Difference between revisions of "BshA"
| Line 80: | Line 80: | ||
=== Database entries === | === Database entries === | ||
| − | * '''Structure:''' | + | * '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?structureId=3MBO 3MBO] (from ''B. anthracis'') {{PubMed|20799687}} |
* '''UniProt:''' [http://www.uniprot.org/uniprot/P42982 P42982] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P42982 P42982] | ||
| Line 121: | Line 121: | ||
=References= | =References= | ||
| − | <pubmed> 20308541 19578333 </pubmed> | + | <pubmed> 20308541 19578333 20799687 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 18:06, 6 December 2010
- Description: L-malic acid glycosyltransferase, involved in bacillithiol synthesis
| Gene name | bshA |
| Synonyms | jojH, ypjH |
| Essential | no |
| Product | L-malic acid glycosyltransferase |
| Function | biosynthesis of bacillithiol |
| MW, pI | 41 kDa, 6.149 |
| Gene length, protein length | 1131 bp, 377 aa |
| Immediate neighbours | cca, bshB1 |
| 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: BSU22460
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
Categories containing this gene/protein
miscellaneous metabolic pathways, resistance against oxidative and electrophile stress
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: UDP-GlcNAc + L-malate = GlcNAc(α1→2)L-malate PubMed; also uses D-malate as a substrate, but with much lower affinity PubMed
- Protein family: NamA subfamily (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- UniProt: P42982
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant: bshA::mls available in John_Helmann lab
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Derek Parsonage, Gerald L Newton, Robert C Holder, Bret D Wallace, Carleitta Paige, Chris J Hamilton, Patricia C Dos Santos, Matthew R Redinbo, Sean D Reid, Al Claiborne
Characterization of the N-acetyl-α-D-glucosaminyl l-malate synthase and deacetylase functions for bacillithiol biosynthesis in Bacillus anthracis .
Biochemistry: 2010, 49(38);8398-414
[PubMed:20799687]
[WorldCat.org]
[DOI]
(I p)
Ahmed Gaballa, Gerald L Newton, Haike Antelmann, Derek Parsonage, Heather Upton, Mamta Rawat, Al Claiborne, Robert C Fahey, John D Helmann
Biosynthesis and functions of bacillithiol, a major low-molecular-weight thiol in Bacilli.
Proc Natl Acad Sci U S A: 2010, 107(14);6482-6
[PubMed:20308541]
[WorldCat.org]
[DOI]
(I p)
Gerald L Newton, Mamta Rawat, James J La Clair, Vishnu Karthik Jothivasan, Tanya Budiarto, Chris J Hamilton, Al Claiborne, John D Helmann, Robert C Fahey
Bacillithiol is an antioxidant thiol produced in Bacilli.
Nat Chem Biol: 2009, 5(9);625-7
[PubMed:19578333]
[WorldCat.org]
[DOI]
(I p)
