Difference between revisions of "ProA"
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Revision as of 13:04, 16 May 2013
- Description: glutamate-5-semialdehyde dehydrogenase, required for normal and osmoadaptive proline biosynthesis
| Gene name | proA |
| Synonyms | |
| Essential | no |
| Product | glutamate-5-semialdehyde dehydrogenase |
| Function | biosynthesis of proline |
| Gene expression levels in SubtiExpress: proA | |
| Metabolic function and regulation of this protein in SubtiPathways: Pro, Stress | |
| MW, pI | 45 kDa, 5.098 |
| Gene length, protein length | 1245 bp, 415 aa |
| Immediate neighbours | proB, ohrA |
| Sequences | Protein DNA DNA_with_flanks |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
biosynthesis/ acquisition of amino acids, coping with hyper-osmotic stress
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU13130
Phenotypes of a mutant
- auxotrophic for proline PubMed
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH (according to Swiss-Prot)
- Protein family: gamma-glutamyl phosphate reductase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- UniProt: P39821
- KEGG entry: [2]
- E.C. number: 1.2.1.41
Additional information
Expression and regulation
- Regulatory mechanism:
- T-box: RNA switch, transcriptional antitermination PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Additional publications: PubMed
Vivianne J Goosens, Ruben A T Mars, Michiel Akeroyd, Andre Vente, Annette Dreisbach, Emma L Denham, Thijs R H M Kouwen, Tjeerd van Rij, Maurien Olsthoorn, Jan Maarten van Dijl
Is proteomics a reliable tool to probe the oxidative folding of bacterial membrane proteins?
Antioxid Redox Signal: 2013, 18(10);1159-64
[PubMed:22540663]
[WorldCat.org]
[DOI]
(I p)
Jeanette Brill, Tamara Hoffmann, Harald Putzer, Erhard Bremer
T-box-mediated control of the anabolic proline biosynthetic genes of Bacillus subtilis.
Microbiology (Reading): 2011, 157(Pt 4);977-987
[PubMed:21233158]
[WorldCat.org]
[DOI]
(I p)
Ana Gutiérrez-Preciado, Tina M Henkin, Frank J Grundy, Charles Yanofsky, Enrique Merino
Biochemical features and functional implications of the RNA-based T-box regulatory mechanism.
Microbiol Mol Biol Rev: 2009, 73(1);36-61
[PubMed:19258532]
[WorldCat.org]
[DOI]
(I p)
