Difference between revisions of "PabA"

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|style="background:#ABCDEF;" align="center"|'''Function''' || biosynthesis of folate and tryptophan
 
|style="background:#ABCDEF;" align="center"|'''Function''' || biosynthesis of folate and tryptophan
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/folate_biosynthesis.html Folate]'''
 
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 21 kDa, 4.782   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 21 kDa, 4.782   

Revision as of 13:38, 16 June 2009

  • 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
Metabolic function and regulation of this protein in SubtiPathways:
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
PabA context.gif
This image was kindly provided by SubtiList






The gene

Basic information

  • Locus tag: BSU00750

Phenotypes of a mutant

Database entries

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

Additional information

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:
  • Localization:

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation: translation repressed by tryptophan (MtrB)
  • Regulatory mechanism: MtrB: translation termination
  • 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

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)

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)