Difference between revisions of "GamA"

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* '''Regulation:'''  
* '''Regulation:'''  
** induced by N-acetylglucosamine {{PubMed|14343123}}  
** induced by N-acetylglucosamine {{PubMed|14343123}}  
** induced by glucosamine ([[GamR]]) {{PubMed|23667565}}  
** induced by glucosamine ([[GamR]]) {{PubMed|24673833,23667565}}  
* '''Regulatory mechanism:'''  
* '''Regulatory mechanism:'''  
** [[GamR]]: transcription repression {{PubMed|23667565}}  
** [[GamR]]: transcription repression {{PubMed|24673833,23667565}}  
* '''Additional information:'''
* '''Additional information:'''
Line 138: Line 138:
<pubmed>10627040, 14343123 23667565 23876412 15755726 </pubmed>
<pubmed>10627040, 14343123 23667565 23876412 24673833,15755726 </pubmed>
[[Category:Protein-coding genes]]
[[Category:Protein-coding genes]]

Revision as of 10:52, 31 March 2014

  • Description: glucosamine-6-phosphate deaminase

Gene name gamA
Synonyms ybfT
Essential no
Product glucosamine-6-phosphate deaminase
Function glucosamine utilization
Gene expression levels in SubtiExpress: gamA
Metabolic function and regulation of this protein in SubtiPathways:
MW, pI 27 kDa, 5.793
Gene length, protein length 747 bp, 249 aa
Immediate neighbours gamP, gamR
Sequences Protein DNA DNA_with_flanks
Genetic context
GamA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
GamA expression.png

Categories containing this gene/protein

cell wall degradation/ turnover, utilization of specific carbon sources

This gene is a member of the following regulons

GamR regulon

The gene

Basic information

  • Locus tag: BSU02360

Phenotypes of a mutant

  • no growth on glucosamine PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: d-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3 (according to Swiss-Prot)
  • Protein family: NagB subfamily (according to Swiss-Prot)
  • Paralogous protein(s): NagB

Extended information on the protein

  • Kinetic information: K(M): 3.0 mM PubMed
  • Modification:
  • Effectors of protein activity:

Database entries

  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • 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


Isabelle Gaugué, Jacques Oberto, Jacqueline Plumbridge
Regulation of amino sugar utilization in Bacillus subtilis by the GntR family regulators, NagR and GamR.
Mol Microbiol: 2014, 92(1);100-15
[PubMed:24673833] [WorldCat.org] [DOI] (I p)

Yanfeng Liu, Long Liu, Hyun-dong Shin, Rachel R Chen, Jianghua Li, Guocheng Du, Jian Chen
Pathway engineering of Bacillus subtilis for microbial production of N-acetylglucosamine.
Metab Eng: 2013, 19;107-15
[PubMed:23876412] [WorldCat.org] [DOI] (I p)

Isabelle Gaugué, Jacques Oberto, Harald Putzer, Jacqueline Plumbridge
The use of amino sugars by Bacillus subtilis: presence of a unique operon for the catabolism of glucosamine.
PLoS One: 2013, 8(5);e63025
[PubMed:23667565] [WorldCat.org] [DOI] (I e)

Florence Vincent, Gideon J Davies, James A Brannigan
Structure and kinetics of a monomeric glucosamine 6-phosphate deaminase: missing link of the NagB superfamily?
J Biol Chem: 2005, 280(20);19649-55
[PubMed:15755726] [WorldCat.org] [DOI] (P p)

Jonathan Reizer, Steffi Bachem, Aiala Reizer, Maryvonne Arnaud, Milton H Saier, Jörg Stülke
Novel phosphotransferase system genes revealed by genome analysis - the complete complement of PTS proteins encoded within the genome of Bacillus subtilis.
Microbiology (Reading): 1999, 145 ( Pt 12);3419-3429
[PubMed:10627040] [WorldCat.org] [DOI] (P p)

Biochem J: 1965, 96;147-54
[PubMed:14343123] [WorldCat.org] [DOI] (P p)