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InterPro: IPR003764 N-acetylglucosamine-6-phosphate deacetylase

Protein matches Help

UniProtKB

Matches:

1381 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR003764 GlcNAc_6-P_deAcase

Type

Family

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR00221	nagA	1381
Signatures in BioMart

InterPro Relationships Help

Contains

IPR006680 Amidohydrolase 1
IPR011059 Metal-dependent hydrolase, composite domain

GO Term annotation Help

Process

GO:0006044 N-acetylglucosamine metabolic process

Function

GO:0008448 N-acetylglucosamine-6-phosphate deacetylase activity

InterPro annotation

Entry Details in BioMart

Abstract

Three enzymes are required for N-acetylglucosamine (NAG) utilization in Escherichia coli: enzyme IInag (gene nagE), N-acetylglucosamine-6-phosphate deacetylase (gene nagA), and glucosamine-6-phosphate isomerase (gene nagB) [1]. This is family of N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 [2].

Structural links Help

PDB - click here

SCOP: b.92.1.5 , c.1.9.10

CATH: 2.30.40.10 , 3.20.20.140

Database links Help

Enzyme: EC:3.5.1.25

CluSTr: ALLvsALL:26755:53.1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR003764

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O32445 N-acetylglucosamine-6-phosphate deacetylase

P34480 Putative N-acetylglucosamine-6-phosphate deacetylase

Q8JZV7 Putative N-acetylglucosamine-6-phosphate deacetylase

Q9VR81 Putative N-acetylglucosamine-6-phosphate deacetylase

Q9Y303 Putative N-acetylglucosamine-6-phosphate deacetylase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR011059	Metal-dependent hydrolase, composite domain
IPR006680	Amidohydrolase 1
IPR003764	N-acetylglucosamine-6-phosphate deacetylase
	SWISS-MODEL
	PDB Chain
	ModBase

Publications Open in usermanual
1.	Peri KG, Goldie H, Waygood EB. Cloning and characterization of the N-acetylglucosamine operon of Escherichia coli. Biochem. Cell Biol. 68 123-37 1990 [PubMed: 2190615]
2.	Yamano N, Oura N, Wang J, Fujishima S. Cloning and sequencing of the genes for N-acetylglucosamine use that construct divergent operons (nagE-nagAC) from Vibrio cholerae non-O1. Biosci. Biotechnol. Biochem. 61 1349-53 1997 [PubMed: 9301118]

Additional Reading Open in usermanual
	Ferreira FM, Mendoza-Hernandez G, Calcagno ML, Minauro F, Delboni LF, Oliva G. Crystallization and preliminary crystallographic analysis of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 56 2000 670-2 [PubMed: 10771446] http://dx.doi.org/10.1107/S0907444900003668
	Hall RS, Brown S, Fedorov AA, Fedorov EV, Xu C, Babbitt PC, Almo SC, Raushel FM. Structural diversity within the mononuclear and binuclear active sites of N-acetyl-D-glucosamine-6-phosphate deacetylase. Biochemistry 46 2007 7953-62 [PubMed: 17567048] http://dx.doi.org/10.1021/bi700544c
	Ferreira FM, Mendoza-Hernandez G, Castaneda-Bueno M, Aparicio R, Fischer H, Calcagno ML, Oliva G. Structural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli. J. Mol. Biol. 359 2006 308-21 [PubMed: 16630633] http://dx.doi.org/10.1016/j.jmb.2006.03.024
	Vincent F, Yates D, Garman E, Davies GJ, Brannigan JA. The three-dimensional structure of the N-acetylglucosamine-6-phosphate deacetylase, NagA, from Bacillus subtilis: a member of the urease superfamily. J. Biol. Chem. 279 2004 2809-16 [PubMed: 14557261] http://dx.doi.org/10.1074/jbc.M310165200

InterPro 23.1