Reviewed, UniProtKB/Swiss-Prot P22144 (XYL2_PICST)

Names and origin

Protein names

Recommended name:
    D-xylulose reductase
    EC=1.1.1.9
Alternative name(s):
    Xylitol dehydrogenase
      Short name=XDH

Gene names

Name:	XYL2
ORF Names:	PICST_86924

Organism

Pichia stipitis (Yeast) [Complete proteome]

Taxonomic identifier

4924 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Pichia

Protein attributes

Sequence length	363 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (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.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Xylose metabolism
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	D-xylose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	D-xylulose reductase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 363	363	D-xylulose reductase		PRO_0000160883
Regions
	Nucleotide binding	183 – 188	6	NAD Potential
Sites
	Metal binding	41	1	Zinc; catalytic By similarity
	Metal binding	66	1	Zinc; catalytic By similarity
	Metal binding	159	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	P22144-1 [UniParc]. Last modified August 1, 1991. Version 1. Checksum: 39E16FD087160248	FASTA	363	38,521
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of the Pichia stipitis xylitol dehydrogenase gene, XYL2, and construction of a xylose-utilizing Saccharomyces cerevisiae transformant." Koetter P., Amore R., Hollenberg C.P., Ciriacy M. Curr. Genet. 18:493-500(1990) [PubMed: 2127555] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 62970 / CBS 5774 / NRRL Y-11542.
[2]	"Characterization and complementation of a Pichia stipitis mutant unable to grow on D-xylose or L-arabinose." Shi N.-Q., Prahl K., Hendrick J., Cruz J., Lu P., Cho J.-Y., Jones S., Jeffries T.W. Appl. Biochem. Biotechnol. 84:201-216(2000) [PubMed: 10849789] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 58785 / CBS 6054 / IFO 10063 / NRRL Y-11545.
[3]	"Genome sequence of the lignocellulose-bioconverting and xylose-fermenting yeast Pichia stipitis." 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. Nat. Biotechnol. 25:319-326(2007) [PubMed: 17334359] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 58785 / CBS 6054 / IFO 10063 / NRRL Y-11545.
[4]	"Dual relationships of xylitol and alcohol dehydrogenases in families of two protein types." Persson B., Hallborn J., Walfridsson M., Hahn-Haegerdal B., Keraenen S., Penttilae M., Joernvall H. FEBS Lett. 324:9-14(1993) [PubMed: 8504864] [Abstract] Cited for: SIMILARITY TO OTHER ZINC-ALCOHOL DEHYDROGENASES.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X55392 Genomic DNA. Translation: CAA39066.1. AF127801 Genomic DNA. Translation: AAD28251.1. AAVQ01000002 Genomic DNA. Translation: EAZ62959.1.
PIR	S13529.
RefSeq	XP_001386982.1.
3D structure databases
HSSP	HSSP built from PDB template 1E3J based on UniProtKB O96496.
ModBase	Search...
Genome annotation databases
GeneID	4852013.
KEGG	pic:PICST_86924.
Phylogenomic databases
OMA	P22144. NLCPHMA.
Enzyme and pathway databases
BRENDA	1.1.1.9. 81766.
Family and domain databases
InterPro	IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn. IPR013149. ADH_Zn-bd. IPR002328. ADH_Zn_CS. [Graphical view]
PANTHER	PTHR11695. ADH_Sf_Zn. 1 hit.
Pfam	PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view]
PROSITE	PS00059. ADH_ZINC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYL2_PICST

Accession

Primary (citable) accession number: P22144
Secondary accession number(s): A3GIB4, Q549G5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	June 16, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)