Hom

• 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: hom
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

Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, membrane proteins, most abundant proteins

This gene is a member of the following regulons

CodY regulon

The gene

Basic information

• Locus tag: BSU32260

Database entries

• BsubCyc: BSU32260

• DBTBS entry: no entry

• SubtiList entry: [1]

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:

• Cofactors:

• Effectors of protein activity: subject to feedback inhibition PubMed

• Interactions:

• Localization:
  • membrane associated PubMed

Database entries

• BsubCyc: BSU32260

• Structure: 2EJW (from Thermus thermophilus hb8, 37% identity, 57% similarity)

• UniProt: P19582

• KEGG entry: [2]

• E.C. number: 1.1.1.3

Expression and regulation

• Operon: hom-thrC-thrB PubMed

• Expression browser: hom PubMed

• Sigma factor:

• Regulation:
  • repressed by casamino acids PubMed
  • repressed during growth in the presence of branched chain amino acids (CodY) PubMed

• Regulatory mechanism:
  • CodY: transcription repression PubMed

• Additional information:
  • subject to feedback inhibition PubMed
  • belongs to the 100 most abundant proteins PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 2167 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 1723 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 3436 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 2047 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 3239 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody: