EzCatDB: D00504
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DB codeD00504
RLCP classification1.30.36211.992 : Hydrolysis
CATH domainDomain 12.60.120.180 : Jelly RollsCatalytic domain
Domain 22.60.40.290 : Immunoglobulin-like
E.C.3.2.1.4
CSA2nlr

CATH domainRelated DB codes (homologues)
2.60.120.180 : Jelly RollsS00533,S00150,S00151,D00538
2.60.40.290 : Immunoglobulin-likeM00219,D00479,D00502,M00026,M00192

Enzyme Name
UniProtKBKEGG

Q54331Q9KIH1
Protein 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
SynonymsCellulase B
Cellulase 12A
PfamPF00553 (CBM_2)
PF01670 (Glyco_hydro_12)
[Graphical view]
PF00553 (CBM_2)
PF01670 (Glyco_hydro_12)
[Graphical view]
CAZyGH12 (Glycoside Hydrolase Family)
GH12 (Glycoside Hydrolase Family)

KEGG pathways
MAP codePathways
MAP00500Starch and sucrose metabolism

UniProtKB:Accession NumberQ54331Q9KIH1
Entry nameQ54331_STRLIQ9KIH1_9ACTO
Activity

Subunit

Subcellular location

Cofactor


Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00760C00478C00551C00001C00760C00551

CompoundCelluloseLicheninbeta-D-GlucanH2OCellulosebeta-D-GlucanTransition-state for glycosylated enzymeGlycosylated enzyme intermediate
TypepolysaccharidecarbohydratepolysaccharideH2Opolysaccharidepolysaccharide

ChEBI


15377




PubChem
439241
46173706
962
22247451

46173706


                
1nlrAUnboundUnboundUnbound UnboundUnboundUnbound 
2nlrAUnboundUnboundUnbound UnboundUnboundTransition-state-analogue:GLC-GLC-G2F 
1oa4AUnboundUnboundUnbound UnboundUnboundUnbound 

Active-site residues
resource
see S00150
pdbCatalytic residues
         
1nlrAASN 100;ASP 104;GLU 120;GLU 203
2nlrAASN 100;ASP 104;GLU 120;GLU 203
1oa4AASN 100;ASP 104;GLU 120;GLU 203

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]p.16037-16038

references
[1]
CommentsX-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 41-274.
PubMed ID9440876
JournalBiochemistry
Year1997
Volume36
Pages16032-9
AuthorsSulzenbacher G, Shareck F, Morosoli R, Dupont C, Davies GJ
TitleThe Streptomyces lividans family 12 endoglucanase: construction of the catalytic cre, expression, and X-ray structure at 1.75 A resolution.
Related PDB1nlr
Related UniProtKBQ54331
[2]
CommentsX-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 41-274.
PubMed ID10200171
JournalBiochemistry
Year1999
Volume38
Pages4826-33
AuthorsSulzenbacher G, Mackenzie LF, Wilson KS, Withers SG, Dupont C, Davies GJ
TitleThe crystal structure of a 2-fluorocellotriosyl complex of the Streptomyces lividans endoglucanase CelB2 at 1.2 A resolution.
Related PDB2nlr
Related UniProtKBQ54331
[3]
CommentsX-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 32-253.
PubMed ID12649442
JournalProtein Sci
Year2003
Volume12
Pages848-60
AuthorsSandgren M, Gualfetti PJ, Shaw A, Gross LS, Saldajeno M, Day AG, Jones TA, Mitchinson C
TitleComparison of family 12 glycoside hydrolases and recruited substitutions important for thermal stability.
Related PDB1oa4
Related UniProtKBQ9KIH1

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).

createdupdated
2004-05-172009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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