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Reviewed, UniProtKB/Swiss-Prot Q8NK50 (DCXR_TRIRE)

Last modified January 19, 2010. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    L-xylulose reductase
      Short name=XR
    EC=1.1.1.10
Gene names
Name: lxr1
OrganismTrichoderma reesei (Hypocrea jecorina)
Taxonomic identifier51453 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeHypocrea

Protein attributes

Sequence length266 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of L-xylulose, D-xylulose, D-fructose, and L-sorbose, with the highest affinity for L-xylulose.

Catalytic activity

Xylitol + NADP+ = L-xylulose + NADPH. Ref.1

Pathway

Carbohydrate degradation; L-arabinose degradation via L-arabinitol; D-xylulose 5-phosphate from L-arabinose (fungal route): step 3/5.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionL-xylulose reductase (NADP+) activity

Inferred from electronic annotation. Source: EC

binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 266266L-xylulose reductase
PRO_0000054558

Regions

Nucleotide binding23 – 5331NADP By similarity

Sites

Active site1741Proton acceptor By similarity
Active site1781 By similarity
Binding site1591Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8NK50-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 1CF56334DA86F109

FASTA26628,478
        10         20         30         40         50         60 
MPQPVPTANR LLDLFSLKGK VVVVTGASGP RGMGIEAARG CAEMGADLAI TYSSRKEGAE 

        70         80         90        100        110        120 
KNAEELTKEY GVKVKVYKVN QSDYNDVERF VNQVVSDFGK IDAFIANAGA TANSGVVDGS 

       130        140        150        160        170        180 
ASDWDHVIQV DLSGTAYCAK AVGAHFKKQG HGSLVITASM SGHVANYPQE QTSYNVAKAG 

       190        200        210        220        230        240 
CIHLARSLAN EWRDFARVNS ISPGYIDTGL SDFIDEKTQE LWRSMIPMGR NGDAKELKGA 

       250        260 
YVYLVSDASS YTTGADIVID GGYTTR 

« Hide

References

[1]"The missing link in the fungal L-arabinose catabolic pathway, identification of the L-xylulose reductase gene."
Richard P., Putkonen M., Vaeaenaenen R., Londesborough J., Penttilae M.
Biochemistry 41:6432-6437(2002) [PubMed: 12009906] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF375616 mRNA. Translation: AAM20896.1.

3D structure databases

SMRQ8NK50. Positions 2-265.
ModBaseSearch...

Phylogenomic databases

PhylomeDBQ8NK50.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13194.
BRENDA1.1.1.10. 280374.

Family and domain databases

InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR19410. ADH_short_C2. 1 hit.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PROSITEPS00061. ADH_SHORT. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDCXR_TRIRE
AccessionPrimary (citable) accession number: Q8NK50
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: October 1, 2002
Last modified: January 19, 2010
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents