DB code: T00246

RLCP classification 1.30.5050.991 : Hydrolysis
CATH domain 1.50.10.10 : Glycosyltransferase Catalytic domain
2.60.40.710 : Immunoglobulin-like
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 D00167 D00503 T00245
1.50.10.10 : Glycosyltransferase S00531 S00048 S00845 D00167 D00500 M00192 T00245
2.60.40.710 : Immunoglobulin-like M00192

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq CAZy Pfam
P37700 Endoglucanase G
EC 3.2.1.4
Endo-1,4-beta-glucanase G
Cellulase G
EGCCG
YP_002505090.1 (Protein)
NC_011898.1 (DNA/RNA sequence)
CBM3 (Carbohydrate-Binding Module Family 3)
GH9 (Glycoside Hydrolase Family 9)
PF00942 (CBM_3)
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
P37700 GUNG_CLOCE Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

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

Compound table
Substrates Products Intermediates
KEGG-id C00760 C00478 C00551 C00001 C00760 C00551 C00185
E.C.
Compound Cellulose Lichenin beta-D-Glucan H2O Cellulose beta-D-Glucan Cellobiose
Type polysaccharide carbohydrate polysaccharide H2O polysaccharide polysaccharide polysaccharide
ChEBI 15377
17057
PubChem 439241
46173706
962
22247451
46173706
439178
1g87A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1g87B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1ga2A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Analogue:GLC-GLC-GLC (chain X) Unbound Bound:GLC-GLC (chain Y)
1ga2B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1k72A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Bound:CBI
1k72B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1kfgA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Analogue:SGC-GLC-SGC-GS1 (chain X) Unbound Unbound
1kfgB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Analogue:SGC-GLC-SGC-GS1 (chain Y) Unbound Unbound
1g87A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1g87B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1ga2A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1ga2B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1k72A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1k72B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1kfgA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1kfgB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1g87 & literature [4], [8], [9]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1g87A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 55;ASP 58;HIS 125;TYR 205;GLU 420
1g87B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 55;ASP 58;HIS 125;TYR 205;GLU 420
1ga2A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 55;ASP 58;HIS 125;TYR 205;GLU 420
1ga2B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 55;ASP 58;HIS 125;TYR 205;GLU 420
1k72A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 55;ASP 58;HIS 125;TYR 205;GLU 420
1k72B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 55;ASP 58;HIS 125;TYR 205;GLU 420
1kfgA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 55;ASP 58;HIS 125;TYR 205;GLU 420
1kfgB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 55;ASP 58;HIS 125;TYR 205;GLU 420
1g87A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1g87B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ga2A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ga2B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1k72A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1k72B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1kfgA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1kfgB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[4]
Fig.4, p.814-815
[6]
p.657-658
[9]
p.9662

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
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
[3]
Resource
Comments
Medline ID
PubMed ID 9352905
Journal J Bacteriol
Year 1997
Volume 179
Pages 6595-601
Authors Gal L, Gaudin C, Belaich A, Pages S, Tardif C, Belaich JP
Title CelG from Clostridium cellulolyticum: a multidomain endoglucanase acting efficiently on crystalline cellulose.
Related PDB
Related UniProtKB
[4]
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
[5]
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
[6]
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
[7]
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
[8]
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 1g87 1ga2 1k72 1kfg
Related UniProtKB
[9]
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 calcium ion, they are not involved in catalysis at all.
Although the structure of the third domain (dockerin repeat region) has not been determined yet, it must have a similar structure to type I dockerin domain from Clostridium thermocellum endoglucanase (PDB; 1daq, Swiss-prot;P38686).
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