PabA

• Description: para-aminobenzoate synthase (subunit B)/ anthranilate synthase (subunit II)
  
  

Gene name	pabA
Synonyms	trpG, trpX
Essential	no
Product	para-aminobenzoate synthase (subunit B)/ anthranilate synthase (subunit II) glutamine amidotransferase (subunit B) and anthranilate synthase (subunit II)
Function	biosynthesis of folate and tryptophan
Interactions involving this protein in SubtInteract: PabA
Metabolic function and regulation of this protein in SubtiPathways: Phe, Tyr, Trp, Folate
MW, pI	21 kDa, 4.782
Gene length, protein length	582 bp, 194 aa
Immediate neighbours	pabB, pabC
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, biosynthesis of cofactors

This gene is a member of the following regulons

TRAP regulon

The gene

Basic information

• Locus tag: BSU00750

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate (according to Swiss-Prot)

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions: PabA-PabB, PabA-TrpE

• Localization:

Database entries

• Structure:

• UniProt: P28819

• KEGG entry: [3]

• E.C. number: 2.6.1.85

Expression and regulation

• Operon: pabB-pabA-pabC-sul-folB-folK-yazB-yacF-lysS PubMed

• Expression browser: pabA PubMed

• Sigma factor: SigA PubMed

• Regulation: translation repressed by tryptophan (MtrB) PubMed

• Regulatory mechanism: MtrB: translation termination PubMed

• Additional information:
  • the pabA-pabC part of the mRNA is substantially stabilized upon depletion of RNase Y PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Original Publications

Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J  
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. 
Mol Microbiol. 2011 81(6): 1459-1473. 
PubMed:21815947