RocA

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  • Description: 3-hydroxy-1-pyrroline-5-carboxylate dehydrogenase

Gene name rocA
Synonyms ipa-76d
Essential no
Product 3-hydroxy-1-pyrroline-5-carboxylate dehydrogenase
Function arginine, ornithine and citrulline utilization
Gene expression levels in SubtiExpress: rocA
Metabolic function and regulation of this protein in SubtiPathways:
rocA
MW, pI 56 kDa, 5.58
Gene length, protein length 1545 bp, 515 aa
Immediate neighbours rocB, rocG
Sequences Protein DNA DNA_with_flanks
Genetic context
RocA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RocA expression.png















Categories containing this gene/protein

utilization of amino acids, phosphoproteins

This gene is a member of the following regulons

AbrB regulon, AhrC regulon, CodY regulon, RocR regulon, SigL regulon

The gene

Basic information

  • Locus tag: BSU37780

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: (S)-1-pyrroline-5-carboxylate + NAD(P)+ + 2 H2O = L-glutamate + NAD(P)H (according to Swiss-Prot)
  • Protein family: RocA subfamily (according to Swiss-Prot)

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylation on (Thr-2 OR Thr-4 OR Tyr-5) PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 3RJL (1-pyrroline-5-carboxylate dehydrogenase from Bacillus licheniformis, 68% identity, 88% similarity)
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • induction by arginine (RocR, AhrC) PubMed
    • repressed during growth in the presence of branched chain amino acids (CodY) PubMed
  • 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

Onuma Chumsakul, Hiroki Takahashi, Taku Oshima, Takahiro Hishimoto, Shigehiko Kanaya, Naotake Ogasawara, Shu Ishikawa
Genome-wide binding profiles of the Bacillus subtilis transition state regulator AbrB and its homolog Abh reveals their interactive role in transcriptional regulation.
Nucleic Acids Res: 2011, 39(2);414-28
[PubMed:20817675] [WorldCat.org] [DOI] (I p)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

Virginie Molle, Yoshiko Nakaura, Robert P Shivers, Hirotake Yamaguchi, Richard Losick, Yasutaro Fujita, Abraham L Sonenshein
Additional targets of the Bacillus subtilis global regulator CodY identified by chromatin immunoprecipitation and genome-wide transcript analysis.
J Bacteriol: 2003, 185(6);1911-22
[PubMed:12618455] [WorldCat.org] [DOI] (P p)

U Klingel, C M Miller, A K North, P G Stockley, S Baumberg
A binding site for activation by the Bacillus subtilis AhrC protein, a repressor/activator of arginine metabolism.
Mol Gen Genet: 1995, 248(3);329-40
[PubMed:7565595] [WorldCat.org] [DOI] (P p)

S Calogero, R Gardan, P Glaser, J Schweizer, G Rapoport, M Debarbouille
RocR, a novel regulatory protein controlling arginine utilization in Bacillus subtilis, belongs to the NtrC/NifA family of transcriptional activators.
J Bacteriol: 1994, 176(5);1234-41
[PubMed:8113162] [WorldCat.org] [DOI] (P p)