NagA

• Description: N-acetylglucosamine-6-phosphate deacetylase
  
  

Gene name	nagA
Synonyms
Essential	no
Product	N-acetylglucosamine-6-phosphate deacetylase
Function	N-acetylglucosamine utilization
Gene expression levels in SubtiExpress: nagA
Metabolic function and regulation of this protein in SubtiPathways: Sugar catabolism, Murein recycling
MW, pI	42 kDa, 5.276
Gene length, protein length	1188 bp, 396 aa
Immediate neighbours	hprK, nagB
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

cell wall degradation/ turnover, utilization of specific carbon sources

This gene is a member of the following regulons

CcpA regulon, NagR regulon

The gene

Basic information

• Locus tag: BSU35010

Phenotypes of a mutant

• no growth on N-acetylglucosamine PubMed

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: N-acetyl-D-glucosamine 6-phosphate + H₂O = D-glucosamine 6-phosphate + acetate (according to Swiss-Prot)

• Protein family: nagA family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information: K(M): 1.4 mM PubMed

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure: 2VHL PubMed

• UniProt: O34450

• KEGG entry: [2]

• E.C. number: 3.5.1.25

Expression and regulation

• Operon: nagA-nagB-nagR PubMed

• Expression browser: nagA PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • induced in the presence of N-acetylglucosamine (NagR) PubMed
  • repressed by glucose (2.9-fold) (CcpA) PubMed

• Regulatory mechanism:
  • NagR: transcription repression PubMed
  • CcpA: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)

Ralph Bertram, Sébastien Rigali, Natalie Wood, Andrzej T Lulko, Oscar P Kuipers, Fritz Titgemeyer
Regulon of the N-acetylglucosamine utilization regulator NagR in Bacillus subtilis.
J Bacteriol: 2011, 193(14);3525-36
[PubMed:21602348] [WorldCat.org] [DOI] (I p)

Florence Vincent, David Yates, Elspeth Garman, Gideon J Davies, James A Brannigan
The three-dimensional structure of the N-acetylglucosamine-6-phosphate deacetylase, NagA, from Bacillus subtilis: a member of the urease superfamily.
J Biol Chem: 2004, 279(4);2809-16
[PubMed:14557261] [WorldCat.org] [DOI] (P p)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [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)

H L Mobley, R J Doyle, U N Streips, S O Langemeier
Transport and incorporation of N-acetyl-D-glucosamine in Bacillus subtilis.
J Bacteriol: 1982, 150(1);8-15
[PubMed:6174502] [WorldCat.org] [DOI] (P p)

C J BATES, C A PASTERNAK
FURTHER STUDIES ON THE REGULATION OF AMINO SUGAR METABOLISM IN BACILLUS SUBTILIS.
Biochem J: 1965, 96(1);147-54
[PubMed:14343123] [WorldCat.org] [DOI] (P p)