NtdA

• Description: pyridoxal phosphate-dependent 3-oxo-glucose-6-phosphate:glutamate aminotransferase
  
  

Gene name	ntdA
Synonyms	yhjL
Essential	no
Product	pyridoxal phosphate-dependent 3-oxo-glucose-6-phosphate:glutamate aminotransferase
Function	synthesis of the antibiotic kanosamine
Gene expression levels in SubtiExpress: ntdA
MW, pI	49 kDa, 5.971
Gene length, protein length	1323 bp, 441 aa
Immediate neighbours	ntdB, ntdR
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

miscellaneous metabolic pathways, biosynthesis of antibacterial compounds

This gene is a member of the following regulons

NtdR regulon

The gene

Basic information

• Locus tag: BSU10550

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • 3-oxo-d-glucose-6-phosphate + glutamate --> kanosamine-6-phosphate PubMed

• Protein family: degT/dnrJ/eryC1 family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):
  • pyridoxalphosphate PubMed

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure:

• UniProt: O07566

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: ntdA-ntdB-ntdC-glcP PubMed

• Expression browser: ntdA PubMed

• Sigma factor: SigA PubMed

• Regulation: induced by 3,3'-neotrehalosadiamine (NtdR) PubMed

• Regulatory mechanism: NtdR: positive regulator PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Original publications

Karin E van Straaten, Jong Bum Ko, Rajendra Jagdhane, Shazia Anjum, David R J Palmer, David A R Sanders
The structure of NtdA, a sugar aminotransferase involved in the kanosamine biosynthetic pathway in Bacillus subtilis, reveals a new subclass of aminotransferases.
J Biol Chem: 2013, 288(47);34121-34130
[PubMed:24097983] [WorldCat.org] [DOI] (I p)

Natasha D Vetter, David M Langill, Shazia Anjum, Julie Boisvert-Martel, Rajendra C Jagdhane, Egiroh Omene, Hongyan Zheng, Karin E van Straaten, Isaac Asiamah, Ed S Krol, David A R Sanders, David R J Palmer
A previously unrecognized kanosamine biosynthesis pathway in Bacillus subtilis.
J Am Chem Soc: 2013, 135(16);5970-3
[PubMed:23586652] [WorldCat.org] [DOI] (I p)

K E van Straaten, D M Langill, D R J Palmer, D A R Sanders
Purification, crystallization and preliminary X-ray analysis of NtdA, a putative pyridoxal phosphate-dependent aminotransferase from Bacillus subtilis.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2009, 65(Pt 4);426-9
[PubMed:19342798] [WorldCat.org] [DOI] (I p)

Takashi Inaoka, Takenori Satomura, Yasutaro Fujita, Kozo Ochi
Novel gene regulation mediated by overproduction of secondary metabolite neotrehalosadiamine in Bacillus subtilis.
FEMS Microbiol Lett: 2009, 291(2);151-6
[PubMed:19087206] [WorldCat.org] [DOI] (I p)

Takashi Inaoka, Kozo Ochi
Glucose uptake pathway-specific regulation of synthesis of neotrehalosadiamine, a novel autoinducer produced in Bacillus subtilis.
J Bacteriol: 2007, 189(1);65-75
[PubMed:17056753] [WorldCat.org] [DOI] (P p)

Takashi Inaoka, Kosaku Takahashi, Hiroshi Yada, Mitsuru Yoshida, Kozo Ochi
RNA polymerase mutation activates the production of a dormant antibiotic 3,3'-neotrehalosadiamine via an autoinduction mechanism in Bacillus subtilis.
J Biol Chem: 2004, 279(5);3885-92
[PubMed:14612444] [WorldCat.org] [DOI] (P p)