EzCatDB: S00203
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DB codeS00203
RLCP classification1.30.35885.972 : Hydrolysis
CATH domainDomain 13.20.20.80 : TIM BarrelCatalytic domain
E.C.3.2.1.4

CATH domainRelated DB codes (homologues)
3.20.20.80 : TIM BarrelS00202,S00210,S00748,S00906,S00907,S00911,S00912,S00915,M00134,M00160,D00479,S00204,S00205,S00206,S00207,S00208,S00209,S00211,S00213,S00214,M00113,T00307,D00165,D00166,D00169,D00176,D00501,D00502,D00503,D00844,D00861,D00864,M00026,M00112,M00193,M00346,T00057,T00062,T00063,T00066,T00067

Enzyme Name
UniProtKBKEGG

A3DJ77
Protein nameEndoglucanase Ccellulase
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 C
EgC
Cellulase C
RefSeqYP_001039199.1 (Protein)
NC_009012.1 (DNA/RNA sequence)
PfamPF00150 (Cellulase)
[Graphical view]
CAZyGH5 (Glycoside Hydrolase Family)

KEGG pathways
MAP codePathways
MAP00500Starch and sucrose metabolism

UniProtKB:Accession NumberA3DJ77
Entry nameGUNC_CLOTH
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-idC00760C00001C00478C00551C00760C00551C00185I00120
CompoundCelluloseH2OLicheninbeta-D-GlucanCellulosebeta-D-GlucanCellobiosePeptidyl-Glu-cellulose
TypepolysaccharideH2Ocarbohydratepolysaccharidepolysaccharidepolysaccharidepolysaccharide
ChEBI
15377




17057

PubChem
962
22247451
439241
46173706

46173706
439178

                
1cecAUnbound UnboundUnboundUnboundUnboundUnboundUnbound
1cenAUnbound UnboundUnboundBound:BGC-GLCUnboundUnboundUnbound
1ceoAUnbound UnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
pdbCatalytic residuescomment
          
1cecAARG 46;ASN 139;GLU 140;HIS 198;TYR 200;GLU 280
 
1cenAARG 46;ASN 139;       ;HIS 198;TYR 200;GLU 280
mutant E140Q
1ceoAARG 46;ASN 139;       ;HIS 198;TYR 200;GLU 280
mutant E140Q

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 must have the same catalytic mechanism as that of the other TIM barrel cellulases (D00501, D00502 & D00503 in EzCatDB).
According to the literature [3], Glu282 and Glu162 (of 1ece from D00502 in EzCatDB) act as a nucleophile and acid-base, respectively. The catalysis proceeds through a dissociative-type (or SN1-like) mechanism, with a formation of oxocarbonium ion in the transition state, during the glycosylation of the active site. During the glycosylation, Glu282 approaches the C1 atom of the glcose, whilst Glu162 protonates the leaving group. At the second stage, or during the deglycosylation, a water molecule can be activated by a general base, Glu162. This deglycosylation also goes through the dissociative-type reaction with an oxocarbonium ion in the transition state, in which water replaced the glycosyl leaving group in the first step.
Moreover, comparing the structural data with that of xylanase (E.C. 3.2.1.8) (D00479 in EzCatDB), Tyr240 (of 1ece) might stabilize the leaving nucleophile, Glu282 in deglycosylation, whilst His238 might modulate the activity of Glu162 (see [3]). On the other hand, Tyr240 might modulate the activity of the nucleophile, according to the data of the other homologous enzyme, beta-glucosidase (E.C. 3.2.1.21) (S00205 in EzCatDB).

createdupdated
2002-10-182012-02-14


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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
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