Reviewed, UniProtKB/Swiss-Prot Q9UUN9 (ALD2_SPOSA)

Names and origin

Protein names	Recommended name:     Aldehyde reductase 2     EC=1.1.1.2 Alternative name(s):     Aldehyde reductase II       Short name=ARII
Organism	Sporobolomyces salmonicolor
Taxonomic identifier	5005 [NCBI]
Taxonomic lineage	Eukaryota › Fungi › Dikarya › Basidiomycota › Pucciniomycotina › Microbotryomycetes › Sporidiobolales › Sporidiobolus

Protein attributes

Sequence length	343 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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. Ref.1 Ref.2
Catalytic activity	An alcohol + NADP+ = an aldehyde + NADPH. Ref.1 Ref.2
Enzyme regulation	Inhibited by quercetin and diphenylhydantoin. Ref.2
Subunit structure	Monomer. Ref.2
Sequence similarities	Belongs to the dihydroflavonol-4-reductase family.
biophysicochemical properties	pH dependence: Optimum pH is 5.5. Temperature dependence: Optimum temperature is 40 degrees Celsius.

Ontologies

Keywords
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	alcohol dehydrogenase (NADP+) activity Ref.1 Inferred from direct assay. Source: UniProtKB coenzyme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 343

342

Aldehyde reductase 2

PRO_0000215575

Experimental info

Mutagenesis

19

1

G → A: Results in loss of substrate inhibition and of NADPH-dependent reductase activity. Ref.1

Mutagenesis

22

1

G → A: Results in loss of substrate inhibition and of NADPH-dependent reductase activity. Ref.1

Mutagenesis

25

1

A → G: Only active when NADPH is replaced by NADH. Ref.1

Secondary structure

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343

Helix Strand Turn

Details...

Beta strand

14 – 18

5

Turn

19 – 21

3

Helix

23 – 34

12

Beta strand

38 – 46

9

Helix

47 – 49

3

Helix

50 – 59

10

Turn

61 – 63

3

Beta strand

64 – 68

5

Turn

75 – 84

10

Beta strand

86 – 90

5

Helix

101 – 121

21

Beta strand

127 – 131

5

Helix

134 – 136

3

Helix

156 – 164

9

Helix

172 – 195

24

Beta strand

198 – 210

13

Helix

216 – 219

4

Helix

223 – 231

9

Helix

237 – 240

4

Beta strand

244 – 249

6

Helix

250 – 262

13

Beta strand

270 – 273

4

Beta strand

276 – 278

3

Helix

280 – 290

11

Helix

313 – 321

9

Helix

330 – 338

9

Sequences

	Sequence		Length	Mass (Da)
	Q9UUN9-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: C6CAAD9DB32E05C3	FASTA	343	37,318
	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

References

[1]	"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." Kita K., Fukura T., Nakase K., Okamoto K., Yanase H., Kataoka M., Shimizu S. Appl. Environ. Microbiol. 65:5207-5211(1999) [PubMed: 10583966] [Abstract] Cited for: 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, FUNCTION. Strain: AKU 4429.
[2]	"Purification and characterization of new aldehyde reductases from Sporobolomyces salmonicolor AKU4429." Kita K., Nakase K., Yanase H., Kataoka M., Shimizu S. J. Mol. Catal., B Enzym. 6:305-313(1999) Cited for: PROTEIN SEQUENCE OF 2-25, FUNCTION, ENZYME REGULATION. Strain: AKU 4429.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF160799 Genomic DNA. Translation: AAF15999.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UJM	X-ray	2.00	A/B	2-343	[»]
1Y1P	X-ray	1.60	A/B	2-342	[»]
1ZZE	X-ray	1.80	A/B	2-342	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.1.1.2. 754.

Family and domain databases

InterPro

IPR001509. Epimerase_deHydtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

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

Pfam

PF01370. Epimerase. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ALD2_SPOSA

Accession

Primary (citable) accession number: Q9UUN9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 46 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)