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Reviewed, UniProtKB/Swiss-Prot Q59545 (XYLD_MORMO)

Last modified June 16, 2009. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
    D-xylulose reductase
    EC=1.1.1.9
Alternative name(s):
    Xylitol dehydrogenase
      Short name=XDH
OrganismMorganella morganii (Proteus morganii)
Taxonomic identifier582 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeMorganella

Protein attributes

Sequence length338 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

Xylitol + NAD+ = D-xylulose + NADH.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Homotetramer Potential.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

Ontologies

Keywords
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionD-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 338338D-xylulose reductase
PRO_0000160885

Sites

Metal binding401Zinc; catalytic By similarity
Metal binding651Zinc; catalytic By similarity
Metal binding1511Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q59545-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 4C6119553DC51873

FASTA33835,952
        10         20         30         40         50         60 
MIMKALVLEK AGKIAIQDWQ SNEVLGDDDV EIKIHTVGIC GSDVHYYQHG RIGPFVVDEP 

        70         80         90        100        110        120 
MVLGHEASGV ITAAGKNVKH LKVGDRVCME PGIPDLQSPQ SRAGIYNLDP AVRFWATPPI 

       130        140        150        160        170        180 
DGCLRESVIH PAAFTFKLPD NVSFAQGAMV EPLAIGMQSA TKAGIKPGDI GLVIGAGTIG 

       190        200        210        220        230        240 
IITQSALAGG CSDVIICDVF DEKLKVAEKY QGLHAVNSKD QQALADKVRE LTGGEGVNVL 

       250        260        270        280        290        300 
FECSGAKPVI ASISDHIAPG GTAVLVGMPI DPAPLDIVAA QAKEVTFKTI LRYANMYPRT 

       310        320        330 
IRLLSSGKLN VAPLLSATYK FKDSVEAYER AAEPVRLM 

« Hide

References

[1]"Molecular characterization of xylitol catabolic pathways in the Enterobacteriaceae."
Gallo M.A., Mortlock R.P.
Thesis (1991), University of Wisconsin-Madison, United States
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 25829 / DSM 6675 / NCTC 417.
[2]"Inducible xylitol dehydrogenases in enteric bacteria."
Doten R.C., Mortlock R.P.
J. Bacteriol. 162:845-848(1985) [PubMed: 3886639] [Abstract]
Cited for: CHARACTERIZATION.
Strain: ATCC 25829 / DSM 6675 / NCTC 417.

Cross-references

Sequence databases

L34345 Genomic DNA. Translation: AAA25324.1.

3D structure databases

HSSPHSSP built from PDB template 1E3J based on UniProtKB O96496.
ModBaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MON-12199.
BRENDA1.1.1.9. 2621.

Family and domain databases

InterProIPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR002328. ADH_Zn_CS.
[Graphical view]
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
ProDomPD040557. GroES_related. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYLD_MORMO
AccessionPrimary (citable) accession number: Q59545
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

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