Difference between revisions of "Hom"
| Line 29: | Line 29: | ||
<div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | ||
|- | |- | ||
| − | |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=hom_3314828_3316129_-1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:hom_expression.png|500px]] | + | |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=hom_3314828_3316129_-1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:hom_expression.png|500px|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU32260]] |
|- | |- | ||
|} | |} | ||
Revision as of 14:29, 16 May 2013
- Description: homoserine dehydrogenase (NADPH)
| Gene name | hom |
| Synonyms | |
| Essential | no |
| Product | homoserine dehydrogenase (NADPH) |
| Function | biosynthesis of methionine and threonine |
| Gene expression levels in SubtiExpress: hom | |
| Metabolic function and regulation of this protein in SubtiPathways: Lys, Thr | |
| MW, pI | 47 kDa, 4.9 |
| Gene length, protein length | 1299 bp, 433 aa |
| Immediate neighbours | thrC, yutH |
| 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
biosynthesis/ acquisition of amino acids, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU32260
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H (according to Swiss-Prot)
- Protein family: homoserine dehydrogenase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity: subject to feedback inhibition PubMed
- Localization:
- membrane associated PubMed
Database entries
- Structure: 2EJW (from Thermus thermophilus hb8, 37% identity, 57% similarity)
- UniProt: P19582
- KEGG entry: [2]
- E.C. number: 1.1.1.3
Additional information
Expression and regulation
- Sigma factor:
- Regulation:
- repressed by casamino acids PubMed
- Regulatory mechanism:
- Additional information: subject to feedback inhibition PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Ana Gutiérrez-Preciado, Tina M Henkin, Frank J Grundy, Charles Yanofsky, Enrique Merino
Biochemical features and functional implications of the RNA-based T-box regulatory mechanism.
Microbiol Mol Biol Rev: 2009, 73(1);36-61
[PubMed:19258532]
[WorldCat.org]
[DOI]
(I p)
Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711]
[WorldCat.org]
[DOI]
(I p)
Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147]
[WorldCat.org]
[DOI]
(P p)
C Parsot, G N Cohen
Cloning and nucleotide sequence of the Bacillus subtilis hom gene coding for homoserine dehydrogenase. Structural and evolutionary relationships with Escherichia coli aspartokinases-homoserine dehydrogenases I and II.
J Biol Chem: 1988, 263(29);14654-60
[PubMed:3139660]
[WorldCat.org]
(P p)
