RocA

• 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
Metabolic function and regulation of this protein in SubtiPathways: Ammonium/ glutamate
MW, pI	56 kDa, 5.58
Gene length, protein length	1545 bp, 515 aa
Immediate neighbours	rocB, rocG
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU37780

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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)

• Paralogous protein(s):

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:

• Interactions:

• Localization:

Database entries

• Structure: 2BJA (with bound NADH from Thermus thermophilus, 43% identity, 59% similarity) PubMed

• UniProt: P39634

• KEGG entry: [3]

• E.C. number: 1.5.1.12

Expression and regulation

• Operon: rocA-rocB-rocC PubMed

• Sigma factor: SigL PubMed

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

• Regulatory mechanism:
  • CodY: transcription repression PubMed
  • RocR: transcription activation PubMed
  • AhrC: transcription activation PubMed
  • AbrB: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)