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Information on EC 3.2.1.4 - cellulase

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EC Tree
     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.4 cellulase
IUBMB Comments
Will also hydrolyse 1,4-linkages in beta-D-glucans also containing 1,3-linkages.
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UNIPROT: Q3LHN3
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
cellulase, cel7a, cellobiohydrolase i, cel5a, cel6a, avicelase, endocellulase, celluclast, cel7b, cbhii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.5 cellulase
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Abscission cellulase
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alkali cellulase
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Alkaline cellulase
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avicelase
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beta-1,4-endoglucan hydrolase
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beta-1,4-glucanase
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Carboxymethyl cellulase
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Carboxymethyl-cellulase
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carboxymethylcellulase
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CEL1
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cellobiohydrolase
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celluase A
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celludextrinase
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Cellulase
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cellulase A 3
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Cellulase E1
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Cellulase E2
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Cellulase E4
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Cellulase E5
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Cellulase SS
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Cellulase V1
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cellulosin AP
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CMCase
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CX-cellulase
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EG1
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EG2
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EG3
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EGA
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EGB
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EGC
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EGCCA
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EGCCC
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EGCCD
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EGCCF
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EGCCG
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EGD
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EGE
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EGF
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EGH
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EGI
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EGIV
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EGM
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EGSS
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EGX
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EGY
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EGZ
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endo-1,4-beta-D-glucanase
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endo-1,4-beta-glucanase
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endo-1,4-beta-glucanase E1
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endo-1,4-beta-glucanase V1
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endocellulase E1
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endoglucanase
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endoglucanase D
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FI-CMCASE
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pancellase SS
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Thermoactive cellulase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
4-beta-D-glucan 4-glucanohydrolase
Will also hydrolyse 1,4-linkages in beta-D-glucans also containing 1,3-linkages.
CAS REGISTRY NUMBER
COMMENTARY hide
9012-54-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acid-swollen cellulose + H2O
?
show the reaction diagram
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?
carboxymethyl cellulose + H2O
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show the reaction diagram
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?
lichenan + H2O
?
show the reaction diagram
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?
oat spelt xylan + H2O
?
show the reaction diagram
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?
additional information
?
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q3LHN3_EUBCE
1148
0
127127
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
127047
x * 127047, the enzyme consists of an N-terminal signal peptide, two glycosyl hydrolase family 5 catalytic modules, two novel carbohydrate-binding modules, two linker sequences, and a C-terminal sequence with an unknown function, MW calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 127047, the enzyme consists of an N-terminal signal peptide, two glycosyl hydrolase family 5 catalytic modules, two novel carbohydrate-binding modules, two linker sequences, and a C-terminal sequence with an unknown function, MW calculated from sequence
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yoda, K.; Toyoda, A.; Mukoyama, Y.; Nakamura, Y.; Minato, H.
Cloning, sequencing, and expression of a Eubacterium cellulosolvens 5 gene encoding an endoglucanase (Cel5A) with novel carbohydrate-binding modules, and properties of Cel5A
Appl. Environ. Microbiol.
71
5787-5793
2005
[Eubacterium] cellulosolvens (Q3LHN3), [Eubacterium] cellulosolvens
Manually annotated by BRENDA team