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Information on EC 3.2.1.78 - mannan endo-1,4-beta-mannosidase and Organism(s) Rhodothermus marinus and UniProt Accession P49425

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This record set is specific for:
Rhodothermus marinus
UNIPROT: P49425 not found.
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Word Map
The taxonomic range for the selected organisms is: Rhodothermus marinus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
beta-mannanase, endo-beta-mannanase, man5a, endo-mannanase, manb-1601, endo-beta-1,4-mannanase, man26a, man26b, man5c, caman, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
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 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-mannan mannanohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
37288-54-3
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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
carob-galactomannan + H2O
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show the reaction diagram
i.e. locust bean gum
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?
guar gum + H2O
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show the reaction diagram
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?
additional information
?
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requires at least five sugar moieties for effective catalytic activity, no substrate: yeast mannan
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?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ATCC 43812
Swissprot
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
113000
x * 113000, deduced from gene sequence, upon expression in Escherichia coli, two fragments of 45000 and 50000 Da
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 113000, deduced from gene sequence, upon expression in Escherichia coli, two fragments of 45000 and 50000 Da
additional information
C-terminal domain of 550 amino acid residues with homology to glycosidase family 26
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
1 h, 70% residual activity, truncated protein fragments produced in Escherichia coli, 1 h, 87% residual activity, protein derived from Rhodothermus marinus
90
1 h, 25% residual activity, truncated protein fragments produced in Escherichia coli
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Politz, O.; Krah, M.; Thomsen, K.K.; Borriss, R.
A highly thermostable endo-(1,4)-beta-mannanase from the marine bacterium Rhodothermus marinus
Appl. Microbiol. Biotechnol.
53
715-721
2000
Rhodothermus marinus (P49425)
Manually annotated by BRENDA team