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InterPro: IPR001701 Glycoside hydrolase, family 9

Protein matchesHelp
UniProtKB
Matches:
962 proteins
AccessionHelp IPR001701 Glyco_hydro_9
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR012341 Six-hairpin glycosidase
IPR018221 Glycoside hydrolase, family 9, active site
GO Term annotationHelp
Process GO:0005975 carbohydrate metabolic process
Function GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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 9 GH9 comprises enzymes with several known activities; endoglucanase (EC:3.2.1.4); cellobiohydrolase (EC:3.2.1.91). These enzymes were formerly known as cellulase family E.

Structural linksHelp
SCOP: a.102.1.2 , b.2.2.2
Database linksHelp
PDBe-motif: PS00592 , PS00698
Enzyme: EC:3.2.1.4
CAZy: GH9
PROSITE doc: PDOC00511
PANDIT: PF00759
Blocks: IPB001701
Pfam Clan: CL0059.11

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR001701 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
A2XYW8 Endoglucanase 13

O04478 Endoglucanase 7

P05522 Endoglucanase 1

P14090 Endoglucanase C

P22699 Endoglucanase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR003305 Carbohydrate-binding, CenC-like
IPR007110 Immunoglobulin-like
IPR003599 Immunoglobulin subtype
IPR001701 Glycoside hydrolase, family 9
IPR013783 Immunoglobulin-like fold
IPR004197 Glycoside hydrolase, family 9, N-terminal, Ig-like
IPR014756 Immunoglobulin E-set
IPR013098 Immunoglobulin I-set
IPR019028 Carbohydrate binding domain CBM49
IPR012341 Six-hairpin glycosidase
IPR008928 Six-hairpin glycosidase-like
IPR008979 Galactose-binding domain-like
IPR018221 Glycoside hydrolase, family 9, active site
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
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 ReadingHelp
Schubot FD, Kataeva IA, Chang J, Shah AK, Ljungdahl LG, Rose JP, Wang BC.
Structural basis for the exocellulase activity of the cellobiohydrolase CbhA from Clostridium thermocellum.
Biochemistry 43 2004 1163-70 [PubMed: 14756552]
http://dx.doi.org/10.1021/bi030202i
Parsiegla G, Belaich A, Belaich JP, Haser R.
Crystal structure of the cellulase Cel9M enlightens structure/function relationships of the variable catalytic modules in glycoside hydrolases.
Biochemistry 41 2002 11134-42 [PubMed: 12220178]
http://dx.doi.org/10.1021/bi025816m
Sakon J, Irwin D, Wilson DB, Karplus PA.
Structure and mechanism of endo/exocellulase E4 from Thermomonospora fusca.
Nat. Struct. Biol. 4 1997 810-8 [PubMed: 9334746]
http://dx.doi.org/10.1038/nsb1097-810
Mandelman D, Belaich A, Belaich JP, Aghajari N, Driguez H, Haser R.
X-Ray crystal structure of the multidomain endoglucanase Cel9G from Clostridium cellulolyticum complexed with natural and synthetic cello-oligosaccharides.
J. Bacteriol. 185 2003 4127-35 [PubMed: 12837787]
http://dx.doi.org/10.1128/JB.185.14.4127-4135.2003
Khademi S, Guarino LA, Watanabe H, Tokuda G, Meyer EF.
Structure of an endoglucanase from termite, Nasutitermes takasagoensis.
Acta Crystallogr. D Biol. Crystallogr. 58 2002 653-9 [PubMed: 11914490]
http://dx.doi.org/10.1107/S0907444902002366
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InterPro 23.1