Difference between revisions of "ArgB"
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|style="background:#ABCDEF;" align="center"|'''Function''' || biosynthesis of arginine | |style="background:#ABCDEF;" align="center"|'''Function''' || biosynthesis of arginine | ||
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− | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http:// | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU11210 argB] |
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/glutamate.html Ammonium/ glutamate]''' | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/glutamate.html Ammonium/ glutamate]''' | ||
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[argJ]]'', ''[[argD]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[argJ]]'', ''[[argD]]'' | ||
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− | | | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU11210 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU11210 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU11210 Advanced_DNA] |
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|colspan="2" | '''Genetic context''' <br/> [[Image:argB_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:argB_context.gif]] |
Revision as of 12:31, 13 May 2013
- Description: N-acetylglutamate 5-phosphotransferase
Gene name | argB |
Synonyms | |
Essential | no |
Product | N-acetylglutamate 5-phosphotransferase |
Function | biosynthesis of arginine |
Gene expression levels in SubtiExpress: argB | |
Metabolic function and regulation of this protein in SubtiPathways: Ammonium/ glutamate | |
MW, pI | 27 kDa, 6.214 |
Gene length, protein length | 774 bp, 258 aa |
Immediate neighbours | argJ, argD |
Sequences | Protein DNA Advanced_DNA |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
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: BSU11210
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate (according to Swiss-Prot)
- Protein family: acetylglutamate kinase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: P68729
- KEGG entry: [3]
- E.C. number: 2.7.2.8
Additional information
- subject to Clp-dependent proteolysis upon glucose starvation PubMed
Expression and regulation
- Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed
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)
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)