Difference between revisions of "PabA"
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* '''Additional information:''' | * '''Additional information:''' | ||
+ | ** the ''[[pabA]]-[[pabC]]'' part of the mRNA is substantially stabilized upon depletion of [[Rny|RNase Y]] {{PubMed|21815947}} | ||
=Biological materials = | =Biological materials = | ||
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<pubmed>16285852, 19385727</pubmed> | <pubmed>16285852, 19385727</pubmed> | ||
==Original Publications== | ==Original Publications== | ||
+ | <big>''Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J'' </big> | ||
+ | <big>'''RNA processing in ''Bacillus subtilis'': identification of targets of the essential RNase Y.''' </big> | ||
+ | <big>Mol Microbiol. 2011 81(6): 1459-1473. </big> | ||
+ | [http://www.ncbi.nlm.nih.gov/pubmed/21815947 PubMed:21815947] | ||
<pubmed>8647825,7515880,9084182,17114263 ,, </pubmed> | <pubmed>8647825,7515880,9084182,17114263 ,, </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 19:39, 19 November 2011
- 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
|
Contents
Categories containing this gene/protein
biosynthesis/ acquisition of amino acids, biosynthesis of cofactors
This gene is a member of the following regulons
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:
Database entries
- Structure:
- UniProt: P28819
- KEGG entry: [3]
- E.C. number: 2.6.1.85
Additional information
Expression and regulation
- 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
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
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