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InterPro: IPR001362 Glycoside hydrolase, family 32

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UniProtKB

Matches:

1528 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

IPR001362 Glyco_hydro_32

Type

Family

Signatures Help

Database	ID	Name	Proteins
SMART	SM00640	Glyco_32	1528
Signatures in BioMart

InterPro Relationships Help

Children

IPR006232 Sucrose-6-phosphate hydrolase

Contains

IPR013148 Glycosyl hydrolases family 32, N-terminal
IPR013189 Glycosyl hydrolase family 32, C-terminal
IPR018053 Glycoside hydrolase, family 32, active site

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

O-Glycosyl hydrolases EC:3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [1, 2, 3]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site [4]. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in clans.

Glycoside hydrolase family 32 GH32 comprises enzymes with several known activities; invertase (EC:3.2.1.26); inulinase (EC:3.2.1.7); levanase (EC:3.2.1.65); exo-inulinase (EC:3.2.1.80); sucrose:sucrose 1-fructosyltransferase (EC:2.4.1.99); fructan:fructan 1-fructosyltransferase (EC:2.4.1.100).

Structural links Help

PDB - click here

SCOP: b.29.1.19 , b.67.2.3

CATH: 2.60.120.560

Database links Help

PDBe-motif: PS00609

Enzyme: EC:3.2.1.26

CAZy: GH32

PROSITE doc: PDOC00532

Blocks: IPB001362

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001362

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, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. U.S.A. 92 7090-4 1995 [PubMed: 7624375] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=7624375&action=stream&blobtype=pdf
2.	Davies G, Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 3 853-9 1995 [PubMed: 8535779] http://dx.doi.org/10.1016/S0969-2126(01)00220-9
3.	Bairoch A. Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT. 1999
4.	Henrissat B, Coutinho PM. Carbohydrate-Active Enzymes server. 1999

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