Difference between revisions of "YpdA"
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU22950&redirect=T BSU22950] | ||
* '''DBTBS entry:''' no entry | * '''DBTBS entry:''' no entry | ||
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU22950&redirect=T BSU22950] | ||
* '''Structure:''' | * '''Structure:''' |
Revision as of 14:05, 2 April 2014
- Description: similar to thioredoxin reductase
Gene name | ypdA |
Synonyms | |
Essential | no |
Product | unknown |
Function | unknown |
Gene expression levels in SubtiExpress: ypdA | |
MW, pI | 36 kDa, 6.083 |
Gene length, protein length | 972 bp, 324 aa |
Immediate neighbours | prsW, gudB |
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
electron transport/ other, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU22950
Phenotypes of a mutant
Database entries
- BsubCyc: BSU22950
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: Trx reductase family
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
- cell membrane (according to Swiss-Prot)
Database entries
- BsubCyc: BSU22950
- Structure:
- UniProt: P50736
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- 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
YpdA, YqiW, YphP and YtxJ cooccur in those species predicted to synthesize bacillithiol.
References
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)