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InterPro: IPR013148 Glycosyl hydrolases family 32, N-terminal

UniProtKB

Matches:

1694 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

IPR013148 Glyco_hydro_32_N

IPR001362

Type

Domain

Signatures Help

Found in

IPR001362 Glycoside hydrolase, family 32
IPR006232 Sucrose-6-phosphate hydrolase

Contains

IPR018053 Glycoside hydrolase, family 32, active site

InterPro annotation

This domain corresponds to the N-terminal domain of glycosyl transferase family 32 which forms a five bladed beta propeller structure [1].

SCOP: b.67.2.3

Enzyme: EC:3.2.1.26

Blocks: IPB013148

IPR013148

Numbers of overlapping proteins

Average numbers of overlapping amino acids

A2X5P7 Beta-fructofuranosidase, insoluble isoenzyme 1

O33833 Beta-fructosidase

O42878 Putative invertase

P00724 Invertase 2

Q43866 Beta-fructofuranosidase, insoluble isoenzyme CWINV1

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.	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 18903-10 2004 [PubMed: 14973124] http://dx.doi.org/10.1074/jbc.M313911200

Additional Reading Open in usermanual
	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