Skip Header

Contribute Send feedback
Read comments (?) or add your own

O94735 (XYL1_PICGU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 52. 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADPH-dependent D-xylose reductase
Short name=XR
EC=1.1.1.-
Gene names
Name:XYL1
ORF Names:PGUG_00922
OrganismMeyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii) [Complete proteome]
Taxonomic identifier294746 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Meyerozyma

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Pathway

Carbohydrate metabolism; D-xylose degradation.

Sequence similarities

Belongs to the aldo/keto reductase family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Xylose metabolism
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processD-xylose metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionoxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 317317NADPH-dependent D-xylose reductase
PRO_0000124666

Regions

Nucleotide binding164 – 1652NADP By similarity
Nucleotide binding213 – 22210NADP By similarity
Nucleotide binding269 – 27911NADP By similarity

Sites

Active site471Proton donor By similarity
Binding site1091Substrate By similarity
Site761Lowers pKa of active site Tyr By similarity

Experimental info

Sequence conflict41T → K in AAD09330. Ref.1
Sequence conflict101E → D in AAD09330. Ref.1
Sequence conflict231K → N in AAD09330. Ref.1
Sequence conflict511K → R in ABB87187. Ref.2
Sequence conflict551E → D in AAD09330. Ref.1
Sequence conflict751S → P in ABB87187. Ref.2
Sequence conflict931R → K in AAD09330. Ref.1
Sequence conflict1361I → H in AAD09330. Ref.1
Sequence conflict1361I → T in ABB87187. Ref.2
Sequence conflict1391G → D in AAD09330. Ref.1
Sequence conflict1391G → D in ABB87187. Ref.2
Sequence conflict1421I → L in AAD09330. Ref.1
Sequence conflict1521M → L in AAD09330. Ref.1
Sequence conflict1671P → S in AAD09330. Ref.1
Sequence conflict1771G → S in AAD09330. Ref.1
Sequence conflict1991I → V in AAD09330. Ref.1
Sequence conflict2241N → D in AAD09330. Ref.1
Sequence conflict245 – 2484EKAN → GKVK in AAD09330. Ref.1
Sequence conflict2931K → Q in AAD09330. Ref.1
Sequence conflict3171V → I in AAD09330. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O94735 [UniParc].

Last modified July 10, 2007. Version 2.
Checksum: DA18DF2A03186327

FASTA31736,086
        10         20         30         40         50         60 
MSITLNSGYE MPSVGFGCWK VDKATCADTI YNAIKVGYRL FDGAEDYGNE KEVGEGINRA 

        70         80         90        100        110        120 
LDEGLVARDE LFVVSKLWNS FHDPKNVEKA LDRTLSDLKV DYLDLFLIHF PIAFKFVPFE 

       130        140        150        160        170        180 
EKYPPGFYCG DGDKFIYEGV PIIDTWRALE KMVEKGKIRS IGISNFPGAL IQDLLRGAKI 

       190        200        210        220        230        240 
KPAVLQIEHH PYLQQPRLIE YVQSQGIAIT AYSSFGPQSF VELNHPRVKD VKPLFEHDVI 

       250        260        270        280        290        300 
KSVAEKANKT PAQVLLRWAT QRGLAVIPKS NNPDRLLSNL KVNDFDLSQE DFKEISKLDI 

       310 
ELRFNNPWDW DKIPTFV

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of Candida guilliermondii xylose reductase gene (xyl1) in Pichia pastoris."
Handumrongkul C., Ma D.-P., Silva J.L.
Appl. Microbiol. Biotechnol. 49:399-404(1998) [PubMed: 9615481] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
Strain: ATCC 20118 / CBS 6319 / IFO 0838 / JCM 2298 / NCYC 1399.
[2]"Isolation and phylogenetic relationship of aldose reductase in Candida species."
Guo C., He P., Lu D., Shen A., Jiang N.
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Evolution of pathogenicity and sexual reproduction in eight Candida genomes."
Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J. expand/collapse author list , Harris D., Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W., Kellis M., Cuomo C.A.
Nature 459:657-662(2009) [PubMed: 19465905] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF020040 mRNA. Translation: AAD09330.1.
DQ297454 Genomic DNA. Translation: ABB87187.1.
CH408155 Genomic DNA. Translation: EDK36824.1.
RefSeqXP_001487545.1. XM_001487495.1.

3D structure databases

ProteinModelPortalO94735.
SMRO94735. Positions 3-317.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5128729.
KEGGpgu:PGUG_00922.

Phylogenomic databases

OrthoDBEOG47SWPM.

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_PICGU
AccessionPrimary (citable) accession number: O94735
Secondary accession number(s): A5DCB7, Q2V572
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: July 10, 2007
Last modified: December 14, 2011
This is version 52 of the entry and version 2 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents