DB code: M00346

RLCP classification 1.30.36027.984 : Hydrolysis
CATH domain 3.20.20.80 : TIM Barrel Catalytic domain
2.60.40.- : Immunoglobulin-like
2.-.-.- :
1.-.-.- :
-.-.-.- :
E.C. 3.2.1.78
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.20.20.80 : TIM Barrel S00202 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

Uniprot Enzyme Name
UniprotKB Protein name Synonyms CAZy Pfam
Q9XCV5
Man26A
CBM23 (Carbohydrate-Binding Module Family 23)
GH26 (Glycoside Hydrolase Family 26)
PF03425 (CBM_11)
PF02156 (Glyco_hydro_26)
PF00395 (SLH)
[Graphical View]

KEGG enzyme 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

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q9XCV5 Q9XCV5_CELFI

KEGG Pathways
Map code Pathways E.C.
MAP00051 Fructose and mannose metabolism

Compound table
Substrates Products Intermediates
KEGG-id C02492 C00883 C00001 C02492 C00883 I00118
E.C.
Compound 1,4-beta-D-Mannan Galactomannan H2O 1,4-beta-D-Mannan Galactomannan Peptidyl-Glu-D-mannan
Type polysaccharide polysaccharide H2O polysaccharide polysaccharide
ChEBI 27680
15377
27680
PubChem 439336
22247451
962
439336
2bvtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:BMA-BMA-BMA Unbound Unbound
2bvtB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:BMA-BMA-BMA Unbound Unbound
2bvyA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2x2yA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2x2yB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2bvtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2bvtB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2bvyA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2x2yA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2x2yB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Literature [2]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
2bvtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ARG 171;HIS 174;GLU 175;TRP 180;TYR 248;GLU 282;TRP 322
2bvtB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ARG 171;HIS 174;GLU 175;TRP 180;TYR 248;GLU 282;TRP 322
2bvyA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ARG 171;HIS 174;GLU 175;TRP 180;TYR 248;GLU 282;TRP 322
2x2yA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ARG 171;HIS 174;GLU 175;TRP 180;TYR 248;GLU 282;TRP 322
2x2yB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ARG 171;HIS 174;GLU 175;TRP 180;TYR 248;GLU 282;TRP 322
2bvtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2bvtB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2bvyA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2x2yA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2x2yB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
FIGURE 1b
[8]
Fig. 2

References
[1]
Resource
Comments
Medline ID
PubMed ID 10639071
Journal Acc Chem Res
Year 2000
Volume 33
Pages 11-8
Authors Zechel DL, Withers SG
Title Glycosidase mechanisms: anatomy of a finely tuned catalyst.
Related PDB
Related UniProtKB
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 52-514 IN COMPLEX WITH BETA-D-MANNOSE.
Medline ID
PubMed ID 16171384
Journal Biochemistry
Year 2005
Volume 44
Pages 12700-8
Authors Le Nours J, Anderson L, Stoll D, Stalbrand H, Lo Leggio L
Title The structure and characterization of a modular endo-beta-1,4-mannanase from Cellulomonas fimi.
Related PDB 2bvt 2bvy
Related UniProtKB Q9XCV5
[3]
Resource
Comments
Medline ID
PubMed ID
Journal Biocatal Biotransformation
Year 2008
Volume 26
Pages 86-95
Authors Anderson L, Hagglund P, Stoll D, Lo Leggio L, Drakenberg T, Stalbrand H
Title Kinetics and stereochemistry of the Cellulomonas fimi beta-mannanase studied using H-1-NMR.
Related PDB
Related UniProtKB
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 52-514 IN COMPLEX WITH MAGNESIUM.
Medline ID
PubMed ID 20426480
Journal Biochemistry
Year 2010
Volume 49
Pages 4884-96
Authors Hekmat O, Lo Leggio L, Rosengren A, Kamarauskaite J, Kolenova K, Stalbrand H
Title Rational 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 PDB 2x2y
Related UniProtKB Q9XCV5
[5]
Resource
Comments
Medline ID
PubMed ID
Journal Process Biochem
Year 2010
Volume 45
Pages 1203-13
Authors van Zyl WH, Rose SH, Trollope K, Gorgens JF
Title Fungal beta-mannanases: Mannan hydrolysis, heterologous production and biotechnological applications.
Related PDB
Related UniProtKB

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.

Created Updated
2012-02-08 2012-05-15