Difference between revisions of "Sandbox"
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− | * '''Description:''' | + | * '''Description:''' homoserine dehydrogenase (NADPH) <br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
|- | |- | ||
|style="background:#ABCDEF;" align="center"|'''Gene name''' | |style="background:#ABCDEF;" align="center"|'''Gene name''' | ||
− | |'' | + | |''hom'' |
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' '' | |style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' '' | ||
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|style="background:#ABCDEF;" align="center"| '''Essential''' || no | |style="background:#ABCDEF;" align="center"| '''Essential''' || no | ||
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''Product''' || | + | |style="background:#ABCDEF;" align="center"| '''Product''' || homoserine dehydrogenase (NADPH) |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"|'''Function''' || | + | |style="background:#ABCDEF;" align="center"|'''Function''' || biosynthesis of methionine and threonine |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || | + | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 47 kDa, 4.9 |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || | + | |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1299 bp, 433 aa |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ | + | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[thrC]]'', ''[[yutH]]'' |
|- | |- | ||
|colspan="2" style="background:#FAF8CC;" align="center"|'''Hier soll was neues rein''' | |colspan="2" style="background:#FAF8CC;" align="center"|'''Hier soll was neues rein''' | ||
|- | |- | ||
− | |colspan="2" | '''Genetic context''' <br/> [[Image: | + | |colspan="2" | '''Genetic context''' <br/> [[Image:hom_context.gif]] |
<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> | ||
|- | |- | ||
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* '''DBTBS entry:''' no entry | * '''DBTBS entry:''' no entry | ||
− | * '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+ | + | * '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10460] |
=== Additional information=== | === Additional information=== | ||
Line 72: | Line 72: | ||
* '''Interactions:''' | * '''Interactions:''' | ||
− | * '''Localization:''' | + | * '''Localization:''' membrane associated [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed] |
=== Database entries === | === Database entries === | ||
Line 80: | Line 80: | ||
* '''Swiss prot entry:''' | * '''Swiss prot entry:''' | ||
− | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+ | + | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU32260] |
* '''E.C. number:''' | * '''E.C. number:''' | ||
Line 92: | Line 92: | ||
* '''[[Sigma factor]]:''' | * '''[[Sigma factor]]:''' | ||
− | * '''Regulation:''' | + | * '''Regulation:''' repressed by casamino acids [http://www.ncbi.nlm.nih.gov/pubmed/12107147 PubMed] |
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
Line 118: | Line 118: | ||
=References= | =References= | ||
+ | # Mäder et al. (2002) Transcriptome and Proteome Analysis of ''Bacillus subtilis'' Gene Expression Modulated by Amino Acid Availability. ''J. Bacteriol'' '''184:''' 1844288-4295 [http://www.ncbi.nlm.nih.gov/pubmed/12107147 PubMed] | ||
+ | # Hahne et al. (2008) From complementarity to comprehensiveness - targeting the membrane proteome of growing ''Bacillus subtilis'' by divergent approaches. Proteomics '''8:''' 4123-4136 [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed] | ||
+ | # Parsot C, Cohen GN. (1988) 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.'' '''Oct 15;263(29):''' 14654-60. [http://www.ncbi.nlm.nih.gov/sites/entrez/3139660 PubMed] | ||
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed] | # Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed] |
Revision as of 17:56, 15 April 2009
- Description: homoserine dehydrogenase (NADPH)
Gene name | hom |
Synonyms | |
Essential | no |
Product | homoserine dehydrogenase (NADPH) |
Function | biosynthesis of methionine and threonine |
MW, pI | 47 kDa, 4.9 |
Gene length, protein length | 1299 bp, 433 aa |
Immediate neighbours | thrC, yutH |
Hier soll was neues rein | |
Genetic context ![]() This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Coordinates:
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: membrane associated PubMed
Database entries
- Structure:
- Swiss prot entry:
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Regulation: repressed by casamino acids PubMed
- 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
References
- Mäder et al. (2002) Transcriptome and Proteome Analysis of Bacillus subtilis Gene Expression Modulated by Amino Acid Availability. J. Bacteriol 184: 1844288-4295 PubMed
- Hahne et al. (2008) From complementarity to comprehensiveness - targeting the membrane proteome of growing Bacillus subtilis by divergent approaches. Proteomics 8: 4123-4136 PubMed
- Parsot C, Cohen GN. (1988) 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. Oct 15;263(29): 14654-60. PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed