OxdC
- Description: oxalate decarboxylase
Gene name | oxdC |
Synonyms | yvrK |
Essential | no |
Product | oxalate decarboxylase |
Function | unknown |
Gene expression levels in SubtiExpress: oxdC | |
MW, pI | 43 kDa, 5.101 |
Gene length, protein length | 1155 bp, 385 aa |
Immediate neighbours | yvrJ, yvrL |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
acid stress proteins (controlled by YvrI-YvrHa), phosphoproteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU33240
Phenotypes of a mutant
Database entries
- BsubCyc: BSU33240
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Oxalate = formate + CO2 (according to Swiss-Prot)
- Protein family:
- Paralogous protein(s): OxdD
Extended information on the protein
- Kinetic information:
- Modification:
- phosphorylated on Arg-12 PubMed
- Effectors of protein activity:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- BsubCyc: BSU33240
- Structure: 1UW8
- UniProt: O34714
- KEGG entry: [2]
- E.C. number: 4.1.1.2
Additional information
Expression and regulation
- Regulation: induced by acidic growth conditions PubMed
- Regulatory mechanism:
- Additional information:
- number of protein molecules per cell (minimal medium with glucose and ammonium): 193 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 4306 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 2602 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 4926 PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
John Helmann, Cornell University, USA Homepage
Your additional remarks
References
Reviews
Original publications