EzCatDB: T00246
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DB codeT00246
RLCP classification1.30.5050.991 : Hydrolysis
CATH domainDomain 11.50.10.10 : GlycosyltransferaseCatalytic domain
Domain 22.60.40.710 : Immunoglobulin-like
Domain 31.10.1330.10 : Type 1 dockerin domain
E.C.3.2.1.4

CATH domainRelated DB codes (homologues)
1.10.1330.10 : Type 1 dockerin domainD00167,D00503,T00245
1.50.10.10 : GlycosyltransferaseS00531,S00048,S00845,D00167,D00500,M00192,T00245
2.60.40.710 : Immunoglobulin-likeM00192

Enzyme Name
UniProtKBKEGG

P37700
Protein nameEndoglucanase Gcellulase
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
Endo-1,4-beta-glucanase G
Cellulase G
EGCCG
RefSeqYP_002505090.1 (Protein)
NC_011898.1 (DNA/RNA sequence)
PfamPF00942 (CBM_3)
PF00404 (Dockerin_1)
PF00759 (Glyco_hydro_9)
[Graphical view]
CAZyGH9 (Glycoside Hydrolase Family)

KEGG pathways
MAP codePathways
MAP00500Starch and sucrose metabolism

UniProtKB:Accession NumberP37700
Entry nameGUNG_CLOCE
ActivityEndohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Subunit
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00760C00478C00551C00001C00760C00551C00185
CompoundCelluloseLicheninbeta-D-GlucanH2OCellulosebeta-D-GlucanCellobiose
TypepolysaccharidecarbohydratepolysaccharideH2Opolysaccharidepolysaccharidepolysaccharide
ChEBI


15377


17057
PubChem
439241
46173706
962
22247451

46173706
439178
               
1g87A01UnboundUnboundUnbound UnboundUnboundUnbound
1g87B01UnboundUnboundUnbound UnboundUnboundUnbound
1ga2A01UnboundUnboundUnbound Analogue:GLC-GLC-GLC(chain X)UnboundBound:GLC-GLC(chain Y)
1ga2B01UnboundUnboundUnbound UnboundUnboundUnbound
1k72A01UnboundUnboundUnbound UnboundUnboundBound:CBI
1k72B01UnboundUnboundUnbound UnboundUnboundUnbound
1kfgA01UnboundUnboundUnbound Analogue:SGC-GLC-SGC-GS1(chain X)UnboundUnbound
1kfgB01UnboundUnboundUnbound Analogue:SGC-GLC-SGC-GS1(chain Y)UnboundUnbound
1g87A02UnboundUnboundUnbound UnboundUnboundUnbound
1g87B02UnboundUnboundUnbound UnboundUnboundUnbound
1ga2A02UnboundUnboundUnbound UnboundUnboundUnbound
1ga2B02UnboundUnboundUnbound UnboundUnboundUnbound
1k72A02UnboundUnboundUnbound UnboundUnboundUnbound
1k72B02UnboundUnboundUnbound UnboundUnboundUnbound
1kfgA02UnboundUnboundUnbound UnboundUnboundUnbound
1kfgB02UnboundUnboundUnbound UnboundUnboundUnbound

Active-site residues
resource
PDB;1g87 & literature [4], [8], [9]
pdbCatalytic residues
         
1g87A01ASP 55;ASP 58;HIS 125;TYR 205;GLU 420
1g87B01ASP 55;ASP 58;HIS 125;TYR 205;GLU 420
1ga2A01ASP 55;ASP 58;HIS 125;TYR 205;GLU 420
1ga2B01ASP 55;ASP 58;HIS 125;TYR 205;GLU 420
1k72A01ASP 55;ASP 58;HIS 125;TYR 205;GLU 420
1k72B01ASP 55;ASP 58;HIS 125;TYR 205;GLU 420
1kfgA01ASP 55;ASP 58;HIS 125;TYR 205;GLU 420
1kfgB01ASP 55;ASP 58;HIS 125;TYR 205;GLU 420
1g87A02 
1g87B02 
1ga2A02 
1ga2B02 
1k72A02 
1k72B02 
1kfgA02 
1kfgB02 

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

references
[1]
CommentsCALCIUM-BINDING DATA.
Medline ID90147577
PubMed ID2302168
JournalBiochem J
Year1990
Volume265
Pages261-5
AuthorsChauvaux S, Beguin P, Aubert JP, Bhat KM, Gow LA, Wood TM, Bairoch A
TitleCalcium-binding affinity and calcium-enhanced activity of Clostridium thermocellum endoglucanase D.
[2]
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.
[3]
PubMed ID9352905
JournalJ Bacteriol
Year1997
Volume179
Pages6595-601
AuthorsGal L, Gaudin C, Belaich A, Pages S, Tardif C, Belaich JP
TitleCelG from Clostridium cellulolyticum: a multidomain endoglucanase acting efficiently on crystalline cellulose.
[4]
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.
[5]
PubMed ID11273698
JournalJ Mol Biol
Year2001
Volume307
Pages745-53
AuthorsLytle BL, Volkman BF, Westler WM, Heckman MP, Wu JH
TitleSolution structure of a type I dockerin domain, a novel prokaryotic, extracellular calcium-binding domain.
[6]
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.
[7]
PubMed ID11844767
JournalJ Bacteriol
Year2002
Volume184
Pages1378-84
AuthorsBelaich A, Parsiegla G, Gal L, Villard C, Haser R, Belaich JP
TitleCel9M, a new family 9 cellulase of the Clostridium cellulolyticum cellulosome.
[8]
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.
Related PDB1g87,1ga2,1k72,1kfg
[9]
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 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).

createdupdated
2004-08-182009-02-26


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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