DB code: D00167

RLCP classification	1.30.5050.991 : Hydrolysis
CATH domain	1.50.10.10 : Glycosyltransferase	Catalytic domain
CATH 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)
1.10.1330.10 : Type 1 dockerin domain	D00503 T00245 T00246
1.50.10.10 : Glycosyltransferase	S00531 S00048 S00845 D00500 M00192 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 29105				15377 15377
PubChem	32051 32051		439241 439241	46173706 46173706	22247451 962 22247451 962		46173706 46173706

1ia6A	Bound:_ZN	Unbound	Unbound	Unbound		Unbound	Unbound
1ia7A	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	ASP 56;ASP 59;HIS 126;TYR 204;GLU 410	CYS 22;CYS 38;HIS 39;HIS 55(Zinc binding)
1ia7A	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).

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