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Information on EC 3.2.1.78 - mannan endo-1,4-beta-mannosidase and Organism(s) Thermotoga petrophila and UniProt Accession A5IMX7
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EC Tree
3.2.1.78 mannan endo-1,4-beta-mannosidaseSpecify your search results
Word Map
- 3.2.1.78
- mannans
- galactomannans
- locust
- glucomannans
- guar
- konjac
- mannobiose
- alpha-galactosidase
- reesei
- manno-oligosaccharides
- carob
- radicle
-
micropylar
-
mannan-degrading
-
ivory
-
kraft
- mannotetraose
- beta-mannans
- mannopentaose
-
hemicellulase
-
softwood
-
endohydrolases
- cellulosome
- cellvibrio
- endo-1,4-beta-glucanase
-
copra
-
thermomonospora
-
mannan-binding
- food industry
- agriculture
- synthesis
- pharmacology
- degradation
- biotechnology
- paper production
- nutrition
- medicine
- industry
- drug development
The taxonomic range for the selected organisms is: Thermotoga petrophila
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
beta-mannanase, endo-beta-mannanase, man5a, endo-mannanase, manb-1601, man26a, endo-beta-1,4-mannanase, man26b, man5c, endo-1,4-beta-mannanase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,4-beta-D-mannan mannanohydrolase
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beta-1,4-mannan 4-mannanohydrolase
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beta-D-mannanase
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Beta-mannanase
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beta-mannanase B
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endo-1,4-beta-mannanase
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endo-1,4-mannanase
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endo-beta-1,4-mannase
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endo-beta-mannanase
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mannanase, endo-1,4-beta-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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SYSTEMATIC NAME
IUBMB Comments
4-beta-D-mannan mannanohydrolase
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CAS REGISTRY NUMBER
COMMENTARY
37288-54-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
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the enzyme catalyzes the hydrolysis of beta-1,4-mannoside linkages in various mannan-containing polysaccharides, such as glucomannans and galactomannans. Protein-ligand interactions from crystal structure analysis, circular dichroism spectroscopy, overview
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?
additional information
?
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the enzyme catalyzes the hydrolysis of beta-1,4-mannoside linkages in various mannan-containing polysaccharides, such as glucomannans and galactomannans. Protein-ligand interactions from crystal structure analysis, circular dichroism spectroscopy, overview
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
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the enzyme catalyzes the hydrolysis of beta-1,4-mannoside linkages in various mannan-containing polysaccharides, such as glucomannans and galactomannans. Protein-ligand interactions from crystal structure analysis, circular dichroism spectroscopy, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the hydrolysis of beta-1,4-mannoside linkages in various mannan-containing polysaccharides, such as glucomannans and galactomannans. Protein-ligand interactions from crystal structure analysis, circular dichroism spectroscopy, overview
-
-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from the Kubiki oil reservoir in Niigata (Japan)
UniProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
the temperature range for growth is 47-88°C with an optimum at 80°C
additional information
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the temperature range for growth is 47-88°C with an optimum at 80°C
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the glycosyl hydrolase family 5, GH5
physiological function
the enzyme beta-mannanase is responsible for the cleavage of beta-1,4-linked internal linkages of the mannan polymer to produce new chain ends
additional information
additional information
the enzyme is composed of three distinct domains and shows some level of molecular flexibility in solution, nevertheless it has a preferred conformation, which can be described by the rigid-body modeling procedure, structure analysis. The enzyme contains a linker with a compact structure that occupies a small volume with respect to its large number of amino acids, role of the length and flexibility of the linker on the spatial arrangement of the constitutive domains. The linker can optimize the geometry between the other two domains with respect to the substrate at high temperatures. The hydrodynamic radii of full-length enzyme and single catalytic domain are independent of protein concentration over the range 0.5 to 8 mg/ml at 20°C and pH 6
additional information
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the enzyme is composed of three distinct domains and shows some level of molecular flexibility in solution, nevertheless it has a preferred conformation, which can be described by the rigid-body modeling procedure, structure analysis. The enzyme contains a linker with a compact structure that occupies a small volume with respect to its large number of amino acids, role of the length and flexibility of the linker on the spatial arrangement of the constitutive domains. The linker can optimize the geometry between the other two domains with respect to the substrate at high temperatures. The hydrodynamic radii of full-length enzyme and single catalytic domain are independent of protein concentration over the range 0.5 to 8 mg/ml at 20°C and pH 6
additional information
the structure of the catalytic domain reveals a canonical (alpha/beta)8-barrel scaffold surrounded by loops and short helices that form the catalytic interface, subsites forming the active-site cleft with residues W134, E198, R200, E235, H283 and W284 are directly involved in glucose binding, structure analysis of full-length enzyme and catalytic domain, overview
additional information
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the structure of the catalytic domain reveals a canonical (alpha/beta)8-barrel scaffold surrounded by loops and short helices that form the catalytic interface, subsites forming the active-site cleft with residues W134, E198, R200, E235, H283 and W284 are directly involved in glucose binding, structure analysis of full-length enzyme and catalytic domain, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme shows some level of molecular flexibility in solution and is composed of three distinct domains, a GH5 catalytic domain (373 amino acid residues) and a carbohydrate-binding domain (172 amino acid residues) connected through a linker (102 amino acid residues). Secondary structure, overview
additional information
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the enzyme shows some level of molecular flexibility in solution and is composed of three distinct domains, a GH5 catalytic domain (373 amino acid residues) and a carbohydrate-binding domain (172 amino acid residues) connected through a linker (102 amino acid residues). Secondary structure, overview
additional information
the two-domain enzyme encompasses a GH5 catalytic domain with a C-terminal CBM27 accessory domain, structure analysis and comparisons, overview
additional information
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the two-domain enzyme encompasses a GH5 catalytic domain with a C-terminal CBM27 accessory domain, structure analysis and comparisons, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization of catalytic domain. Crystals from conditions with phosphate or citrate salts as precipitant belong to space group P212121, resolution to 1.4 A, while a crystal from a condition with ethanol as precipitant belongs to space group I212121, resolution to 1.45 A
purified recombinant His-tagged full-length enzyme and catalytic domain, X-ray diffraction structure determination and analysis by dynamic light scattering and small-angle X-ray scattering. molecular modelling
purified recombinant isolated His-tagged catalytic domain in apoform and complexed with iodine, glucose, maltose, and maltose + gycerol, sitting drop vapor diffusion method, mixing of 0.0005 ml of 12 mg/ml protein in 25 mM Tris-HCl, pH 7.5, with 0.0005 ml of precipitant solution containing 0.1 M citrate, pH 5.5, 1 M ammonium phosphate, and 0.2 M sodium chloride, 20°C, soaking of crystals in ligand solutions, X-ray diffraction structure determination and analysis at 1.40-1,92 A resolution
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
85
pH 6.0, the full-length enzyme is completely stable, while the isolated catalytic domain starts to precipitate
additional information
additional information
the CBM27 accessory domain is critical for thermal stability, it reduces the melting temperature from 100°C to 88°C
additional information
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the CBM27 accessory domain is critical for thermal stability, it reduces the melting temperature from 100°C to 88°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged full-length enzyme and catalytic domain by nickel affinity chromatography
recombinant His-tagged full-length enzyme and isolated catalytic domain from Escerichia coli strain BL21(DE3)DELTASlyD by nickel affinity chromatography, gel filtration, and ultrafiltration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Tpet_1542, recombinant expression of His-tagged full-length enzyme and isolated catalytic domain in Escerichia coli strain BL21(DE3)DELTASlyD
recombinant expression of His-tagged full-length enzyme and catalytic domain
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Santos, C.R.; Squina, F.M.; Navarro, A.M.; Ruller, R.; Prade, R.; Murakami, M.T.
Cloning, expression, purification, crystallization and preliminary X-ray diffraction studies of the catalytic domain of a hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1
Acta Crystallogr. Sect. F
66
1078-1081
2010
Thermotoga petrophila (A5IMX7), Thermotoga petrophila RKU-1 (A5IMX7), Thermotoga petrophila RKU-1
dos Santos, C.; Paiva, J.; Meza, A.; Cota, J.; Alvarez, T.; Ruller, R.; Prade, R.; Squina, F.; Murakami, M.
Molecular insights into substrate specificity and thermal stability of a bacterial GH5-CBM27 endo-1,4-beta-D-mannanase
J. Struct. Biol.
177
469-476
2012
Thermotoga petrophila (A5IMX7), Thermotoga petrophila, Thermotoga petrophila RKU-1 (A5IMX7)
da Silva, V.M.; Colussi, F.; de Oliveira Neto, M.; Braz, A.S.; Squina, F.M.; Oliveira, C.L.; Garcia, W.
Modular hyperthermostable bacterial endo-beta-1,4-mannanase: molecular shape, flexibility and temperature-dependent conformational changes
PLoS ONE
9
e92996
2014
Thermotoga petrophila (A5IMX7), Thermotoga petrophila, Thermotoga petrophila RKU-1 (A5IMX7)
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Release 2023.1 (January 2023)
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