YszB
Revision as of 10:06, 20 April 2012 by 134.76.70.252 (talk)
- Description: chorismate mutase
Gene name | pheB |
Synonyms | |
Essential | no |
Product | chorismate mutase |
Function | biosynthesis of phenylalanine |
Metabolic function and regulation of this protein in SubtiPathways: Phe, Tyr, Trp | |
MW, pI | 16 kDa, 6.36 |
Gene length, protein length | 441 bp, 147 aa |
Immediate neighbours | pheA, obg |
Get the DNA and protein sequences (Barbe et al., 2009) | |
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
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU27910
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: UPF0735 family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: P21204
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Sigma factor:
- Regulation:
- Regulatory mechanism:
- 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
Frederik Claeyssens, Kara E Ranaghan, Narin Lawan, Stephen J Macrae, Frederick R Manby, Jeremy N Harvey, Adrian J Mulholland
Analysis of chorismate mutase catalysis by QM/MM modelling of enzyme-catalysed and uncatalysed reactions.
Org Biomol Chem: 2011, 9(5);1578-90
[PubMed:21243152]
[WorldCat.org]
[DOI]
(I p)
K Trach, J A Hoch
The Bacillus subtilis spo0B stage 0 sporulation operon encodes an essential GTP-binding protein.
J Bacteriol: 1989, 171(3);1362-71
[PubMed:2537815]
[WorldCat.org]
[DOI]
(P p)