GabD

• Description: succinate-semialdehyde dehydrogenase (NADP), general stress protein
  
  

Gene name	gabD
Synonyms	ycnH
Essential	no
Product	succinate-semialdehyde dehydrogenase (NADP)
Function	utilization of gamma-amino butyric acid
Gene expression levels in SubtiExpress: gabD
MW, pI	50 kDa, 4.763
Gene length, protein length	1386 bp, 462 aa
Immediate neighbours	gabT, glcU
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

utilization of amino acids, general stress proteins (controlled by SigB)

This gene is a member of the following regulons

GabR regulon, SigB regulon

The gene

Basic information

• Locus tag: BSU03910

Phenotypes of a mutant

• • growth defect in the presence of gamma-aminobutyrate PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s): YfmT, AldY, YcbD, GbsA, DhaS, IolA, PutC, RocA, AldX, YwdH

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure: 3RHH (from from Bacillus halodurans C-125 complexed with NADP, 327identity, 68% similarity)

• UniProt: P94428

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:
  • gabT-gabD PubMed
  • gabD PubMed

• Expression browser: gabD PubMed

• Sigma factor:
  • gabT: SigA PubMed
  • gabD: SigB PubMed

• Regulation:
  • gabT: expressed in the presence of gamma-butyric acid and pyridoxal 5'-phosphate (GabR) PubMed
  • gabD: induced by stress (SigB) PubMed

• Regulatory mechanism:
  • GabR: transcription activation PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

Linc Sonenshein, Tufts University, Boston, MA, USA Homepage

References

<pubmed>15223311,12123465,,11544224 15805528, </pubmed>