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

• Sigma factor: SigA PubMed

• Regulation: translation repressed by tryptophan (MtrB) PubMed

• Regulatory mechanism: MtrB: translation termination PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

Paul Babitzke, Carol S Baker, Tony Romeo
Regulation of translation initiation by RNA binding proteins.
Annu Rev Microbiol: 2009, 63;27-44
[PubMed:19385727] [WorldCat.org] [DOI] (I p)

Paul Gollnick, Paul Babitzke, Alfred Antson, Charles Yanofsky
Complexity in regulation of tryptophan biosynthesis in Bacillus subtilis.
Annu Rev Genet: 2005, 39;47-68
[PubMed:16285852] [WorldCat.org] [DOI] (P p)

Original Publications

Helen Yakhnin, Alexander V Yakhnin, Paul Babitzke
Translation control of trpG from transcripts originating from the folate operon promoter of Bacillus subtilis is influenced by translation-mediated displacement of bound TRAP, while translation control of transcripts originating from a newly identified trpG promoter is not.
J Bacteriol: 2007, 189(3);872-9
[PubMed:17114263] [WorldCat.org] [DOI] (P p)

Antoine de Saizieu, Pierre Vankan, Cassandra Vockler, Adolphus P G M van Loon
The trp RNA-binding attenuation protein (TRAP) regulates the steady-state levels of transcripts of the Bacillus subtilis folate operon.
Microbiology (Reading): 1997, 143 ( Pt 3);979-989
[PubMed:9084182] [WorldCat.org] [DOI] (P p)

C Baumann, J Otridge, P Gollnick
Kinetic and thermodynamic analysis of the interaction between TRAP (trp RNA-binding attenuation protein) of Bacillus subtilis and trp leader RNA.
J Biol Chem: 1996, 271(21);12269-74
[PubMed:8647825] [WorldCat.org] [DOI] (P p)

P Babitzke, J T Stults, S J Shire, C Yanofsky
TRAP, the trp RNA-binding attenuation protein of Bacillus subtilis, is a multisubunit complex that appears to recognize G/UAG repeats in the trpEDCFBA and trpG transcripts.
J Biol Chem: 1994, 269(24);16597-604
[PubMed:7515880] [WorldCat.org] (P p)