EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR006148 Glucosamine/galactosamine-6-phosphate isomerase

Protein matches Help

UniProtKB

Matches:

1816 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

IPR006148 Glc/Gal-6P_isomerase

Secondary

IPR000457

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01182	Glucosamine_iso	1816
Signatures in BioMart

InterPro Relationships Help

Children

IPR004547 Glucosamine-6-phosphate isomerase

Found in

IPR005900 6-phosphogluconolactonase

Contains

IPR018321 Glucosamine-6-phosphate isomerase, conserved site

GO Term annotation Help

Process

GO:0005975 carbohydrate metabolic process

InterPro annotation

Entry Details in BioMart

Abstract

This entry contains 6-phosphogluconolactonase (EC:3.1.1.31), Glucosamine-6-phosphate isomerase (EC:3.5.99.6), and Galactosamine-6-phosphate isomerase. 6-phosphogluconolactonase is the enzyme responsible for the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate, the second step in the pentose phosphate pathway. Glucosamine-6-phosphate isomerase (or Glucosamine 6-phosphate deaminase) is the enzyme responsible for the conversion of D-glucosamine 6-phosphate into D-fructose 6-phosphate [1]. It is the last specific step in the pathway for N-acetylglucosamine (GlcNAC) utilization in bacteria such as Escherichia coli (gene nagB) or in fungi such as Candida albicans (gene NAG1). A region located in the central part of Glucosamine-6-phosphate isomerase contains a conserved histidine which has been shown [1], in nagB, to be important for the pyranose ring-opening step of the catalytic mechanism.

Structural links Help

PDB - click here

SCOP: c.124.1.1

CATH: 3.40.50.1360

Database links Help

Enzyme: EC:3.5.99.6

PANDIT: PF01182

Pfam Clan: CL0246.4

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006148

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O18229 Putative 6-phosphogluconolactonase

O88958 Glucosamine-6-phosphate isomerase 1

P37262 6-phosphogluconolactonase-like protein 2

P46926 Glucosamine-6-phosphate isomerase 1

Q9VMP9 Glucosamine-6-phosphate isomerase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR018321	Glucosamine-6-phosphate isomerase, conserved site
IPR004547	Glucosamine-6-phosphate isomerase
IPR018322	Glucosamine-6-phosphate isomerase, subgroup
IPR006148	Glucosamine/galactosamine-6-phosphate isomerase
IPR005900	6-phosphogluconolactonase
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Oliva G, Fontes MR, Garratt RC, Altamirano MM, Calcagno ML, Horjales E. Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution. Structure 3 1323-32 1995 [PubMed: 8747459] http://dx.doi.org/10.1016/S0969-2126(01)00270-2

Additional Reading Open in usermanual
	Arreola R, Valderrama B, Morante ML, Horjales E. Two mammalian glucosamine-6-phosphate deaminases: a structural and genetic study. FEBS Lett. 551 2003 63-70 [PubMed: 12965206] http://dx.doi.org/10.1016/S0014-5793(03)00896-2
	Horjales E, Altamirano MM, Calcagno ML, Garratt RC, Oliva G. The allosteric transition of glucosamine-6-phosphate deaminase: the structure of the T state at 2.3 A resolution. Structure 7 1999 527-37 [PubMed: 10378272] http://dx.doi.org/10.1016/S0969-2126(99)80069-0
	Rudino-Pinera E, Morales-Arrieta S, Rojas-Trejo SP, Horjales E. Structural flexibility, an essential component of the allosteric activation in Escherichia coli glucosamine-6-phosphate deaminase. Acta Crystallogr. D Biol. Crystallogr. 58 2002 10-20 [PubMed: 11752775]
	Bustos-Jaimes I, Sosa-Peinado A, Rudino-Pinera E, Horjales E, Calcagno ML. On the role of the conformational flexibility of the active-site lid on the allosteric kinetics of glucosamine-6-phosphate deaminase. J. Mol. Biol. 319 2002 183-9 [PubMed: 12051945] http://dx.doi.org/10.1016/S0022-2836(02)00096-7

InterPro 23.1