nagB

nagB
168

glucosamine-6-phosphate deaminase

Locus
BSU_35020
Molecular weight
26.84 kDa
Isoelectric point
5.72
Protein length
242 aaSequenceBlast
Gene length
729 bpSequenceBlast
Function
N-acetylglucosamine utilization
Product
glucosamine-6-phosphate deaminase
Essential
no
Synonyms
nagB
Outlinks
BsubCyc SubtiList UniProt STRING Genoscapist PaperBLAST

Genomic Context

Categories containing this gene/protein

List of homologs in different organisms, belongs to COG0363 (Galperin et al., 2021)

This gene is a member of the following regulons

Gene
Coordinates
3,596,543  3,597,271
The protein
Catalyzed reaction/ biological activity
α-D-glucosamine 6-phosphate + H2O --> β-D-fructose 6-phosphate + NH4+ (according to UniProt)
Protein family
glucosamine/galactosamine-6-phosphate isomerase family (with GamA, according to UniProt)
Structure
2BKX (PDB) PubMed
O35000 (AlphaFold)
Paralogous protein(s)
GamA
Expression and Regulation
Operons
Genes
nagA-nagB-nagR
Description
PubMed
Regulation
induced in the presence of N-acetylglucosamine (NagR) PubMed
Regulatory mechanism
NagR: repression, PubMed, in nagR regulon
CcpA: repression, PubMed, in ccpA regulon
Sigma factors
SigA: sigma factor, PubMed, in sigA regulon
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nagA→nagR

2025-04-04 08:11:11

ghost

118

dfb9f60c6cb4712882f6e111396691335972d607

2CE10C0E65E696F5F9B1AAC17ED9D19E163A6ECF

Biological materials
Mutant
MGNA-A336 (nagB::erm), available at the NBRP B. subtilis, Japan
BKE35020 (nagB::erm  trpC2) available at BGSC,  PubMed, upstream reverse: _UP1_ATACGTTTGACATTCCATTA,  downstream forward: _UP4_CCTTGAAAGGAACATGCTGA
BKK35020 (nagB::kan  trpC2) available at BGSC,  PubMed, upstream reverse: _UP1_ATACGTTTGACATTCCATTA,  downstream forward: _UP4_CCTTGAAAGGAACATGCTGA
References
Reviews
Gilmore MC, Cava FBacterial peptidoglycan recycling.Trends in microbiology. 2024 Nov 28; . PMID: 39613687
Plumbridge J Regulation of the Utilization of Amino Sugars by Escherichia coli and Bacillus subtilis: Same Genes, Different Control. Journal of molecular microbiology and biotechnology. 2015; 25(2-3):154-67. doi:10.1159/000369583. PMID:26159076
Original Publications
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Page visits: 2960

Time of last update: 2025-04-05 18:36:53

Author of last update: Jstuelk