D00501
type: Enzyme
rlcp: p972
cath: TIM Barrel
cath: Seminal Fluid Protein PDC-109 (Domain B)
ec: https://purl.uniprot.org/enzyme/3.2.1.4
uniprot: P07103
uniprot: P06565
uniprot: O85465
kegg enzyme: cellulase
kegg enzyme: endo-1,4-beta-D-glucanase
kegg enzyme: beta-1,4-glucanase
kegg enzyme: beta-1,4-endoglucan hydrolase
kegg enzyme: celluase A
kegg enzyme: cellulosin AP
kegg enzyme: endoglucanase D
kegg enzyme: alkali cellulase
kegg enzyme: cellulase A 3
kegg enzyme: celludextrinase
kegg enzyme: 9.5 cellulase
kegg enzyme: avicelase
kegg enzyme: pancellase SS
kegg enzyme: 1,4-(1,3
kegg enzyme: 1,4)-beta-D-glucan 4-glucanohydrolase
kegg pathway: Starch and sucrose metabolism
kegg substrate: Cellulose
kegg substrate: H2O
kegg substrate: Lichenin
kegg substrate: beta-D-Glucan
kegg product: Cellulose
kegg product: Cellobiose
kegg intermediate: Peptidyl-Glu-cellulose
pdb: 1egzA
pdb: 1egzB
pdb: 1egzC
pdb: 1qhzA
pdb: 1qi0A
pdb: 1qi2A
pdb: 4a3hA
pdb: 8a3hA
pdb: 1a3hA
pdb: 2a3hA
pdb: 3a3hA
pdb: 5a3hA
pdb: 6a3hA
pdb: 7a3hA
pdb bound state: Unbound
  compound: Cellulose
  pdb: 1egzA
pdb bound state: Unbound
  compound: Cellulose
  pdb: 1egzB
pdb bound state: Unbound
  compound: Cellulose
  pdb: 1egzC
pdb bound state: Unbound
  compound: Cellulose
  pdb: 1qhzA
pdb bound state: Unbound
  compound: Cellulose
  pdb: 1qi0A
pdb bound state: Unbound
  compound: Cellulose
  pdb: 1qi2A
pdb bound state: Analogue
  compound: Cellulose
  pdb: 4a3hA
  ligand het code: DCB
pdb bound state: Unbound
  compound: Cellulose
  pdb: 8a3hA
pdb bound state: Unbound
  compound: Cellulose
  pdb: 1a3hA
pdb bound state: Unbound
  compound: Cellulose
  pdb: 2a3hA
pdb bound state: Unbound
  compound: Cellulose
  pdb: 3a3hA
pdb bound state: Unbound
  compound: Cellulose
  pdb: 5a3hA
pdb bound state: Unbound
  compound: Cellulose
  pdb: 6a3hA
pdb bound state: Unbound
  compound: Cellulose
  pdb: 7a3hA
pdb bound state: Unbound
  compound: Lichenin
  pdb: 1egzA
pdb bound state: Unbound
  compound: Lichenin
  pdb: 1egzB
pdb bound state: Unbound
  compound: Lichenin
  pdb: 1egzC
pdb bound state: Unbound
  compound: Lichenin
  pdb: 1qhzA
pdb bound state: Unbound
  compound: Lichenin
  pdb: 1qi0A
pdb bound state: Unbound
  compound: Lichenin
  pdb: 1qi2A
pdb bound state: Unbound
  compound: Lichenin
  pdb: 4a3hA
pdb bound state: Unbound
  compound: Lichenin
  pdb: 8a3hA
pdb bound state: Unbound
  compound: Lichenin
  pdb: 1a3hA
pdb bound state: Unbound
  compound: Lichenin
  pdb: 2a3hA
references: A common protein fold and similar active site in two distinct families of beta-glycanases.
references: Crystal structure of the catalytic domain of a bacterial cellulase belonging to family 5.
references: Crystal structure of thermostable family 5 endocellulase E1 from Acidothermus cellulolyticus in complex with cellotetraose.
references: The crystal structure of a family 5 endoglucanase mutant in complexed and uncomplexed forms reveals an induced fit activation mechanism.
references: Solution structure of the cellulose-binding domain of the endoglucanase Z secreted by Erwinia chrysanthemi.
references: Structure of the Bacillus agaradherans family 5 endoglucanase at 1.6 A and its cellobiose complex at 2.0 A resolution.
references: Snapshots along an enzymatic reaction coordinate: analysis of a retaining beta-glycoside hydrolase.
references: Insights into ligand-induced conformational change in Cel5A from Bacillus agaradhaerens revealed by a catalytically active crystal form.
references: Type II protein secretion in gram-negative pathogenic bacteria: the study of the structure/secretion relationships of the cellulase Cel5 (formerly EGZ) from Erwinia chrysanthemi.
references: A novel combination of two classic catalytic schemes.
comment: 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, D00502 & D00503 in EzCatDB).

TIM Barrel
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.20.20.80
catalytic domain: index.html

Seminal Fluid Protein PDC-109 (Domain B)
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.10.10.20

Starch and sucrose metabolism
type: KeggPathway
references: KEGG:MAP00500

Cellulose
type: KeggSubstrate
references: KEGG:C00760
compound type: polysaccharide
type: KeggProduct

H2O
type: KeggSubstrate
references: KEGG:C00001
compound type: H2O
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Lichenin
type: KeggSubstrate
references: KEGG:C00478
compound type: carbohydrate
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

beta-D-Glucan
type: KeggSubstrate
references: KEGG:C00551
compound type: polysaccharide
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Cellobiose
type: KeggProduct
references: KEGG:C00185
compound type: polysaccharide
references: CHEBI:17057
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Peptidyl-Glu-cellulose
type: KeggIntermediate
references: KEGG:I00120

1egzA
type: Pdb
references: 1egz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1egz
catalytic residue: ARG 57;ASN 132;GLU 133;HIS 192;TYR 194;GLU 220

1egzB
type: Pdb
references: 1egz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1egz
catalytic residue: ARG 57;ASN 132;GLU 133;HIS 192;TYR 194;GLU 220

1egzC
type: Pdb
references: 1egz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1egz
catalytic residue: ARG 57;ASN 132;GLU 133;HIS 192;TYR 194;GLU 220

1qhzA
type: Pdb
references: 1qhz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qhz
catalytic residue: ARG 62;ASN 138;GLU 139;HIS 200;TYR 202;GLU 228

1qi0A
type: Pdb
references: 1qi0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qi0
catalytic residue: ARG 62;ASN 138;GLU 139;HIS 200;TYR 202;GLU 228

1qi2A
type: Pdb
references: 1qi2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qi2
catalytic residue: ARG 62;ASN 138;GLU 139;HIS 200;TYR 202;GLU 228

4a3hA
type: Pdb
references: 4a3h
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4a3h
catalytic residue: ARG 62;ASN 138;GLU 139;HIS 200;TYR 202;GLU 228

8a3hA
type: Pdb
references: 8a3h
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:8a3h
catalytic residue: ARG 62;ASN 138;GLU 139;HIS 200;TYR 202;GLU 228

1a3hA
type: Pdb
references: 1a3h
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a3h
catalytic residue: ARG 62;ASN 138;GLU 139;HIS 200;TYR 202;GLU 228

2a3hA
type: Pdb
references: 2a3h
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2a3h
catalytic residue: ARG 62;ASN 138;GLU 139;HIS 200;TYR 202;GLU 228

3a3hA
type: Pdb
references: 3a3h
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3a3h
catalytic residue: ARG 62;ASN 138;GLU 139;HIS 200;TYR 202;GLU 228

5a3hA
type: Pdb
references: 5a3h
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5a3h
catalytic residue: ARG 62;ASN 138;GLU 139;HIS 200;TYR 202;GLU 228

6a3hA
type: Pdb
references: 6a3h
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:6a3h
catalytic residue: ARG 62;ASN 138;GLU 139;HIS 200;TYR 202;GLU 228

7a3hA
type: Pdb
references: 7a3h
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:7a3h
catalytic residue: ARG 62;ASN 138;GLU 139;HIS 200;TYR 202;GLU 228

A common protein fold and similar active site in two distinct families of beta-glycanases.
type: BibliographicResource
comment: X-ray crystallography (2.15 Angstroms)
medline id: 95393242
references: http://www.ncbi.nlm.nih.gov/pubmed/7664125
journal: Nat Struct Biol
volume: 2
pages: 569-76
published year: 1995
authors:
  item: Dominguez R
  item: Souchon H
  item: Spinelli S
  item: Dauter Z
  item: Wilson KS
  item: Chauvaux S
  item: Beguin P
  item: Alzari PM
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P07985

Crystal structure of the catalytic domain of a bacterial cellulase belonging to family 5.
type: BibliographicResource
comment: X-ray crystallography (1.64 Angstroms) of 27-406
medline id: 96097400
references: http://www.ncbi.nlm.nih.gov/pubmed/8535787
journal: Structure
volume: 3
pages: 939-49
published year: 1995
authors:
  item: Ducros V
  item: Czjzek M
  item: Belaich A
  item: Gaudin C
  item: Fierobe HP
  item: Belaich JP
  item: Davies GJ
  item: Haser R
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P17901

Crystal structure of thermostable family 5 endocellulase E1 from Acidothermus cellulolyticus in complex with cellotetraose.
type: BibliographicResource
comment: X-ray crystallography (2.4 Angstroms)
medline id: 96346058
references: http://www.ncbi.nlm.nih.gov/pubmed/8718854
journal: Biochemistry
volume: 35
pages: 10648-60
published year: 1996
authors:
  item: Sakon
  item: J.
  item: Adney
  item: W S.
  item: Himmel
  item: M E.
  item: Thomas
  item: S R.
  item: Karplus
  item: P A
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P54583

The crystal structure of a family 5 endoglucanase mutant in complexed and uncomplexed forms reveals an induced fit activation mechanism.
type: BibliographicResource
comment: X-ray crystallography (2.3 Angstroms) of mutant GLN-140.
medline id: 96192088
references: http://www.ncbi.nlm.nih.gov/pubmed/8632467
journal: J Mol Biol
volume: 257
pages: 1042-51
published year: 1996
authors:
  item: Dominguez R
  item: Souchon H
  item: Lascombe M
  item: Alzari PM
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P07985

Solution structure of the cellulose-binding domain of the endoglucanase Z secreted by Erwinia chrysanthemi.
type: BibliographicResource
comment: structure by NMR of 365-426
medline id: 98070232
references: http://www.ncbi.nlm.nih.gov/pubmed/9405041
journal: Biochemistry
volume: 36
pages: 16074-86
published year: 1997
authors:
  item: Brun E
  item: Moriaud F
  item: Gans P
  item: Blackledge MJ
  item: Barras F
  item: Marion D
references: P07103

Structure of the Bacillus agaradherans family 5 endoglucanase at 1.6 A and its cellobiose complex at 2.0 A resolution.
type: BibliographicResource
comment: X-ray crystallography (1.57 Angstroms) of 30-329
medline id: 98153671
references: http://www.ncbi.nlm.nih.gov/pubmed/9485319
journal: Biochemistry
volume: 37
pages: 1926-32
published year: 1998
authors:
  item: Davies GJ
  item: Dauter M
  item: Brzozowski AM
  item: Bjornvad ME
  item: Andersen KV
  item: Schulein M
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: O85465

Snapshots along an enzymatic reaction coordinate: analysis of a retaining beta-glycoside hydrolase.
type: BibliographicResource
comment: X-ray crystallography (1.64 Angstroms) of 30-329
medline id: 98384136
references: http://www.ncbi.nlm.nih.gov/pubmed/9718293
journal: Biochemistry
volume: 37
pages: 11707-13
published year: 1998
authors:
  item: Davies GJ
  item: Mackenzie L
  item: Varrot A
  item: Dauter M
  item: Brzozowski AM
  item: Schulein M
  item: Withers SG
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: O85465

Insights into ligand-induced conformational change in Cel5A from Bacillus agaradhaerens revealed by a catalytically active crystal form.
type: BibliographicResource
comment: X-ray crystallography (1.75/1.95/2.1 Angstroms)
references: http://www.ncbi.nlm.nih.gov/pubmed/10731432
journal: J Mol Biol
volume: 297
pages: 819-28
published year: 2000
authors:
  item: Varrot A
  item: Schulein M
  item: Davies GJ
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Type II protein secretion in gram-negative pathogenic bacteria: the study of the structure/secretion relationships of the cellulase Cel5 (formerly EGZ) from Erwinia chrysanthemi.
type: BibliographicResource
comment: X-ray crystallography (2.3 Angstroms) of 44-335
medline id: 21392910
references: http://www.ncbi.nlm.nih.gov/pubmed/11501995
journal: J Mol Biol
volume: 310
pages: 1055-66
published year: 2001
authors:
  item: Chapon V
  item: Czjzek M
  item: El Hassouni M
  item: Py B
  item: Juy M
  item: Barras F
references: P07103

A novel combination of two classic catalytic schemes.
type: BibliographicResource
comment: X-ray crystallography, catalysis
references: http://www.ncbi.nlm.nih.gov/pubmed/12079387
journal: J Mol Biol
volume: 320
pages: 303-9
published year: 2002
authors:
  item: Shaw A
  item: Bott R
  item: Vonrhein C
  item: Bricogne G
  item: Power S
  item: Day AG

Analogue
compound: beta-D-Glucan
pdb: 4a3hA
ligand het code: DCB

Analogue
compound: Cellobiose
pdb: 8a3hA
ligand het code: IDC

Bound
compound: Cellobiose
pdb: 2a3hA
ligand het code: CTR

IntermediateAnalogue
compound: Peptidyl-Glu-cellulose
pdb: 1qi2A
ligand het code: FCT

IntermediateAnalogue
compound: Peptidyl-Glu-cellulose
pdb: 5a3hA
ligand het code: FFC

IntermediateAnalogue
compound: Peptidyl-Glu-cellulose
pdb: 6a3hA
ligand het code: FCT

ReferenceForCatalyticMechanism
reference index: 3
reference section: p.10656-10657, Fig.9
reference step: 4

ReferenceForCatalyticMechanism
reference index: 6
reference section: Fig.3
reference step: 4

ReferenceForCatalyticMechanism
reference index: 7
reference section: Fig.1, Fig.2
reference step: 4