DB code: D00504

RLCP classification 1.30.36211.992 : Hydrolysis
CATH domain 2.60.120.180 : Jelly Rolls Catalytic domain
2.60.40.290 : Immunoglobulin-like
E.C. 3.2.1.4
CSA 2nlr
M-CSA 2nlr
MACiE

CATH domain Related DB codes (homologues)
2.60.40.290 : Immunoglobulin-like M00219 D00479 D00502 M00026 M00192
2.60.120.180 : Jelly Rolls S00533 S00150 S00151 D00538

Uniprot Enzyme Name
UniprotKB Protein name Synonyms CAZy Pfam
Q54331
Cellulase B
CBM2 (Carbohydrate-Binding Module Family 2)
GH12 (Glycoside Hydrolase Family 12)
PF00553 (CBM_2)
PF01670 (Glyco_hydro_12)
[Graphical View]
Q9KIH1
Cellulase 12A
CBM2 (Carbohydrate-Binding Module Family 2)
GH12 (Glycoside Hydrolase Family 12)
PF00553 (CBM_2)
PF01670 (Glyco_hydro_12)
[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
Q9KIH1 Q9KIH1_9ACTO
Q54331 Q54331_STRLI

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
E.C.
Compound Cellulose Lichenin beta-D-Glucan H2O Cellulose beta-D-Glucan Transition-state for glycosylated enzyme Glycosylated enzyme intermediate
Type polysaccharide carbohydrate polysaccharide H2O polysaccharide polysaccharide
ChEBI 15377
PubChem 439241
46173706
22247451
962
46173706
1nlrA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2nlrA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:GLC-GLC-G2F
1oa4A 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.
see S00150

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1nlrA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 100;ASP 104;GLU 120;GLU 203
2nlrA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 100;ASP 104;GLU 120;GLU 203
1oa4A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 100;ASP 104;GLU 120;GLU 203

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
p.16037-16038

References
[1]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 41-274.
Medline ID
PubMed ID 9440876
Journal Biochemistry
Year 1997
Volume 36
Pages 16032-9
Authors Sulzenbacher G, Shareck F, Morosoli R, Dupont C, Davies GJ
Title The Streptomyces lividans family 12 endoglucanase: construction of the catalytic cre, expression, and X-ray structure at 1.75 A resolution.
Related PDB 1nlr
Related UniProtKB Q54331
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 41-274.
Medline ID
PubMed ID 10200171
Journal Biochemistry
Year 1999
Volume 38
Pages 4826-33
Authors Sulzenbacher G, Mackenzie LF, Wilson KS, Withers SG, Dupont C, Davies GJ
Title The crystal structure of a 2-fluorocellotriosyl complex of the Streptomyces lividans endoglucanase CelB2 at 1.2 A resolution.
Related PDB 2nlr
Related UniProtKB Q54331
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 32-253.
Medline ID
PubMed ID 12649442
Journal Protein Sci
Year 2003
Volume 12
Pages 848-60
Authors Sandgren M, Gualfetti PJ, Shaw A, Gross LS, Saldajeno M, Day AG, Jones TA, Mitchinson C
Title Comparison of family 12 glycoside hydrolases and recruited substitutions important for thermal stability.
Related PDB 1oa4
Related UniProtKB Q9KIH1

Comments
This enzyme belongs to the glycosidase family-12.
This enzyme is composed of two domains, N-terminal catalytic domain and C-terminal cellulose-binding domain. Although the structure of the C-terminal cellulose-binding domain has not been solved yet, homology search can suggest its domain structure.
The catalytic mechanism of this enzyme must be the same as that of its homologous enzyme, cellulase (S00150 in EzCatDB).

Created Updated
2004-05-17 2009-02-26