DB code: D00167

RLCP classification 1.30.5050.991 : Hydrolysis
CATH domain 1.50.10.10 : Glycosyltransferase Catalytic domain
1.10.1330.10 : Type 1 dockerin domain
E.C. 3.2.1.4
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
1.50.10.10 : Glycosyltransferase S00531 S00048 S00845 D00500 M00192 T00245 T00246
1.10.1330.10 : Type 1 dockerin domain D00503 T00245 T00246

Uniprot Enzyme Name
UniprotKB Protein name Synonyms CAZy Pfam
Q9EYQ2
Cellulase Cel9-M
GH9 (Glycoside Hydrolase Family 9)
PF00404 (Dockerin_1)
PF00759 (Glyco_hydro_9)
[Graphical View]

KEGG enzyme name
cellulase
endo-1,4-beta-D-glucanase
beta-1,4-glucanase
beta-1,4-endoglucan hydrolase
celluase A
cellulosin AP
endoglucanase D
alkali cellulase
cellulase A 3
celludextrinase
9.5 cellulase
avicelase
pancellase SS
1,4-(1,3
1,4)-beta-D-glucan 4-glucanohydrolase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q9EYQ2 Q9EYQ2_CLOCE

KEGG Pathways
Map code Pathways E.C.
MAP00500 Starch and sucrose metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00038 C00760 C00478 C00551 C00001 C00760 C00551
E.C.
Compound Zinc Cellulose Lichenin beta-D-Glucan H2O Cellulose beta-D-Glucan
Type heavy metal polysaccharide carbohydrate polysaccharide H2O polysaccharide polysaccharide
ChEBI 29105
15377
PubChem 32051
439241
46173706
962
22247451
46173706
1ia6A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_ZN Unbound Unbound Unbound Unbound Unbound
1ia7A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_ZN Unbound Unbound Unbound Unbound Bound:GLC-GLC

Reference for Active-site residues
resource references E.C.
PDB;1ia7 & literature [6], [7], [10], [13]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1ia6A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 56;ASP 59;HIS 126;TYR 204;GLU 410 CYS 22;CYS 38;HIS 39;HIS 55(Zinc binding)
1ia7A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 56;ASP 59;HIS 126;TYR 204;GLU 410 CYS 22;CYS 38;HIS 39;HIS 55(Zinc binding)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[5]
p.91
[7]
Fig.4, p.814-815
[10]
p.11138

References
[1]
Resource
Comments CALCIUM-BINDING DATA.
Medline ID 90147577
PubMed ID 2302168
Journal Biochem J
Year 1990
Volume 265
Pages 261-5
Authors Chauvaux S, Beguin P, Aubert JP, Bhat KM, Gow LA, Wood TM, Bairoch A
Title Calcium-binding affinity and calcium-enhanced activity of Clostridium thermocellum endoglucanase D.
Related PDB
Related UniProtKB
[2]
Resource
Comments ACTIVE SITE HIS-516, AND MUTAGENESIS OF ALL HISTIDINE RESIDUES.
Medline ID 91244802
PubMed ID 2037583
Journal J Biol Chem
Year 1991
Volume 266
Pages 10313-8
Authors Tomme P, Chauvaux S, Beguin P, Millet J, Aubert JP, Claeyssens M
Title Identification of a histidyl residue in the active center of endoglucanase D from Clostridium thermocellum.
Related PDB
Related UniProtKB
[3]
Resource
Comments ACTIVE SITE ASP-546.
Medline ID 92344589
PubMed ID 1637316
Journal Biochem J
Year 1992
Volume 285
Pages 319-24
Authors Tomme P, van Beeumen J, Claeyssens M
Title Modification of catalytically important carboxy residues in endoglucanase D from Clostridium thermocellum.
Related PDB
Related UniProtKB
[4]
Resource
Comments ACTIVE SITE GLU-555, AND MUTAGENESIS OF ASPARTIC ACID AND GLUTAMIC ACID RESIDUES.
Medline ID 92165798
PubMed ID 1537833
Journal J Biol Chem
Year 1992
Volume 267
Pages 4472-8
Authors Chauvaux S, Beguin P, Aubert JP
Title Site-directed mutagenesis of essential carboxylic residues in Clostridium thermocellum endoglucanase CelD.
Related PDB
Related UniProtKB
[5]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Medline ID
PubMed ID
Journal Nature
Year 1992
Volume 357
Pages 89-91
Authors Juy M, Amit AG, Alzari PM, Poljak RJ, Claeyssens M, Beguin P, Aubert J-P
Title Three-dimensional structure of a thermostable bacterial cellulase.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 7730353
Journal J Biol Chem
Year 1995
Volume 270
Pages 9757-62
Authors Chauvaux S, Souchon H, Alzari PM, Chariot P, Beguin P
Title Structural and functional analysis of the metal-binding sites of Clostridium thermocellum endoglucanase CelD.
Related PDB
Related UniProtKB
[7]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 47-651
Medline ID 9334746
PubMed ID 9334746
Journal Nat Struct Biol
Year 1997
Volume 4
Pages 810-8
Authors Sakon J, Irwin D, Wilson DB, Karplus PA
Title Structure and mechanism of endo/exocellulase E4 from Thermomonospora fusca.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 11273698
Journal J Mol Biol
Year 2001
Volume 307
Pages 745-53
Authors Lytle BL, Volkman BF, Westler WM, Heckman MP, Wu JH
Title Solution structure of a type I dockerin domain, a novel prokaryotic, extracellular calcium-binding domain.
Related PDB
Related UniProtKB
[9]
Resource
Comments X-ray crystallography (1.4 Angstroms)
Medline ID
PubMed ID 11914490
Journal Acta Crystallogr D Biol Crystallogr
Year 2002
Volume 58
Pages 653-659
Authors Khademi S, Guarino LA, Watanabe H, Tokuda G, Meyer EF
Title Structure of an endoglucanase from termite, Nasutitermes takasagoensis.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 12220178
Journal Biochemistry
Year 2002
Volume 41
Pages 11134-42
Authors Parsiegla G, Belaich A, Belaich JP, Haser R
Title Crystal structure of the cellulase Cel9M enlightens structure/function relationships of the variable catalytic modules in glycoside hydrolases.
Related PDB 1ia6 1ia7
Related UniProtKB Q9EYQ2
[11]
Resource
Comments
Medline ID
PubMed ID 11844767
Journal J Bacteriol
Year 2002
Volume 184
Pages 1378-84
Authors Belaich A, Parsiegla G, Gal L, Villard C, Haser R, Belaich JP
Title Cel9M, a new family 9 cellulase of the Clostridium cellulolyticum cellulosome.
Related PDB
Related UniProtKB

Comments
This enzyme belongs to the glycosidase family-9, with an inverting mechanism.
This enzyme is composed of the N-terminal catalytic domain and the C-terminal Dockerin repeat. Although the structure of the Dockerin repeat region has not been determined yet, it must have a similar structure to that of Dockerin domain (PDB;1daq).
Although this enzyme binds a zinc ion and a calcium ion, they are not involved in catalysis.
This enzyme seems to have the same catalytic mechanism as that of its homologous enzymes, endoglucanase (M00192, T00246 in EzCatDB) and cellulase (S00531 in EzCatDB).

Created Updated
2004-08-18 2009-02-26