EzCatDB: D00167
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DB codeD00167
RLCP classification1.30.5050.991 : Hydrolysis
CATH domainDomain 11.50.10.10 : GlycosyltransferaseCatalytic 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 domainD00503,T00245,T00246
1.50.10.10 : GlycosyltransferaseS00531,S00048,S00845,D00500,M00192,T00245,T00246

Enzyme Name
UniProtKBKEGG

Q9EYQ2
Protein name
cellulase
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
SynonymsCellulase Cel9-M
PfamPF00404 (Dockerin_1)
PF00759 (Glyco_hydro_9)
[Graphical view]
CAZyGH9 (Glycoside Hydrolase Family)

KEGG pathways
MAP codePathways
MAP00500Starch and sucrose metabolism

UniProtKB:Accession NumberQ9EYQ2
Entry nameQ9EYQ2_CLOCE
Activity
Subunit
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00038C00760C00478C00551C00001C00760C00551
CompoundZincCelluloseLicheninbeta-D-GlucanH2OCellulosebeta-D-Glucan
Typeheavy metalpolysaccharidecarbohydratepolysaccharideH2Opolysaccharidepolysaccharide
ChEBI29105



15377


PubChem32051

439241
46173706
962
22247451

46173706
               
1ia6ABound:_ZNUnboundUnboundUnbound UnboundUnbound
1ia7ABound:_ZNUnboundUnboundUnbound UnboundBound:GLC-GLC

Active-site residues
resource
PDB;1ia7 & literature [6], [7], [10], [13]
pdbCatalytic residuesCofactor-binding residues
          
1ia6AASP 56;ASP 59;HIS 126;TYR 204;GLU 410
CYS 22;CYS 38;HIS 39;HIS 55(Zinc binding)
1ia7AASP 56;ASP 59;HIS 126;TYR 204;GLU 410
CYS 22;CYS 38;HIS 39;HIS 55(Zinc binding)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[5]p.91
[7]Fig.4, p.814-815
[10]p.11138

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]
CommentsACTIVE SITE HIS-516, AND MUTAGENESIS OF ALL HISTIDINE RESIDUES.
Medline ID91244802
PubMed ID2037583
JournalJ Biol Chem
Year1991
Volume266
Pages10313-8
AuthorsTomme P, Chauvaux S, Beguin P, Millet J, Aubert JP, Claeyssens M
TitleIdentification of a histidyl residue in the active center of endoglucanase D from Clostridium thermocellum.
[3]
CommentsACTIVE SITE ASP-546.
Medline ID92344589
PubMed ID1637316
JournalBiochem J
Year1992
Volume285
Pages319-24
AuthorsTomme P, van Beeumen J, Claeyssens M
TitleModification of catalytically important carboxy residues in endoglucanase D from Clostridium thermocellum.
[4]
CommentsACTIVE SITE GLU-555, AND MUTAGENESIS OF ASPARTIC ACID AND GLUTAMIC ACID RESIDUES.
Medline ID92165798
PubMed ID1537833
JournalJ Biol Chem
Year1992
Volume267
Pages4472-8
AuthorsChauvaux S, Beguin P, Aubert JP
TitleSite-directed mutagenesis of essential carboxylic residues in Clostridium thermocellum endoglucanase CelD.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
JournalNature
Year1992
Volume357
Pages89-91
AuthorsJuy M, Amit AG, Alzari PM, Poljak RJ, Claeyssens M, Beguin P, Aubert J-P
TitleThree-dimensional structure of a thermostable bacterial cellulase.
[6]
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.
[7]
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.
[8]
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.
[9]
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.
[10]
PubMed ID12220178
JournalBiochemistry
Year2002
Volume41
Pages11134-42
AuthorsParsiegla G, Belaich A, Belaich JP, Haser R
TitleCrystal structure of the cellulase Cel9M enlightens structure/function relationships of the variable catalytic modules in glycoside hydrolases.
Related PDB1ia6,1ia7
Related UniProtKBQ9EYQ2
[11]
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.

comments
This enzyme belongs to the glycosidase family-9, with an inverting mechanism.
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 Dockerin domain (PDB;1daq).
Although this enzyme binds a zinc ion and a calcium ion, they are not involved in catalysis.
This enzyme seems to have the same catalytic mechanism as that of its homologous enzymes, endoglucanase (M00192, T00246 in EzCatDB) and cellulase (S00531 in EzCatDB).

createdupdated
2004-08-182009-02-26


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