NtdA

From SubtiWiki
Revision as of 19:54, 12 November 2013 by Jstuelk (talk | contribs) (Original publications)
Jump to: navigation, search
  • 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
YhjL context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
NtdA expression.png















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

Phenotypes of a mutant

Database entries

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

Additional information

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):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • 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:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Takashi Inaoka, Kozo Ochi
Activation of dormant secondary metabolism neotrehalosadiamine synthesis by an RNA polymerase mutation in Bacillus subtilis.
Biosci Biotechnol Biochem: 2011, 75(4);618-23
[PubMed:21512256] [WorldCat.org] [DOI] (I p)

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)