Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.2.1.78 - mannan endo-1,4-beta-mannosidase and Organism(s) Paenibacillus sp. BME-14 and UniProt Accession C6KL35

for references in articles please use BRENDA:EC3.2.1.78
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Paenibacillus sp. BME-14
UNIPROT: C6KL35 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Paenibacillus sp. BME-14
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,4-beta-D-mannan mannanohydrolase
-
-
-
-
beta-1,4-mannan 4-mannanohydrolase
-
-
-
-
beta-D-mannanase
-
-
-
-
Beta-mannanase
-
-
-
-
beta-mannanase B
-
-
-
-
endo-1,4-beta-mannanase
-
-
-
-
endo-1,4-mannanase
-
-
-
-
endo-beta-1,4-mannase
-
-
-
-
endo-beta-mannanase
-
-
-
-
mannanase, endo-1,4-beta-
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
4-beta-D-mannan mannanohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
37288-54-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
konjac glucomannan + H2O
?
show the reaction diagram
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
sequence consists of a carbohydrate binding module belonging to family 6 and a family 26 catalytic domain
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
C6KL35_9BACL
475
1
53600
TrEMBL
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 53600, calculated
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
deletion of the CBM6 domain increases the enzyme stability while enabling it to retain 80% and 60% of its initial activity after treatment at 80°C and 90°C for 30 min
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fu, X.; Huang, X.; Liu, P.; Lin, L.; Wu, G.; Li, C.; Feng, C.; Hong, Y.
Cloning and characterization of a novel mannanase from Paenibacillus sp. BME-14
J. Microbiol. Biotechnol.
20
518-524
2010
Paenibacillus sp. (C6KL35), Paenibacillus sp. BME-14 (C6KL35)
Manually annotated by BRENDA team