PyrB
Revision as of 09:11, 19 April 2012 by 134.76.70.252 (talk)
- Description: aspartate carbamoyltransferase
Gene name | pyrB |
Synonyms | |
Essential | no |
Product | aspartate carbamoyltransferase |
Function | pyrimidine biosynthesis |
Metabolic function and regulation of this protein in SubtiPathways: Pyrimidines, Nucleotides (regulation) | |
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
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
biosynthesis/ acquisition of nucleotides, phosphoproteins
This gene is a member of the following regulons
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:
Database entries
- UniProt: 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
- Regulatory mechanism:
- PyrR: RNA switch, transcription termination/ antitermination (in the presence of uridine nucleotides: termination, in their absence: antitermination) PubMed
- 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