EzCatDB: S00531
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DB codeS00531
RLCP classification1.30.5050.991 : Hydrolysis
CATH domainDomain 11.50.10.10 : GlycosyltransferaseCatalytic domain
E.C.3.2.1.4

CATH domainRelated DB codes (homologues)
1.50.10.10 : GlycosyltransferaseS00048,S00845,D00167,D00500,M00192,T00245,T00246

Enzyme Name
UniProtKBKEGG

O77044
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
SynonymsEndo-b-1,4-glucanase (Cellulase NtEG)
EC 3.2.1.4
PfamPF00759 (Glyco_hydro_9)
[Graphical view]
CAZyGH9 (Glycoside Hydrolase Family)

KEGG pathways
MAP codePathways
MAP00500Starch and sucrose metabolism

UniProtKB:Accession NumberO77044
Entry nameO77044_9NEOP
Activity
Subunit
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00001C00760C00478C00551C00760C00551
CompoundH2OCelluloseLicheninbeta-D-GlucanCellulosebeta-D-Glucan
TypeH2Opolysaccharidecarbohydratepolysaccharidepolysaccharidepolysaccharide
ChEBI15377





PubChem962
22247451

439241
46173706

46173706
              
1ks8A UnboundUnboundUnboundUnboundUnbound
1kscA UnboundUnboundUnboundUnboundUnbound
1ksdA UnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
PDB;1ks8 & literature [1], [4], [5]
pdbCatalytic residues
         
1ks8AASP 54;ASP 57;HIS 124;TYR 206;GLU 412
1kscAASP 54;ASP 57;HIS 124;TYR 206;GLU 412
1ksdAASP 54;ASP 57;HIS 124;TYR 206;GLU 412

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]Fig.4, p.814-815
[3]p.657-658
[5]p.9662

references
[1]
PubMed ID7730353
JournalJ Biol Chem
Year1995
Volume270
Pages9757-62
AuthorsChauvaux S, Souchon H, Alzari PM, Chariot P, Beguin P
TitleStructural and functional analysis of the metal-binding sites of Clostridium thermocellum endoglucanase CelD.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 47-651
Medline ID9334746
PubMed ID9334746
JournalNat Struct Biol
Year1997
Volume4
Pages810-8
AuthorsSakon J, Irwin D, Wilson DB, Karplus PA
TitleStructure and mechanism of endo/exocellulase E4 from Thermomonospora fusca.
[3]
CommentsX-ray crystallography (1.4 Angstroms)
PubMed ID11914490
JournalActa Crystallogr D Biol Crystallogr
Year2002
Volume58
Pages653-659
AuthorsKhademi S, Guarino LA, Watanabe H, Tokuda G, Meyer EF
TitleStructure of an endoglucanase from termite, Nasutitermes takasagoensis.
Related PDB1ks8,1ksc,1ksd
[4]
CommentsX-ray crystallography
PubMed ID12837787
JournalJ Bacteriol
Year2003
Volume185
Pages4127-35
AuthorsMandelman D, Belaich A, Belaich JP, Aghajari N, Driguez H, Haser R
TitleX-Ray crystal structure of the multidomain endoglucanase Cel9G from Clostridium cellulolyticum complexed with natural and synthetic cello-oligosaccharides.
[5]
PubMed ID15274620
JournalBiochemistry
Year2004
Volume43
Pages9655-63
AuthorsZhou W, Irwin DC, Escovar-Kousen J, Wilson DB
TitleKinetic studies of Thermobifida fusca Cel9A active site mutant enzymes.

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).

createdupdated
2004-08-182009-02-26


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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)
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