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InterPro: IPR018053 Glycoside hydrolase, family 32, active site

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864 proteins

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Accession

IPR018053 Glyco_hydro_32_AS

Type

Active_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00609	GLYCOSYL_HYDROL_F32	864
Signatures in BioMart

InterPro Relationships Help

Found in

IPR001362 Glycoside hydrolase, family 32
IPR006232 Sucrose-6-phosphate hydrolase
IPR013148 Glycosyl hydrolases family 32, N-terminal

GO Term annotation Help

Process

GO:0005975 carbohydrate metabolic process

Function

GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds

InterPro annotation

Entry Details in BioMart

Abstract

It has been shown [1, 2] that the following glycosyl hydrolases can be classified into a single family on the basis of sequence similarities:

Inulinase (EC:3.2.1.7) (or inulase) from the fungi Kluyveromyces marxianus (Yeast) (Candida kefyr).
Beta-fructofuranosidase (EC:3.2.1.26), commonly known as invertase in fungi and plants and as sucrase in bacteria (gene sacA or scrB).
Raffinose invertase (EC:3.2.1.26) (gene rafD) from Escherichia coli raffinose plasmid pRSD2.
Levanase (EC:3.2.1.65) (gene sacC) from Bacillus subtilis.

One of the conserved regions in these enzymes is located in the N-terminal section and contains an aspartic acid residue which has been shown, in yeast invertase to be important for the catalytic mechanism [3].

Structural links Help

PDB - click here

SCOP: b.67.2.3

Database links Help

Enzyme: EC:3.2.1.26

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR018053

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A2X5P7 Beta-fructofuranosidase, insoluble isoenzyme 1

O33833 Beta-fructosidase

O42878 Putative invertase

P00724 Invertase 2

Q43866 Beta-fructofuranosidase, insoluble isoenzyme CWINV1

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013148	Glycosyl hydrolases family 32, N-terminal
IPR018053	Glycoside hydrolase, family 32, active site
IPR001362	Glycoside hydrolase, family 32
IPR013189	Glycosyl hydrolase family 32, C-terminal
IPR008985	Concanavalin A-like lectin/glucanase
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain

Publications Open in usermanual
1.	Henrissat B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280 ( Pt 2) 309-16 1991 [PubMed: 1747104] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=1747104
2.	Gunasekaran P, Karunakaran T, Cami B, Mukundan AG, Preziosi L, Baratti J. Cloning and sequencing of the sacA gene: characterization of a sucrase from Zymomonas mobilis. J. Bacteriol. 172 6727-35 1990 [PubMed: 2254250] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=2254250&action=stream&blobtype=pdf
3.	Reddy VA, Maley F. Identification of an active-site residue in yeast invertase by affinity labeling and site-directed mutagenesis. J. Biol. Chem. 265 10817-20 1990 [PubMed: 2113524] http://intl.jbc.org/cgi/content/abstract/265/19/10817

Additional Reading Open in usermanual
	Alberto F, Bignon C, Sulzenbacher G, Henrissat B, Czjzek M. The three-dimensional structure of invertase (beta-fructosidase) from Thermotoga maritima reveals a bimodular arrangement and an evolutionary relationship between retaining and inverting glycosidases. J. Biol. Chem. 279 2004 18903-10 [PubMed: 14973124] http://dx.doi.org/10.1074/jbc.M313911200
	Nagem RA, Rojas AL, Golubev AM, Korneeva OS, Eneyskaya EV, Kulminskaya AA, Neustroev KN, Polikarpov I. Crystal structure of exo-inulinase from Aspergillus awamori: the enzyme fold and structural determinants of substrate recognition. J. Mol. Biol. 344 2004 471-80 [PubMed: 15522299] http://dx.doi.org/10.1016/j.jmb.2004.09.024
	Arand M, Golubev AM, Neto JR, Polikarpov I, Wattiez R, Korneeva OS, Eneyskaya EV, Kulminskaya AA, Shabalin KA, Shishliannikov SM, Chepurnaya OV, Neustroev KN. Purification, characterization, gene cloning and preliminary X-ray data of the exo-inulinase from Aspergillus awamori. Biochem. J. 362 2002 131-5 [PubMed: 11829749] http://dx.doi.org/10.1042/0264-6021:3620131
	Alberto F, Jordi E, Henrissat B, Czjzek M. Crystal structure of inactivated Thermotoga maritima invertase in complex with the trisaccharide substrate raffinose. Biochem. J. 395 2006 457-62 [PubMed: 16411890] http://dx.doi.org/10.1042/BJ20051936

InterPro 23.1