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InterPro: IPR002594 Glycoside hydrolase, family 12

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213 proteins

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Accession

IPR002594 Glyco_hydro_12

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01670	Glyco_hydro_12	213
Signatures in BioMart

InterPro Relationships Help

Contains

IPR013319 Glycoside hydrolase, family 11/12, catalytic domain

GO Term annotation Help

Process

GO:0000272 polysaccharide catabolic process

Function

GO:0008810 cellulase activity

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 12 GH12 comprises enzymes with two known activities: endoglucanase (EC:3.2.1.4)and xyloglucan hydrolase (EC not defined). These enzymes were formerly known as cellulase family H.

Structural links Help

PDB - click here

SCOP: b.29.1.11

CATH: 2.60.120.180

Database links Help

Enzyme: EC:3.2.1.4

CAZy: GH12

PANDIT: PF01670

Blocks: IPB002594

Pfam Clan: CL0004.16

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR002594

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P16630 Endoglucanase S

P22669 Endoglucanase-1

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013319	Glycoside hydrolase, family 11/12, catalytic domain
IPR002594	Glycoside hydrolase, family 12
IPR008985	Concanavalin A-like lectin/glucanase
	SWISS-MODEL
	ModBase

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
	Khademi S, Zhang D, Swanson SM, Wartenberg A, Witte K, Meyer EF. Determination of the structure of an endoglucanase from Aspergillus niger and its mode of inhibition by palladium chloride. Acta Crystallogr. D Biol. Crystallogr. 58 2002 660-7 [PubMed: 11914491] http://dx.doi.org/10.1107/S0907444902003360
	Sulzenbacher G, Shareck F, Morosoli R, Dupont C, Davies GJ. The Streptomyces lividans family 12 endoglucanase: construction of the catalytic cre, expression, and X-ray structure at 1.75 A resolution. Biochemistry 36 1997 16032-9 [PubMed: 9440876] http://dx.doi.org/10.1021/bi972407v
	Crennell SJ, Cook D, Minns A, Svergun D, Andersen RL, Nordberg Karlsson E. Dimerisation and an increase in active site aromatic groups as adaptations to high temperatures: X-ray solution scattering and substrate-bound crystal structures of Rhodothermus marinus endoglucanase Cel12A. J. Mol. Biol. 356 2006 57-71 [PubMed: 16343530] http://dx.doi.org/10.1016/j.jmb.2005.11.004
	Sandgren M, Berglund GI, Shaw A, Stahlberg J, Kenne L, Desmet T, Mitchinson C. Crystal complex structures reveal how substrate is bound in the -4 to the +2 binding sites of Humicola grisea Cel12A. J. Mol. Biol. 342 2004 1505-17 [PubMed: 15364577] http://dx.doi.org/10.1016/j.jmb.2004.07.098
	Sandgren M, Gualfetti PJ, Shaw A, Gross LS, Saldajeno M, Day AG, Jones TA, Mitchinson C. Comparison of family 12 glycoside hydrolases and recruited substitutions important for thermal stability. Protein Sci. 12 2003 848-60 [PubMed: 12649442] http://dx.doi.org/10.1110/ps.0237703
	Sandgren M, Gualfetti PJ, Paech C, Paech S, Shaw A, Gross LS, Saldajeno M, Berglund GI, Jones TA, Mitchinson C. The Humicola grisea Cel12A enzyme structure at 1.2 A resolution and the impact of its free cysteine residues on thermal stability. Protein Sci. 12 2003 2782-93 [PubMed: 14627738] http://dx.doi.org/10.1110/ps.03220403

InterPro 23.1