NasB
Revision as of 12:57, 2 April 2014 by 134.76.38.147 (talk)
- Description: nitrate reductase (electron transfer subunit)
Gene name | nasB |
Synonyms | nasBA |
Essential | no |
Product | nitrate reductase (electron transfer subunit) |
Function | utilization of nitrate |
Gene expression levels in SubtiExpress: nasB | |
Interactions involving this protein in SubtInteract: NasB | |
Metabolic function and regulation of this protein in SubtiPathways: nasB | |
MW, pI | 84 kDa, 5.483 |
Gene length, protein length | 2310 bp, 770 aa |
Immediate neighbours | nasC, nasA |
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
utilization of nitrogen sources other than amino acids
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU03320
Phenotypes of a mutant
Database entries
- BsubCyc: BSU03320
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s): NasD
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
Database entries
- BsubCyc: BSU03320
- Structure:
- UniProt: P42433
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Additional information:
Biological materials
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Víctor M Luque-Almagro, Andrew J Gates, Conrado Moreno-Vivián, Stuart J Ferguson, David J Richardson, M Dolores Roldán
Bacterial nitrate assimilation: gene distribution and regulation.
Biochem Soc Trans: 2011, 39(6);1838-43
[PubMed:22103536]
[WorldCat.org]
[DOI]
(I p)
D J Richardson, B C Berks, D A Russell, S Spiro, C J Taylor
Functional, biochemical and genetic diversity of prokaryotic nitrate reductases.
Cell Mol Life Sci: 2001, 58(2);165-78
[PubMed:11289299]
[WorldCat.org]
[DOI]
(P p)
Original publications