EzCatDB: M00346
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DB codeM00346
RLCP classification1.30.36027.984 : Hydrolysis
CATH domainDomain 13.20.20.80 : TIM BarrelCatalytic domain
Domain 22.60.40.- : Immunoglobulin-like
Domain 32.-.-.-
Domain 41.-.-.-
Domain 5-.-.-.-
E.C.3.2.1.78

CATH domainRelated DB codes (homologues)
3.20.20.80 : TIM BarrelS00202,S00210,S00748,S00906,S00907,S00911,S00912,S00915,M00134,M00160,D00479,S00204,S00205,S00206,S00207,S00203,S00208,S00209,S00211,S00213,S00214,M00113,T00307,D00165,D00166,D00169,D00176,D00501,D00502,D00503,D00844,D00861,D00864,M00026,M00112,M00193,T00057,T00062,T00063,T00066,T00067

Enzyme Name
UniProtKBKEGG

Q9XCV5
Protein name
Mannan endo-1,4-beta-mannosidase
Endo-1,4-beta-mannanase
Endo-beta-1,4-mannase
Beta-mannanase B
Beta-1, 4-mannan 4-mannanohydrolase
Endo-beta-mannanase
Beta-D-mannanase
1,4-beta-D-mannan mannanohydrolase
SynonymsMan26A
PfamPF03425 (CBM_11)
PF02156 (Glyco_hydro_26)
PF00395 (SLH)
[Graphical view]
CAZyGH26 (Glycoside Hydrolase Family)

KEGG pathways
MAP codePathways
MAP00051Fructose and mannose metabolism

UniProtKB:Accession NumberQ9XCV5
Entry nameQ9XCV5_CELFI
Activity
Subunit
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC02492C00883C00001C02492C00883I00118
Compound1,4-beta-D-MannanGalactomannanH2O1,4-beta-D-MannanGalactomannanPeptidyl-Glu-D-mannan
TypepolysaccharidepolysaccharideH2Opolysaccharidepolysaccharide
ChEBI
27680
15377

27680

PubChem
439336
962
22247451

439336

              
2bvtA01UnboundUnbound Analogue:BMA-BMA-BMAUnboundUnbound
2bvtB01UnboundUnbound Analogue:BMA-BMA-BMAUnboundUnbound
2bvyA01UnboundUnbound UnboundUnboundUnbound
2x2yA01UnboundUnbound UnboundUnboundUnbound
2x2yB01UnboundUnbound UnboundUnboundUnbound
2bvtA02UnboundUnbound UnboundUnboundUnbound
2bvtB02UnboundUnbound UnboundUnboundUnbound
2bvyA02UnboundUnbound UnboundUnboundUnbound
2x2yA02UnboundUnbound UnboundUnboundUnbound
2x2yB02UnboundUnbound UnboundUnboundUnbound

Active-site residues
resource
Literature [2]
pdbCatalytic residues
         
2bvtA01ARG 171;HIS 174;GLU 175;TRP 180;TYR 248;GLU 282;TRP 322
2bvtB01ARG 171;HIS 174;GLU 175;TRP 180;TYR 248;GLU 282;TRP 322
2bvyA01ARG 171;HIS 174;GLU 175;TRP 180;TYR 248;GLU 282;TRP 322
2x2yA01ARG 171;HIS 174;GLU 175;TRP 180;TYR 248;GLU 282;TRP 322
2x2yB01ARG 171;HIS 174;GLU 175;TRP 180;TYR 248;GLU 282;TRP 322
2bvtA02 
2bvtB02 
2bvyA02 
2x2yA02 
2x2yB02 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]FIGURE 1b
[8]Fig. 2

references
[1]
PubMed ID10639071
JournalAcc Chem Res
Year2000
Volume33
Pages11-8
AuthorsZechel DL, Withers SG
TitleGlycosidase mechanisms: anatomy of a finely tuned catalyst.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 52-514 IN COMPLEX WITH BETA-D-MANNOSE.
PubMed ID16171384
JournalBiochemistry
Year2005
Volume44
Pages12700-8
AuthorsLe Nours J, Anderson L, Stoll D, Stalbrand H, Lo Leggio L
TitleThe structure and characterization of a modular endo-beta-1,4-mannanase from Cellulomonas fimi.
Related PDB2bvt,2bvy
Related UniProtKBQ9XCV5
[3]
JournalBiocatal Biotransformation
Year2008
Volume26
Pages86-95
AuthorsAnderson L, Hagglund P, Stoll D, Lo Leggio L, Drakenberg T, Stalbrand H
TitleKinetics and stereochemistry of the Cellulomonas fimi beta-mannanase studied using H-1-NMR.
[4]
CommentsX-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 52-514 IN COMPLEX WITH MAGNESIUM.
PubMed ID20426480
JournalBiochemistry
Year2010
Volume49
Pages4884-96
AuthorsHekmat O, Lo Leggio L, Rosengren A, Kamarauskaite J, Kolenova K, Stalbrand H
TitleRational engineering of mannosyl binding in the distal glycone subsites of Cellulomonas fimi endo-beta-1,4-mannanase: mannosyl binding promoted at subsite -2 and demoted at subsite -3.
Related PDB2x2y
Related UniProtKBQ9XCV5
[5]
JournalProcess Biochem
Year2010
Volume45
Pages1203-13
Authorsvan Zyl WH, Rose SH, Trollope K, Gorgens JF
TitleFungal beta-mannanases: Mannan hydrolysis, heterologous production and biotechnological applications.

comments
This enzyme belongs to the glycosidase family-26, which adopts (alpha/beta)8 barrel structure.
This enzyme is composed of the N-terminal catalytic domain, which belongs to the glycosidase family-26 with (alpha/beta)8 barrel domain, Immunoglobulin-like domain (Ig-like), carbohydrate-binding module family-23 (CBM23), and S-layer homology domain (SLH), and the C-terminal region. Only the structures of the N-terminal two domains, the catalytic domain and Ig-like domain, have been elucidated.
The enzymes in family-26 hydrolyzes only mannan and galactomannan, whereas the counterpart enzymes from family-5 hydrolyze glucomannan as well as mannnan and galactomannan.
Moreover, a homologous enzyme (S00915 in EzCatDB) is an exo-acting mannanase, producing disaccharide, mannobiose, or galactomannobiose, from the non-reducing end of mannan or galactomannan, whereas this enzyme and other homologous enzyme (S00911 in EzCatDB) are endo-mannanases.
Since this enzyme has got the same active site as those from family-26 beta-mannanases (S00911 and S00915 in EzCatDB), this enzyme can catalyze the same reaction as those homologous enzymes.

createdupdated
2012-02-082012-05-15


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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