Difference between revisions of "PyrB"
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=== Basic information === | === Basic information === | ||
− | * '''Locus tag:''' | + | * '''Locus tag:''' BSU15490 |
===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
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* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P05654 P05654] | * '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P05654 P05654] | ||
− | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+ | + | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU15490] |
* '''E.C. number:''' [http://www.expasy.org/enzyme/2.1.3.2 2.1.3.2] | * '''E.C. number:''' [http://www.expasy.org/enzyme/2.1.3.2 2.1.3.2] |
Revision as of 12:00, 3 June 2009
- Description: aspartate carbamoyltransferase
Gene name | pyrB |
Synonyms | |
Essential | no |
Product | aspartate carbamoyltransferase |
Function | pyrimidine biosynthesis |
MW, pI | 34 kDa, 5.341 |
Gene length, protein length | 912 bp, 304 aa |
Immediate neighbours | pyrP, pyrC |
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: BSU15490
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate (according to Swiss-Prot)
- Protein family: ATCase/OTCase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification: phosphorylation on Ser-303 PubMed
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure: 2AT2
- Swiss prot entry: P05654
- KEGG entry: [3]
- E.C. number: 2.1.3.2
Additional information
- subject to Clp-dependent proteolysis upon glucose starvation PubMed
Expression and regulation
- Operon:
- Regulation:
- Regulatory mechanism:
- 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
- Gerth et al. (2008) Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis. J Bacteriol 190:321-331 PubMed
- Macek et al. (2007) The serine/ threonine/ tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol. Cell. Proteomics 6: 697-707 PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed