Difference between revisions of "YugJ"
Line 117: | Line 117: | ||
* '''Additional information:''' | * '''Additional information:''' | ||
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium): 1310 {{PubMed|24696501}} | ||
+ | ** number of protein molecules per cell (complex medium with amino acids, without glucose): 1788 {{PubMed|24696501}} | ||
=Biological materials = | =Biological materials = |
Revision as of 09:29, 17 April 2014
- Description: similar to NADH-dependent butanol dehydrogenase
Gene name | yugJ |
Synonyms | |
Essential | no |
Product | unknown |
Function | unknown |
Gene expression levels in SubtiExpress: yugJ | |
MW, pI | 42 kDa, 5.221 |
Gene length, protein length | 1161 bp, 387 aa |
Immediate neighbours | yugK, yuzA |
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
poorly characterized/ putative enzymes
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU31370
Phenotypes of a mutant
Database entries
- BsubCyc: BSU31370
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: iron-containing alcohol dehydrogenase family (according to Swiss-Prot)
- Paralogous protein(s): YugK
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- BsubCyc: BSU31370
- Structure:
- UniProt: O05239
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Sigma factor:
- 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
Laura R Jarboe
YqhD: a broad-substrate range aldehyde reductase with various applications in production of biorenewable fuels and chemicals.
Appl Microbiol Biotechnol: 2011, 89(2);249-57
[PubMed:20924577]
[WorldCat.org]
[DOI]
(I p)
Original publications
The corresponding protein in E. coli
Changhan Lee, Insook Kim, Junghoon Lee, Kang-Lok Lee, Bumchan Min, Chankyu Park
Transcriptional activation of the aldehyde reductase YqhD by YqhC and its implication in glyoxal metabolism of Escherichia coli K-12.
J Bacteriol: 2010, 192(16);4205-14
[PubMed:20543070]
[WorldCat.org]
[DOI]
(I p)
José Manuel Pérez, Felipe A Arenas, Gonzalo A Pradenas, Juan M Sandoval, Claudio C Vásquez
Escherichia coli YqhD exhibits aldehyde reductase activity and protects from the harmful effect of lipid peroxidation-derived aldehydes.
J Biol Chem: 2008, 283(12);7346-53
[PubMed:18211903]
[WorldCat.org]
[DOI]
(P p)