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

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Allison Kriel, Shaun R Brinsmade, Jessica L Tse, Ashley K Tehranchi, Alycia N Bittner, Abraham L Sonenshein, Jue D Wang
GTP dysregulation in Bacillus subtilis cells lacking (p)ppGpp results in phenotypic amino acid auxotrophy and failure to adapt to nutrient downshift and regulate biosynthesis genes.
J Bacteriol: 2014, 196(1);189-201
[PubMed:24163341] [WorldCat.org] [DOI] (I p)

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)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [WorldCat.org] [DOI] (P 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)