakamori S.; "Cloning, sequence analysis, and expression in Escherichia coli of the gene encoding monovalent cation-activated levodione reductase from Corynebacterium aquaticum M-13."; Biosci. Biotechnol. Biochem. 65:830-836(2001).
[2]	PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION. STRAIN=M-13; PubMed=10508066 [NCBI, ExPASy, EBI, Israel, Japan] Wada M., Yoshizumi A., Nakamori S., Shimizu S.; "Purification and characterization of monovalent cation-activated levodione reductase from Corynebacterium aquaticum M-13."; Appl. Environ. Microbiol. 65:4399-4403(1999).
[3]	X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR, AND MUTAGENESIS OF GLU-103. STRAIN=M-13; DOI=10.1074/jbc.M208146200; PubMed=12621044 [NCBI, ExPASy, EBI, Israel, Japan] Sogabe S., Yoshizumi A., Fukami T.A., Shiratori Y., Shimizu S., Takagi H., Nakamori S., Wada M.; "The crystal structure and stereospecificity of levodione reductase from Corynebacterium aquaticum M-13."; J. Biol. Chem. 278:19387-19395(2003).

Comments

FUNCTION: Catalyzes the regio- and stereoselective reversible NAD-dependent reduction of (6R)-2,2,6-trimethyl-1,4-cyclohexanedione (levodione) to (4R,6R)-4-hydroxy-2,2,6-trimethylcyclohexanone (actinol).
CATALYTIC ACTIVITY: (4R,6R)-4-hydroxy-2,2,6-trimethylcyclohexanone + NAD⁺ = (6R)-2,2,6-trimethyl-1,4-cyclohexanedione + NADH.
ENZYME REGULATION: Strongly activated by monovalent cations, such as K(+), Na(+), and NH4(+).
SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AB042262; BAA95121.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1IY8; X-ray; 1.60 A; A/B/C/D/E/F/G/H=1-267.

[ExPASy / RCSB / EBI]

PDBsum

1IY8; -.

ModBase

Q9LBG2.

Ontologies

GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0016491;	Molecular function: oxidoreductase activity (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

PANTHER

PTHR19410; ADH_short_C2; 1.

Pfam

PF00106; adh_short; 1.
Pfam graphical view of domain structure.

PRINTS

PR00081; GDHRDH.
PR00080; SDRFAMILY.

ProtoNet

Q9LBG2.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 267`	`267`	`Levodione reductase.`	`PRO_0000054721`
`NP_BIND`	`17 42`	`26`	`NAD.`
`ACT_SITE`	`165 165`		`Proton acceptor.`
`BINDING`	`152 152`		`Substrate.`
`SITE`	`103 103`	`1`	`Role in the determination of stereospecificity.`
`MUTAGEN`	`103 103`		`E->A,D,N,Q: 26-fold increase in Km and a much lower enantiomeric excess of the reaction products.`
`STRAND`	`15 19`	`5`
`TURN`	`20 22`	`3`
`HELIX`	`24 35`	`12`
`STRAND`	`39 45`	`7`
`HELIX`	`47 60`	`14`
`STRAND`	`66 70`	`5`
`HELIX`	`76 90`	`15`
`STRAND`	`94 98`	`5`
`HELIX`	`109 111`	`3`
`HELIX`	`114 124`	`11`
`HELIX`	`126 142`	`17`
`STRAND`	`146 150`	`5`
`HELIX`	`153 155`	`3`
`STRAND`	`160 162`	`3`
`HELIX`	`163 183`	`21`
`HELIX`	`184 186`	`3`
`STRAND`	`189 195`	`7`
`HELIX`	`201 210`	`10`
`HELIX`	`215 223`	`9`
`HELIX`	`234 244`	`11`
`HELIX`	`247 249`	`3`
`STRAND`	`256 260`	`5`
`TURN`	`261 265`	`5`

Sequence information

Length: 267 AA [This is the length of the unprocessed precursor]

Molecular weight: 27920 Da [This is the MW of the unprocessed precursor]

CRC64: 6F05C89383500304 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTATSSPTTR FTDRVVLITG GGSGLGRATA VRLAAEGAKL SLVDVSSEGL EASKAAVLET 

        70         80         90        100        110        120 
APDAEVLTTV ADVSDEAQVE AYVTATTERF GRIDGFFNNA GIEGKQNPTE SFTAAEFDKV 

       130        140        150        160        170        180 
VSINLRGVFL GLEKVLKIMR EQGSGMVVNT ASVGGIRGIG NQSGYAAAKH GVVGLTRNSA 

       190        200        210        220        230        240 
VEYGRYGIRI NAIAPGAIWT PMVENSMKQL DPENPRKAAE EFIQVNPSKR YGEAPEIAAV 

       250        260 
VAFLLSDDAS YVNATVVPID GGQSAAY

Q9LBG2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools