NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 39-54; 75-83; 153-161; 182-184 AND 336-343, MUTAGENESIS OF GLY-19; GLY-22 AND ALA-25, AND FUNCTION.
STRAIN=AKU 4429;
PubMed=10583966 [NCBI, ExPASy, EBI, Israel, Japan]
Kita K., Fukura T., Nakase K., Okamoto K., Yanase H., Kataoka M., Shimizu S.;
"Cloning, overexpression, and mutagenesis of the Sporobolomyces salmonicolor AKU4429 gene encoding a new aldehyde reductase, which catalyzes the stereoselective reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (S)-4-chloro-3-hydroxybutanoate.";
Appl. Environ. Microbiol. 65:5207-5211(1999).

[2]

PROTEIN SEQUENCE OF 2-25, FUNCTION, AND ENZYME REGULATION.
STRAIN=AKU 4429;
Kita K., Nakase K., Yanase H., Kataoka M., Shimizu S.;
"Purification and characterization of new aldehyde reductases from Sporobolomyces salmonicolor AKU4429.";
J. Mol. Catal., B Enzym. 6:305-313(1999).

Comments

FUNCTION: Catalyzes the asymmetric reduction of o-substituted aliphatic and aromatic aldehydes and ketones to an S-enantiomer. Reduces ethyl 4-chloro-3-oxobutanoate to ethyl (S)-4-chloro-3-hydroxybutanoate.
CATALYTIC ACTIVITY: An alcohol + NADP⁺ = an aldehyde + NADPH.
ENZYME REGULATION: Inhibited by quercetin and diphenylhydantoin.
BIOPHYSICOCHEMICAL PROPERTIES:

pH dependence: Optimum pH is 5.5;
Temperature dependence: Optimum temperature is 40 degrees Celsius;
SUBUNIT: Monomer.
SIMILARITY: Belongs to the dihydroflavonol-4-reductase 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

AF160799; AAF15999.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1UJM; X-ray; 2.00 A; A/B=1-343.	[ExPASy / RCSB / EBI]
1Y1P; X-ray; 1.60 A; A/B=1-343.	[ExPASy / RCSB / EBI]
1ZZE; X-ray; 1.80 A; A/B=1-343.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1UJM; -.
1Y1P; -.
1ZZE; -.

ModBase

Q9UUN9.

Ontologies

GO:0008106;	Molecular function: alcohol dehydrogenase (NADP+) activity (inferred from direct assay from UniProtKB).
GO:0050662;	Molecular function: coenzyme binding (inferred from electronic annotation from InterPro).
GO:0044237;	Biological process: cellular metabolic process (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

IPR001509; Epimerase_deHydtase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

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

Pfam

PF01370; Epimerase; 1.
Pfam graphical view of domain structure.

ProtoNet

Q9UUN9.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 343`	`342`	`Aldehyde reductase 2.`	`PRO_0000215575`
`MUTAGEN`	`19 19`		`G->A: Results in loss of substrate inhibition and of NADPH-dependent reductase activity.`
`MUTAGEN`	`22 22`		`G->A: Results in loss of substrate inhibition and of NADPH-dependent reductase activity.`
`MUTAGEN`	`25 25`		`A->G: Only active when NADPH is replaced by NADH.`
`STRAND`	`14 18`	`5`
`TURN`	`19 21`	`3`
`HELIX`	`23 34`	`12`
`STRAND`	`38 46`	`9`
`HELIX`	`47 49`	`3`
`HELIX`	`50 59`	`10`
`TURN`	`61 63`	`3`
`STRAND`	`64 68`	`5`
`TURN`	`75 84`	`10`
`STRAND`	`86 90`	`5`
`HELIX`	`101 121`	`21`
`STRAND`	`127 131`	`5`
`HELIX`	`134 136`	`3`
`HELIX`	`156 164`	`9`
`HELIX`	`172 195`	`24`
`STRAND`	`198 210`	`13`
`HELIX`	`216 219`	`4`
`HELIX`	`223 231`	`9`
`HELIX`	`237 240`	`4`
`STRAND`	`244 249`	`6`
`HELIX`	`250 262`	`13`
`STRAND`	`270 273`	`4`
`STRAND`	`276 278`	`3`
`HELIX`	`280 290`	`11`
`HELIX`	`313 321`	`9`
`HELIX`	`330 338`	`9`

Sequence information

Length: 343 AA [This is the length of the unprocessed precursor]

Molecular weight: 37318 Da [This is the MW of the unprocessed precursor]

CRC64: C6CAAD9DB32E05C3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAKIDNAVLP EGSLVLVTGA NGFVASHVVE QLLEHGYKVR GTARSASKLA NLQKRWDAKY 

        70         80         90        100        110        120 
PGRFETAVVE DMLKQGAYDE VIKGAAGVAH IASVVSFSNK YDEVVTPAIG GTLNALRAAA 

       130        140        150        160        170        180 
ATPSVKRFVL TSSTVSALIP KPNVEGIYLD EKSWNLESID KAKTLPESDP QKSLWVYAAS 

       190        200        210        220        230        240 
KTEAELAAWK FMDENKPHFT LNAVLPNYTI GTIFDPETQS GSTSGWMMSL FNGEVSPALA 

       250        260        270        280        290        300 
LMPPQYYVSA VDIGLLHLGC LVLPQIERRR VYGTAGTFDW NTVLATFRKL YPSKTFPADF 

       310        320        330        340 
PDQGQDLSKF DTAPSLEILK SLGRPGWRSI EESIKDLVGS ETA

Q9UUN9 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