NagB
- Description: glucosamine-6-phosphate deaminase
Gene name | nagB |
Synonyms | |
Essential | no |
Product | glucosamine-6-phosphate deaminase |
Function | N-acetylglucosamine utilization |
Gene expression levels in SubtiExpress: nagB | |
Metabolic function and regulation of this protein in SubtiPathways: nagB | |
MW, pI | 26 kDa, 5.717 |
Gene length, protein length | 726 bp, 242 aa |
Immediate neighbours | nagA, nagR |
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
cell wall degradation/ turnover, utilization of specific carbon sources
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU35020
Phenotypes of a mutant
Database entries
- BsubCyc: BSU35020
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
- A mutation was found in this gene after evolution under relaxed selection for sporulation PubMed
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3 (according to Swiss-Prot)
- Protein family: NagB subfamily (according to Swiss-Prot)
- Paralogous protein(s): GamA
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
Database entries
- BsubCyc: BSU35020
- UniProt: O35000
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Simon B Fillenberg, Florian C Grau, Gerald Seidel, Yves A Muller
Structural insight into operator dre-sites recognition and effector binding in the GntR/HutC transcription regulator NagR.
Nucleic Acids Res: 2015, 43(2);1283-96
[PubMed:25564531]
[WorldCat.org]
[DOI]
(I p)
Isabelle Gaugué, Jacques Oberto, Jacqueline Plumbridge
Regulation of amino sugar utilization in Bacillus subtilis by the GntR family regulators, NagR and GamR.
Mol Microbiol: 2014, 92(1);100-15
[PubMed:24673833]
[WorldCat.org]
[DOI]
(I p)
Yanfeng Liu, Long Liu, Hyun-dong Shin, Rachel R Chen, Jianghua Li, Guocheng Du, Jian Chen
Pathway engineering of Bacillus subtilis for microbial production of N-acetylglucosamine.
Metab Eng: 2013, 19;107-15
[PubMed:23876412]
[WorldCat.org]
[DOI]
(I p)
Isabelle Gaugué, Jacques Oberto, Harald Putzer, Jacqueline Plumbridge
The use of amino sugars by Bacillus subtilis: presence of a unique operon for the catabolism of glucosamine.
PLoS One: 2013, 8(5);e63025
[PubMed:23667565]
[WorldCat.org]
[DOI]
(I e)
Christopher T Brown, Laura K Fishwick, Binna M Chokshi, Marissa A Cuff, Jay M Jackson, Travis Oglesby, Alison T Rioux, Enrique Rodriguez, Gregory S Stupp, Austin H Trupp, James S Woollcombe-Clarke, Tracy N Wright, William J Zaragoza, Jennifer C Drew, Eric W Triplett, Wayne L Nicholson
Whole-genome sequencing and phenotypic analysis of Bacillus subtilis mutants following evolution under conditions of relaxed selection for sporulation.
Appl Environ Microbiol: 2011, 77(19);6867-77
[PubMed:21821766]
[WorldCat.org]
[DOI]
(I p)
Ralph Bertram, Sébastien Rigali, Natalie Wood, Andrzej T Lulko, Oscar P Kuipers, Fritz Titgemeyer
Regulon of the N-acetylglucosamine utilization regulator NagR in Bacillus subtilis.
J Bacteriol: 2011, 193(14);3525-36
[PubMed:21602348]
[WorldCat.org]
[DOI]
(I p)
Florence Vincent, Gideon J Davies, James A Brannigan
Structure and kinetics of a monomeric glucosamine 6-phosphate deaminase: missing link of the NagB superfamily?
J Biol Chem: 2005, 280(20);19649-55
[PubMed:15755726]
[WorldCat.org]
[DOI]
(P p)
H L Mobley, R J Doyle, U N Streips, S O Langemeier
Transport and incorporation of N-acetyl-D-glucosamine in Bacillus subtilis.
J Bacteriol: 1982, 150(1);8-15
[PubMed:6174502]
[WorldCat.org]
[DOI]
(P p)