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Q6Y0Z3 (XYL1_CANPA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADH-dependent D-xylose reductase

Short name=XR
EC=1.1.1.175
Gene names
Name:XYL1
OrganismCandida parapsilosis (Yeast)
Taxonomic identifier5480 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length324 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reduces D-xylose into xylitol. Preferentially utilizes NADH as a cosubstrate.

Catalytic activity

D-xylose + NAD+ = D-xylonolactone + NADH.

Pathway

Carbohydrate metabolism; D-xylose degradation.

Sequence similarities

Belongs to the aldo/keto reductase family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Xylose metabolism
   LigandNAD
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processD-xylose metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionD-xylose 1-dehydrogenase (NAD) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 324324NADH-dependent D-xylose reductase
PRO_0000124659

Regions

Nucleotide binding220 – 28667NAD By similarity

Sites

Active site541Proton donor By similarity
Binding site1161Substrate By similarity
Site831Lowers pKa of active site Tyr By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6Y0Z3 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: C64951D131707E19

FASTA32436,629
        10         20         30         40         50         60 
MSTATASPAV KLNSGYEIPL VGFGCWKLTN DVASDQIYRA IKSGYRLFDG AEDYANEQEV 

        70         80         90        100        110        120 
GEGIKRAIKE GIVKREELFI TSKLWNSFHD KKNVEVALMK TLSDLNLDYV DLFYIHFPIA 

       130        140        150        160        170        180 
QKPVPIEKKY PPGFYCGDGD KWSIEEVPLL DTWRALEKLV DQGLAKSIGI SNFSAQLIYD 

       190        200        210        220        230        240 
LIRGCTIKPV ALQIEHHPYL TQPKLVEYVQ LHDIQITGYS SFGPQSFLEM DLKRALDTPV 

       250        260        270        280        290        300 
LLEEPTVKSI ADKHGKSPAQ VLLRYQTQRG IAVIPRSNSP DRMAQNLSVI DFELTQDDLQ 

       310        320 
AIAELDCNLR FNEPWDFSNI PVFV 

« Hide

References

[1]"Cloning and characterization of the xyl1 gene, encoding an NADH-preferring xylose reductase from Candida parapsilosis, and its functional expression in Candida tropicalis."
Lee J.K., Koo B.S., Kim S.Y.
Appl. Environ. Microbiol. 69:6179-6188(2003) [PubMed: 14532079] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
Strain: KFCC-10875.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY193716 mRNA. Translation: AAO91803.1.

3D structure databases

ProteinModelPortalQ6Y0Z3.
SMRQ6Y0Z3. Positions 8-324.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
Gene3DG3DSA:3.20.20.100. Aldo/ket_red. 1 hit.
PANTHERPTHR11732. Aldo/ket_red. 1 hit.
PfamPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFPIRSF000097. AKR. 1 hit.
PRINTSPR00069. ALDKETRDTASE.
SUPFAMSSF51430. Aldo/ket_red. 1 hit.
PROSITEPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYL1_CANPA
AccessionPrimary (citable) accession number: Q6Y0Z3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: July 5, 2004
Last modified: June 28, 2011
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families