Difference between revisions of "YugJ"
| Line 14: | Line 14: | ||
|style="background:#ABCDEF;" align="center"|'''Function''' || unknown | |style="background:#ABCDEF;" align="center"|'''Function''' || unknown | ||
|- | |- | ||
| − | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http:// | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU31370 yugJ] |
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 42 kDa, 5.221 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 42 kDa, 5.221 | ||
| Line 22: | Line 22: | ||
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yugK]]'', ''[[yuzA]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yugK]]'', ''[[yuzA]]'' | ||
|- | |- | ||
| − | | | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU31370 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU31370 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU31370 Advanced_DNA] |
|- | |- | ||
|colspan="2" | '''Genetic context''' <br/> [[Image:yugJ_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:yugJ_context.gif]] | ||
Revision as of 13:43, 13 May 2013
- 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 Advanced_DNA |
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
- 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
- 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
Bauke Oudega, Gregory Koningstein, Luísa Rodrigues, Maria de Sales Ramon, Helmut Hilbert, Andreas Düsterhöft, Thomas M Pohl, Thomas Weitzenegger
Analysis of the Bacillus subtilis genome: cloning and nucleotide sequence of a 62 kb region between 275 degrees (rrnB) and 284 degrees (pai).
Microbiology (Reading): 1997, 143 ( Pt 8);2769-2774
[PubMed:9274030]
[WorldCat.org]
[DOI]
(P p)
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)
