EzCatDB: D00536
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DB codeD00536
RLCP classification1.30.300.2 : Hydrolysis
CATH domainDomain 13.20.20.40 : TIM BarrelCatalytic domain
Domain 22.60.40.- : Immunoglobulin-like
E.C.3.2.1.4
CSA1tml

CATH domainRelated DB codes (homologues)
3.20.20.40 : TIM BarrelS00194,D00537

Enzyme Name
UniProtKBKEGG

P26222
Protein nameEndoglucanase E-2cellulase
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
SynonymsEC 3.2.1.4
Cellulase E-2
Cellulase E2
Endo-1,4-beta-glucanase E-2
PfamPF00553 (CBM_2)
PF01341 (Glyco_hydro_6)
[Graphical view]
CAZyGH6 (Glycoside Hydrolase Family)

KEGG pathways
MAP codePathways
MAP00500Starch and sucrose metabolism

UniProtKB:Accession NumberP26222
Entry nameGUN2_THEFU
ActivityEndohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
SubunitHomodimer.
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00760C00001C00478C00551C00760C00551
CompoundCelluloseH2OLicheninbeta-D-GlucanCellulosebeta-D-Glucan
TypepolysaccharideH2Ocarbohydratepolysaccharidepolysaccharidepolysaccharide
ChEBI
15377




PubChem
22247451
962
439241
46173706

46173706
              
1tmlAUnbound UnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P26222
pdbCatalytic residues
         
1tmlAASP 79;ASP 117;ASP 156;ASP 265

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[10]p.9750-9751
[11]p.204-206

references
[1]
PubMed ID8215374
JournalAppl Environ Microbiol
Year1993
Volume59
Pages3032-43
AuthorsJung ED, Lao G, Irwin D, Barr BK, Benjamin A, Wilson DB
TitleDNA sequences and expression in Streptomyces lividans of an exoglucanase gene and an endoglucanase gene from Thermomonospora fusca.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 32-317.
Medline ID94002001
PubMed ID8399160
JournalBiochemistry
Year1993
Volume32
Pages9906-16
AuthorsSpezio M, Wilson DB, Karplus PA
TitleCrystal structure of the catalytic domain of a thermophilic endocellulase.
Related PDB1tml
Related UniProtKBP26222
[3]
PubMed ID7789807
JournalGene
Year1995
Volume158
Pages23-9
AuthorsQuillet L, Barray S, Labedan B, Petit F, Guespin-Michel J
TitleThe gene encoding the beta-1,4-endoglucanase (CelA) from Myxococcus xanthus: evidence for independent acquisition by horizontal transfer of binding and catalytic domains from actinomycetes.
[4]
PubMed ID8615816
JournalBiochem J
Year1996
Volume315
Pages467-72
AuthorsDamude HG, Ferro V, Withers SG, Warren RA
TitleSubstrate specificity of endoglucanase A from Cellulomonas fimi: fundamental differences between endoglucanases and exoglucanases from family 6.
[5]
PubMed ID8824619
JournalJ Bacteriol
Year1996
Volume178
Pages5732-40
AuthorsAhsan MM, Kimura T, Karita S, Sakka K, Ohmiya K
TitleCloning, DNA sequencing, and expression of the gene encoding Clostridium thermocellum cellulase CelJ, the largest catalytic component of the cellulosome.
[6]
PubMed ID9438981
JournalBiosci Biotechnol Biochem
Year1997
Volume61
Pages2004-9
AuthorsHitomi J, Hatada Y, Kawaminami S, Kawai S, Ito S
TitleAmino acid sequence and stereoselective hydrolytic reaction of an endo-1,4-beta-glucanase from a Bacillus strain.
[7]
PubMed ID9335169
JournalJ Biotechnol
Year1997
Volume57
Pages101-13
AuthorsZhang S, Wilson DB
TitleSurface residue mutations which change the substrate specificity of Thermomonospora fusca endoglucanase E2.
[8]
PubMed ID9649302
JournalBiochemistry
Year1998
Volume37
Pages9220-9
AuthorsBarr BK, Wolfgang DE, Piens K, Claeyssens M, Wilson DB
TitleActive-site binding of glycosides by Thermomonospora fusca endocellulase E2.
[9]
PubMed ID10029552
JournalBiochemistry
Year1999
Volume38
Pages2570-6
AuthorsBeadle BM, Baase WA, Wilson DB, Gilkes NR, Shoichet BK
TitleComparing the thermodynamic stabilities of a related thermophilic and mesophilic enzyme.
[10]
PubMed ID10423254
JournalBiochemistry
Year1999
Volume38
Pages9746-51
AuthorsWolfgang DE, Wilson DB
TitleMechanistic studies of active site mutants of Thermomonospora fusca endocellulase E2.
[11]
CommentsX-ray crystallography
PubMed ID10794732
JournalBiochem J
Year2000
Volume348 Pt 1
Pages201-7
AuthorsDavies GJ, Brzozowski AM, Dauter M, Varrot A, Schulein M
TitleStructure and function of Humicola insolens family 6 cellulases: structure of the endoglucanase, Cel6B, at 1.6 A resolution.
Related PDB1dys
[12]
PubMed ID10731432
JournalJ Mol Biol
Year2000
Volume297
Pages819-28
AuthorsVarrot A, Schulein M, Davies GJ
TitleInsights into ligand-induced conformational change in Cel5A from Bacillus agaradhaerens revealed by a catalytically active crystal form.
[13]
PubMed ID11311718
JournalInt J Biol Macromol
Year2001
Volume28
Pages285-92
AuthorsNovo C, Simoes F, Mendonca D, Matos J, Clemente A
TitlePrimary structure deduction and molecular modelling from a cDNA of a cellobiohydrolase-like protein from the white-rot fungus Coriolus versicolor.
[14]
PubMed ID11514516
JournalJ Bacteriol
Year2001
Volume183
Pages5325-33
AuthorsSteenbakkers PJ, Li XL, Ximenes EA, Arts JG, Chen H, Ljungdahl LG, Op Den Camp HJ
TitleNoncatalytic docking domains of cellulosomes of anaerobic fungi.
[15]
PubMed ID11495244
JournalJ Biomol NMR
Year2001
Volume20
Pages127-33
AuthorsPermi P, Annila A
TitleA new approach for obtaining sequential assignment of large proteins.
[16]
PubMed ID12071852
JournalBiochem J
Year2002
Volume365
Pages193-204
AuthorsSteenbakkers PJ, Ubhayasekera W, Goossen HJ, van Lierop EM, van der Drift C, Vogels GD, Mowbray SL, Op den Camp HJ
TitleAn intron-containing glycoside hydrolase family 9 cellulase gene encodes the dominant 90 kDa component of the cellulosome of the anaerobic fungus Piromyces sp. strain E2.

comments
The catalytic domain of this enzyme homologous to the counterpart enzyme from Humicola insolens (S00194 in EzCatDB).
This family belongs to Glycosidase family-6, which has an inverting mechanism (equatorial to axial conformation). Furthermore, this enzyme belongs to endoglucanase, whilst its family member (EC 3.2.1.91) is exoglucanase.
According to the Swiss-prot (P26222), Asp117 acts as proton donor, whilst Asp265 acts as base. The rest of aspartic residues serve as pKa modulator. However, literature [10] suggests that the residue corresponding to Asp265 plays an important role in binding rather than as base. In contrast, [11] suggests that the possiblity of Asp265 as base catalyst could not be ruled out.

createdupdated
2002-10-152009-03-24
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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