EzCatDB: D00502
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DB codeD00502
RLCP classification1.30.35885.972 : Hydrolysis
CATH domainDomain 13.20.20.80 : TIM BarrelCatalytic domain
Domain 22.60.40.290 : Immunoglobulin-like
E.C.3.2.1.4

CATH domainRelated DB codes (homologues)
2.60.40.290 : Immunoglobulin-likeM00219,D00479,D00504,M00026,M00192
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,D00503,D00844,D00861,D00864,M00026,M00112,M00193,M00346,T00057,T00062,T00063,T00066,T00067

Enzyme Name
UniProtKBKEGG

P54583
Protein nameEndoglucanase E1cellulase
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 E1
Cellulase E1
Endocellulase E1
RefSeqYP_872373.1 (Protein)
NC_008578.1 (DNA/RNA sequence)
PfamPF00553 (CBM_2)
PF00150 (Cellulase)
[Graphical view]
CAZyGH5 (Glycoside Hydrolase Family)

KEGG pathways
MAP codePathways
MAP00500Starch and sucrose metabolism

UniProtKB:Accession NumberP54583
Entry nameGUN1_ACIC1
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

               
1c0dAUnbound UnboundUnboundUnboundUnboundUnbound
1c0dBUnbound UnboundUnboundUnboundUnboundUnbound
1eceAAnalogue:GLC-GLC-GLC-GLC UnboundBound:GLC-GLC-GLC-GLCUnboundUnboundUnbound
1eceBAnalogue:GLC-GLC-GLC-GLC UnboundBound:GLC-GLC-GLC-GLCUnboundUnboundUnbound
1vrxAUnbound UnboundUnboundUnboundUnboundUnbound
1vrxBUnbound UnboundUnboundUnboundUnboundUnbound

Active-site residues
pdbCatalytic residues
         
1c0dAARG 62;ASN 161;GLU 162;HIS 238;TYR 240;GLU 282
1c0dBARG 62;ASN 161;GLU 162;HIS 238;TYR 240;GLU 282
1eceAARG 62;ASN 161;GLU 162;HIS 238;TYR 240;GLU 282
1eceBARG 62;ASN 161;GLU 162;HIS 238;TYR 240;GLU 282
1vrxAARG 62;ASN 161;GLU 162;HIS 238;TYR 240;GLU 282
1vrxBARG 62;ASN 161;GLU 162;HIS 238;TYR 240;GLU 282

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.
[11]
PubMed ID15917594
JournalAppl Biochem Biotechnol
Year2005
Volume121-124
Pages129-48
AuthorsBaker JO, McCarley JR, Lovett R, Yu CH, Adney WS, Rignall TR, Vinzant TB, Decker SR, Sakon J, Himmel ME
TitleCatalytically enhanced endocellulase Cel5A from Acidothermus cellulolyticus.
Related PDB1c0d,1vrx

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 Cellulose-binding domain. The structure of the C-terminal domain has not been determined yet.
This enzyme must have the same catalytic mechanism as that of the other TIM barrel cellulases (S00203, D00501 & D00503 in EzCatDB).
According to the literature [3], Glu282 and Glu162 (of 1ece) 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 BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
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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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