[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 62970 / CBS 5774 / NRRL Y-11542; DOI=10.1007/BF00327019; PubMed=2127555 [NCBI, ExPASy, EBI, Israel, Japan] Koetter P., Amore R., Hollenberg C.P., Ciriacy M.; "Isolation and characterization of the Pichia stipitis xylitol dehydrogenase gene, XYL2, and construction of a xylose-utilizing Saccharomyces cerevisiae transformant."; Curr. Genet. 18:493-500(1990).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 58785 / CBS 6054 / IFO 10063 / NRRL Y-11545; DOI=10.1385/ABAB:84-86:1-9:201; PubMed=10849789 [NCBI, ExPASy, EBI, Israel, Japan] Shi N.-Q., Prahl K., Hendrick J., Cruz J., Lu P., Cho J.-Y., Jones S., Jeffries T.W.; "Characterization and complementation of a Pichia stipitis mutant unable to grow on D-xylose or L-arabinose."; Appl. Biochem. Biotechnol. 84:201-216(2000).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 58785 / CBS 6054 / IFO 10063 / NRRL Y-11545; DOI=10.1038/nbt1290; PubMed=17334359 [NCBI, ExPASy, EBI, Israel, Japan] Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A., Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S., Passoth V., Richardson P.M.; "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting yeast Pichia stipitis."; Nat. Biotechnol. 25:319-326(2007).
[4]	SIMILARITY TO OTHER ZINC-ALCOHOL DEHYDROGENASES. DOI=10.1016/0014-5793(93)81522-2; PubMed=8504864 [NCBI, ExPASy, EBI, Israel, Japan] Persson B., Hallborn J., Walfridsson M., Hahn-Haegerdal B., Keraenen S., Penttilae M., Joernvall H.; "Dual relationships of xylitol and alcohol dehydrogenases in families of two protein types."; FEBS Lett. 324:9-14(1993).

Comments

CATALYTIC ACTIVITY: Xylitol + NAD⁺ = D-xylulose + NADH.
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-arabinitol; D-xylulose 5-phosphate from L-arabinose (fungi route): step 4/5 .
INDUCTION: By xylose. Repressed by glucose.
SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase 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

X55392; CAA39066.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF127801; AAD28251.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AAVQ01000002; EAZ62959.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S13529; S13529.

RefSeq

XP_001386982.1; -.

3D structure databases

HSSP

O96496; 1E3J. [HSSP ENTRY / PDB]

ModBase

P22144.

Ontologies

GO:0046526;	Molecular function: D-xylulose reductase activity (inferred from electronic annotation from EC).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0042732;	Biological process: D-xylose metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
IPR002328; AlcDHase_Zn_CS.
Graphical view of domain structure.

PANTHER

PTHR11695; ADH_Sf_Zn; 1.

Pfam

PF08240; ADH_N; 1.
PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.

PROSITE

PS00059; ADH_ZINC; 1.

ProtoNet

P22144.

Genome annotation databases

GeneID

4852013; -.

KEGG

pic:PICST_86924; -.

Other

UniRef

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

Keywords

Carbohydrate metabolism; Complete proteome; Metal-binding; NAD; Oxidoreductase; Xylose metabolism; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 363`	`363`	`D-xylulose reductase.`	`PRO_0000160883`
`NP_BIND`	`183 188`	`6`	`NAD (Potential).`
`METAL`	`41 41`		`Zinc; catalytic (By similarity).`
`METAL`	`66 66`		`Zinc; catalytic (By similarity).`
`METAL`	`159 159`		`Zinc; catalytic (By similarity).`

Sequence information

Length: 363 AA [This is the length of the unprocessed precursor]

Molecular weight: 38521 Da [This is the MW of the unprocessed precursor]

CRC64: 39E16FD087160248 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTANPSLVLN KIDDISFETY DAPEISEPTD VLVQVKKTGI CGSDIHFYAH GRIGNFVLTK 

        70         80         90        100        110        120 
PMVLGHESAG TVVQVGKGVT SLKVGDNVAI EPGIPSRFSD EYKSGHYNLC PHMAFAATPN 

       130        140        150        160        170        180 
SKEGEPNPPG TLCKYFKSPE DFLVKLPDHV SLELGALVEP LSVGVHASKL GSVAFGDYVA 

       190        200        210        220        230        240 
VFGAGPVGLL AAAVAKTFGA KGVIVVDIFD NKLKMAKDIG AATHTFNSKT GGSEELIKAF 

       250        260        270        280        290        300 
GGNVPNVVLE CTGAEPCIKL GVDAIAPGGR FVQVGNAAGP VSFPITVFAM KELTLFGSFR 

       310        320        330        340        350        360 
YGFNDYKTAV GIFDTNYQNG RENAPIDFEQ LITHRYKFKD AIEAYDLVRA GKGAVKCLID 


GPE

P22144 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