Difference between revisions of "XylB"

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(Expression and regulation)
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=== Database entries ===
 
=== Database entries ===
  
* '''Structure:'''
+
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=2NLX 2NLX] (from ''E. coli'', 35% identity, 52% similarity) {{PubMed|17123542}}
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P39211 P39211]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P39211 P39211]
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=References=
 
=References=
 
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<pubmed>17123542 1921970 2454911 8132469</pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 10:00, 18 February 2010

  • Description: xylulokinase

Gene name xylB
Synonyms yncA
Essential no
Product xylulokinase
Function utilization of xylan and xylose
Metabolic function and regulation of this protein in SubtiPathways:
Sugar catabolism
MW, pI 55 kDa, 6.459
Gene length, protein length 1497 bp, 499 aa
Immediate neighbours xylA, yncB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
XylB context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU17610

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + D-xylulose = ADP + D-xylulose 5-phosphate (according to Swiss-Prot)
  • Protein family: FGGY kinase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization:

Database entries

  • Structure: 2NLX (from E. coli, 35% identity, 52% similarity) PubMed
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Wolfgang Hillen, Erlangen University, Germany Homepage

Your additional remarks

References

Eric Di Luccio, Barbara Petschacher, Jennifer Voegtli, Hui-Ting Chou, Henning Stahlberg, Bernd Nidetzky, David K Wilson
Structural and kinetic studies of induced fit in xylulose kinase from Escherichia coli.
J Mol Biol: 2007, 365(3);783-98
[PubMed:17123542] [WorldCat.org] [DOI] (P p)

A Kraus, C Hueck, D Gärtner, W Hillen
Catabolite repression of the Bacillus subtilis xyl operon involves a cis element functional in the context of an unrelated sequence, and glucose exerts additional xylR-dependent repression.
J Bacteriol: 1994, 176(6);1738-45
[PubMed:8132469] [WorldCat.org] [DOI] (P p)

S Jacob, R Allmansberger, D Gärtner, W Hillen
Catabolite repression of the operon for xylose utilization from Bacillus subtilis W23 is mediated at the level of transcription and depends on a cis site in the xylA reading frame.
Mol Gen Genet: 1991, 229(2);189-96
[PubMed:1921970] [WorldCat.org] [DOI] (P p)

D Gärtner, M Geissendörfer, W Hillen
Expression of the Bacillus subtilis xyl operon is repressed at the level of transcription and is induced by xylose.
J Bacteriol: 1988, 170(7);3102-9
[PubMed:2454911] [WorldCat.org] [DOI] (P p)