Difference between revisions of "ArgG"
(→Expression and regulation) |
|||
Line 50: | Line 50: | ||
+ | |||
+ | = Categories containing this gene/protein = | ||
+ | {{SubtiWiki category|[[biosynthesis/ acquisition of amino acids]]}} | ||
=The protein= | =The protein= | ||
Revision as of 14:58, 30 November 2010
- Description: argininosuccinate synthase, reversible
Gene name | argG |
Synonyms | |
Essential | no |
Product | argininosuccinate synthase, reversible |
Function | biosynthesis of arginine |
Metabolic function and regulation of this protein in SubtiPathways: Ammonium/ glutamate | |
MW, pI | 44 kDa, 5.028 |
Gene length, protein length | 1209 bp, 403 aa |
Immediate neighbours | argH, moaB |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU29450
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
Categories containing this gene/protein
biosynthesis/ acquisition of amino acids
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate (according to Swiss-Prot)
- Protein family: Type 1 subfamily (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification: S-cysteinylation after diamide stress (C187) PubMed
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- UniProt: O34347
- KEGG entry: [2]
- E.C. number: 6.3.4.5
Additional information
Expression and regulation
- Regulatory mechanism:
- AhrC: transcription repression
- 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
Falko Hochgräfe, Jörg Mostertz, Dierk-Christoph Pöther, Dörte Becher, John D Helmann, Michael Hecker
S-cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress.
J Biol Chem: 2007, 282(36);25981-5
[PubMed:17611193]
[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)