EzCatDB: D00503
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DB codeD00503
RLCP classification1.30.35885.972 : Hydrolysis
CATH domainDomain 13.20.20.80 : TIM BarrelCatalytic domain
Domain 21.10.1330.10 : Type 1 dockerin domain
E.C.3.2.1.4

CATH domainRelated DB codes (homologues)
1.10.1330.10 : Type 1 dockerin domainD00167,T00245,T00246
3.20.20.80 : TIM BarrelS00202,S00210,S00748,S00906,S00907,S00911,S00912,S00915,M00134,M00160,D00479,S00204,S00205,S00206,S00207,S00203,S00208,S00209,S00211,S00213,S00214,M00113,T00307,D00165,D00166,D00169,D00176,D00501,D00502,D00844,D00861,D00864,M00026,M00112,M00193,M00346,T00057,T00062,T00063,T00066,T00067

Enzyme Name
UniProtKBKEGG

P17901
Protein nameEndoglucanase Acellulase
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 A
Cellulase A
EGCCA
RefSeqYP_002505438.1 (Protein)
NC_011898.1 (DNA/RNA sequence)
PfamPF00150 (Cellulase)
PF00404 (Dockerin_1)
[Graphical view]
CAZyGH5 (Glycoside Hydrolase Family)

KEGG pathways
MAP codePathways
MAP00500Starch and sucrose metabolism

UniProtKB:Accession NumberP17901
Entry nameGUNA_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

SubstratesProductsintermediates
KEGG-idC00760C00001C00478C00551C00760C00551I00120
CompoundCelluloseH2OLicheninbeta-D-GlucanCellulosebeta-D-GlucanPeptidyl-Glu-cellulose
TypepolysaccharideH2Ocarbohydratepolysaccharidepolysaccharidepolysaccharide
ChEBI
15377





PubChem
962
22247451
439241
46173706

46173706

               
1edgAUnbound UnboundUnboundUnboundUnboundUnbound

Active-site residues
pdbCatalytic residues
         
1edgAARG 79;ASN 169;GLU 170;HIS 254;TYR 256;GLU 307

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]p.10656-10657, Fig.94
[6]Fig.34
[7]Fig.1, Fig.24

references
[1]
CommentsX-ray crystallography (2.15 Angstroms)
Medline ID95393242
PubMed ID7664125
JournalNat Struct Biol
Year1995
Volume2
Pages569-76
AuthorsDominguez R, Souchon H, Spinelli S, Dauter Z, Wilson KS, Chauvaux S, Beguin P, Alzari PM
TitleA common protein fold and similar active site in two distinct families of beta-glycanases.
Related PDB1cec
Related UniProtKBP07985
[2]
CommentsX-ray crystallography (1.64 Angstroms) of 27-406
Medline ID96097400
PubMed ID8535787
JournalStructure
Year1995
Volume3
Pages939-49
AuthorsDucros V, Czjzek M, Belaich A, Gaudin C, Fierobe HP, Belaich JP, Davies GJ, Haser R
TitleCrystal structure of the catalytic domain of a bacterial cellulase belonging to family 5.
Related PDB1edg
Related UniProtKBP17901
[3]
CommentsX-ray crystallography (2.4 Angstroms)
Medline ID96346058
PubMed ID8718854
JournalBiochemistry
Year1996
Volume35
Pages10648-60
AuthorsSakon,J. , Adney,W S. , Himmel,M E. , Thomas,S R. , Karplus,P A
TitleCrystal structure of thermostable family 5 endocellulase E1 from Acidothermus cellulolyticus in complex with cellotetraose.
Related PDB1ece
Related UniProtKBP54583
[4]
CommentsX-ray crystallography (2.3 Angstroms) of mutant GLN-140.
Medline ID96192088
PubMed ID8632467
JournalJ Mol Biol
Year1996
Volume257
Pages1042-51
AuthorsDominguez R, Souchon H, Lascombe M, Alzari PM
TitleThe crystal structure of a family 5 endoglucanase mutant in complexed and uncomplexed forms reveals an induced fit activation mechanism.
Related PDB1cen,1ceo
Related UniProtKBP07985
[5]
Commentsstructure by NMR of 365-426
Medline ID98070232
PubMed ID9405041
JournalBiochemistry
Year1997
Volume36
Pages16074-86
AuthorsBrun E, Moriaud F, Gans P, Blackledge MJ, Barras F, Marion D
TitleSolution structure of the cellulose-binding domain of the endoglucanase Z secreted by Erwinia chrysanthemi.
Related UniProtKBP07103
[6]
CommentsX-ray crystallography (1.57 Angstroms) of 30-329
Medline ID98153671
PubMed ID9485319
JournalBiochemistry
Year1998
Volume37
Pages1926-32
AuthorsDavies GJ, Dauter M, Brzozowski AM, Bjornvad ME, Andersen KV, Schulein M
TitleStructure of the Bacillus agaradherans family 5 endoglucanase at 1.6 A and its cellobiose complex at 2.0 A resolution.
Related PDB1a3h,2a3h
Related UniProtKBO85465
[7]
CommentsX-ray crystallography (1.64 Angstroms) of 30-329
Medline ID98384136
PubMed ID9718293
JournalBiochemistry
Year1998
Volume37
Pages11707-13
AuthorsDavies GJ, Mackenzie L, Varrot A, Dauter M, Brzozowski AM, Schulein M, Withers SG
TitleSnapshots along an enzymatic reaction coordinate: analysis of a retaining beta-glycoside hydrolase.
Related PDB3a3h,4a3h,5a3h,6a3h,7a3h
Related UniProtKBO85465
[8]
CommentsX-ray crystallography (1.75/1.95/2.1 Angstroms)
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.
Related PDB1qhz,1qi0,1qi2
[9]
CommentsX-ray crystallography (2.3 Angstroms) of 44-335
Medline ID21392910
PubMed ID11501995
JournalJ Mol Biol
Year2001
Volume310
Pages1055-66
AuthorsChapon V, Czjzek M, El Hassouni M, Py B, Juy M, Barras F
TitleType II protein secretion in gram-negative pathogenic bacteria: the study of the structure/secretion relationships of the cellulase Cel5 (formerly EGZ) from Erwinia chrysanthemi.
Related UniProtKBP07103
[10]
CommentsX-ray crystallography, catalysis
PubMed ID12079387
JournalJ Mol Biol
Year2002
Volume320
Pages303-9
AuthorsShaw A, Bott R, Vonrhein C, Bricogne G, Power S, Day AG
TitleA novel combination of two classic catalytic schemes.

comments
This family belongs to glycosidase family-5, which has an retaining mechanism (equatorial to equatorial conformation), and also a family of 4/7 superfamily, which has got catalytic residues at the C-terminal ends of beta-4 and beta-7 on the (alpha/beta)8 barrel fold.
This enzyme is composed of the N-terminal catalytic domain and the C-terminal Dockerin repeat. Although the structure of the Dockerin repeat region has not been determined yet, it must have a similar structure to that of 1daq (PDB), which belongs to P38686 (Swiss-prot).
This enzyme must have the same catalytic mechanism as that of the other TIM barrel cellulases (S00203, D00501 & D00502 in EzCatDB).

createdupdated
2002-10-182012-02-14


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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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