Difference between revisions of "ThrB"
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+ | = [[Categories]] containing this gene/protein = | ||
+ | {{SubtiWiki category|[[biosynthesis/ acquisition of amino acids]]}} | ||
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+ | = This gene is a member of the following [[regulons]] = | ||
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=The gene= | =The gene= | ||
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=The protein= | =The protein= | ||
Revision as of 23:04, 8 December 2010
- Description: homoserine kinase
Gene name | thrB |
Synonyms | thrA |
Essential | no |
Product | homoserine kinase |
Function | biosynthesis of threonine |
Metabolic function and regulation of this protein in SubtiPathways: Lys, Thr | |
MW, pI | 33 kDa, 4.735 |
Gene length, protein length | 927 bp, 309 aa |
Immediate neighbours | yuxL, thrC |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
biosynthesis/ acquisition of amino acids
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU32240
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + L-homoserine = ADP + O-phospho-L-homoserine (according to Swiss-Prot)
- Protein family: Homoserine kinase subfamily (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- Structure: 3HUL (from Listeria monocytogenes, 41% identity, 61% similarity)
- UniProt: P04948
- KEGG entry: [2]
- E.C. number: 2.7.1.39
Additional information
Expression and regulation
- 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
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
Evolution of biosynthetic pathways: a common ancestor for threonine synthase, threonine dehydratase and D-serine dehydratase.
EMBO J: 1986, 5(11);3013-9
[PubMed:3098560]
[WorldCat.org]
[DOI]
(P p)