DB code: S00531

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

CATH domain Related DB codes (homologues)
1.50.10.10 : Glycosyltransferase S00048 S00845 D00167 D00500 M00192 T00245 T00246

Uniprot Enzyme Name
UniprotKB Protein name Synonyms CAZy Pfam
O77044
Endo-b-1,4-glucanase (Cellulase NtEG)
EC 3.2.1.4
GH9 (Glycoside Hydrolase Family 9)
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
O77044 O77044_9NEOP

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

Compound table
Substrates Products Intermediates
KEGG-id C00001 C00760 C00478 C00551 C00760 C00551
E.C.
Compound H2O Cellulose Lichenin beta-D-Glucan Cellulose beta-D-Glucan
Type H2O polysaccharide carbohydrate polysaccharide polysaccharide polysaccharide
ChEBI 15377
 15377
PubChem 22247451
 962
 22247451
 962
 		439241
 439241
 		46173706
 46173706
 		46173706
 46173706
1ks8A Unbound Unbound Unbound Unbound Unbound
1kscA Unbound Unbound Unbound Unbound Unbound
1ksdA Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1ks8 & literature [1], [4], [5]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1ks8A ASP 54;ASP 57;HIS 124;TYR 206;GLU 412
1kscA ASP 54;ASP 57;HIS 124;TYR 206;GLU 412
1ksdA ASP 54;ASP 57;HIS 124;TYR 206;GLU 412

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
Fig.4, p.814-815
[3]
p.657-658
[5]
p.9662

References
[1]
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
[2]
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
[3]
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 1ks8 1ksc 1ksd
Related UniProtKB
[4]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12837787
Journal J Bacteriol
Year 2003
Volume 185
Pages 4127-35
Authors Mandelman D, Belaich A, Belaich JP, Aghajari N, Driguez H, Haser R
Title X-Ray crystal structure of the multidomain endoglucanase Cel9G from Clostridium cellulolyticum complexed with natural and synthetic cello-oligosaccharides.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 15274620
Journal Biochemistry
Year 2004
Volume 43
Pages 9655-63
Authors Zhou W, Irwin DC, Escovar-Kousen J, Wilson DB
Title Kinetic studies of Thermobifida fusca Cel9A active site mutant enzymes.
Related PDB
Related UniProtKB

Comments
This enzyme belongs to the glycosidase family-9.
Although this enzyme binds a calcium ion, it is not involved in catalysis at all.
The reaction mechanism of this enzyme must be similar to that of the homologous enzyme (M00192 in EzCatDB).

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