RhaB

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  • Description: rhamnulokinase

Gene name yulC
Synonyms
Essential no
Product rhamnulokinase
Function utilization of rhamnose
Gene expression levels in SubtiExpress: yulC
MW, pI 54 kDa, 5.422
Gene length, protein length 1455 bp, 485 aa
Immediate neighbours yulD, yulB
Sequences Protein DNA DNA_with_flanks
Genetic context
YulC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YulC expression.png
























Categories containing this gene/protein

utilization of specific carbon sources

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU31200

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + L-rhamnulose = ADP + L-rhamnulose 1-phosphate (according to Swiss-Prot)
  • Protein family: rhamnulokinase 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: 2UYT (the enzyme of E. coli)
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Irina A Rodionova, Xiaoqing Li, Vera Thiel, Sergey Stolyar, Krista Stanton, James K Fredrickson, Donald A Bryant, Andrei L Osterman, Aaron A Best, Dmitry A Rodionov
Comparative genomics and functional analysis of rhamnose catabolic pathways and regulons in bacteria.
Front Microbiol: 2013, 4;407
[PubMed:24391637] [WorldCat.org] [DOI] (P e)

Dirk Grueninger, Georg E Schulz
Structure and reaction mechanism of L-rhamnulose kinase from Escherichia coli.
J Mol Biol: 2006, 359(3);787-97
[PubMed:16674975] [WorldCat.org] [DOI] (P p)