homoserine dehydrogenase (NADPH)
function
biosynthesis of methionine and threonine
product
homoserine dehydrogenase (NADPH)
Genomic Context
categories
[category|SW 2|Metabolism] → [category|SW 2.3|Amino acid/ nitrogen metabolism] → [category|SW 2.3.1|Biosynthesis/ acquisition of amino acids] → [category|SW 2.3.1.10|Biosynthesis/ acquisition of methionine/ S-adenosylmethionine][category|SW 2|Metabolism] → [category|SW 2.3|Amino acid/ nitrogen metabolism] → [category|SW 2.3.1|Biosynthesis/ acquisition of amino acids] → [category|SW 2.3.1.6|Biosynthesis/ acquisition of lysine/ threonine][SW|Categories] containing this gene/protein
[SW|biosynthesis/ acquisition of amino acids], [SW|membrane proteins], [SW|most abundant proteins]This gene is a member of the following [SW|regulons]
[SW|CodY regulon], [SW|TnrA regulon], [SW|ThrR regulon]Gene
Coordinates on the chromosome (coding sequence)
3,314,828 -> 3,316,129
The protein
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)Effectors of protein activity
subject to feedback inhibition [Pubmed|19258532]Structure
[PDB|2EJW] (from ''Thermus thermophilus hb8'', 37% identity, 57% similarity)[SW|Localization]
membrane associated [Pubmed|18763711]Expression and Regulation
Operon
''[protein|search|hom]-[protein|search|thrC]-[protein|search|thrB]'' [Pubmed|12107147]Regulation
repressed by casamino acids [Pubmed|12107147]repressed during growth in the presence of branched chain amino acids ([protein|search|CodY]) [Pubmed|24163341]expressed in the presence of lysine or cysteine ([SW|ThrR]) [Pubmed|27260660]Regulatory mechanism
[protein|search|CodY]: transcription repression [Pubmed|24163341][protein|search|TnrA]: transcription repression [Pubmed|25755103][protein|search|ThrR]: transcription repression [Pubmed|27260660]Additional information
subject to feedback inhibition [http://www.ncbi.nlm.nih.gov/sites/entrez/19258532 PubMed]belongs to the 100 [SW|most abundant proteins] [PubMed|15378759]Biological materials
lacZ fusion
pGP312 (in [protein|search|pAC5]), available in [SW|Fabian Commichau]'s lab [Pubmed|27260660]References
12107147,18763711,3139660,19258532,24163341,25777134,15378759,25755103,27260660 
