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 
This image was kindly provided by SubtiList
| |
Contents
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:
- Swiss prot entry: P28819
- KEGG entry: [3]
- E.C. number: 2.6.1.85 7)
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)
