Difference between revisions of "ArgC"
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+ | = [[Categories]] containing this gene/protein = | ||
+ | {{SubtiWiki category|[[biosynthesis/ acquisition of amino acids]]}} | ||
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+ | = This gene is a member of the following [[regulons]] = | ||
+ | {{SubtiWiki regulon|[[AhrC regulon]]}} | ||
=The gene= | =The gene= | ||
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=The protein= | =The protein= | ||
Revision as of 18:24, 8 December 2010
- Description: N-acetyl-g-glutamyl-phosphate reductase
Gene name | argC |
Synonyms | |
Essential | no |
Product | N-acetyl-g-glutamyl-phosphate reductase |
Function | biosynthesis of arginine |
Metabolic function and regulation of this protein in SubtiPathways: Ammonium/ glutamate | |
MW, pI | 37 kDa, 5.167 |
Gene length, protein length | 1038 bp, 346 aa |
Immediate neighbours | yitZ, argJ |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
biosynthesis/ acquisition of amino acids
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU11190
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate = N-acetyl-5-glutamyl phosphate + NADPH (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:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: P23715
- KEGG entry: [3]
- E.C. number: 1.2.1.38
Additional information
Expression and regulation
- 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
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)
M O'Reilly, K Woodson, B C Dowds, K M Devine
The citrulline biosynthetic operon, argC-F, and a ribose transport operon, rbs, from Bacillus subtilis are negatively regulated by Spo0A.
Mol Microbiol: 1994, 11(1);87-98
[PubMed:7511775]
[WorldCat.org]
[DOI]
(P p)
M C Smith, A Mountain, S Baumberg
Nucleotide sequence of the Bacillus subtilis argC gene encoding N-acetylglutamate-gamma-semialdehyde dehydrogenase.
Nucleic Acids Res: 1990, 18(15);4595
[PubMed:2117746]
[WorldCat.org]
[DOI]
(P p)
A Mountain, N H Mann, R N Munton, S Baumberg
Cloning of a Bacillus subtilis restriction fragment complementing auxotrophic mutants of eight Escherichia coli genes of arginine biosynthesis.
Mol Gen Genet: 1984, 197(1);82-9
[PubMed:6096675]
[WorldCat.org]
[DOI]
(P p)