DB code: M00219

CATH domain 2.60.120.- : Jelly Rolls Catalytic domain
2.60.40.290 : Immunoglobulin-like
3.-.-.- : Catalytic domain
2.60.40.290 : Immunoglobulin-like
E.C. 3.2.1.8 3.5.1.-
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
2.60.40.290 : Immunoglobulin-like D00479 D00502 D00504 M00026 M00192

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Includes CAZy Pfam
P54865 Bifunctional xylanase/deacetylase
None Endo-1,4-beta-xylanase D
(Xylanase D)
(XYLD)
EC 3.2.1.8
Acetylated xylan deacetylase
EC 3.5.1.-
CBM2 (Carbohydrate-Binding Module Family 2)
GH11 (Glycoside Hydrolase Family 11)
PF00553 (CBM_2)
PF00457 (Glyco_hydro_11)
PF01522 (Polysacc_deac_1)
[Graphical View]

KEGG enzyme name
endo-1,4-beta-xylanase
(EC 3.2.1.8 )
endo-(1->4)-beta-xylan 4-xylanohydrolase
(EC 3.2.1.8 )
endo-1,4-xylanase
(EC 3.2.1.8 )
xylanase
(EC 3.2.1.8 )
beta-1,4-xylanase
(EC 3.2.1.8 )
endo-1,4-xylanase
(EC 3.2.1.8 )
endo-beta-1,4-xylanase
(EC 3.2.1.8 )
endo-1,4-beta-D-xylanase
(EC 3.2.1.8 )
1,4-beta-xylan xylanohydrolase
(EC 3.2.1.8 )
beta-xylanase
(EC 3.2.1.8 )
beta-1,4-xylan xylanohydrolase
(EC 3.2.1.8 )
endo-1,4-beta-xylanase
(EC 3.2.1.8 )
beta-D-xylanase
(EC 3.2.1.8 )

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P54865 XYND_CELFI Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C00707 L00032 C00001 C00707 C00033
E.C. 3.2.1.8
3.5.1.-
3.2.1.8
3.5.1.-
3.2.1.8
3.5.1.-
3.5.1.-
Compound Xylan Acetyl xylan H2O Xylan Acetate
Type polysaccharide carbohydrate,polysaccharide H2O polysaccharide carboxyl group
ChEBI 15377
15366
PubChem 22247451
962
176
21980959
1e5bA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1e5cA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1xbdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
2xbdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1hehC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1hejC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1e5bA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant R262G
1e5cA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant R262G
1xbdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2xbdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1hehC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1hejC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. of steps in catalysis

References
[1]
Resource
Comments
Medline ID
PubMed ID 1886523
Journal Microbiol Rev
Year 1991
Volume 55
Pages 303-15
Authors Gilkes NR, Henrissat B, Kilburn DG, Miller RC Jr, Warren RA
Title Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 8170399
Journal Mol Microbiol
Year 1994
Volume 11
Pages 375-82
Authors Millward-Sadler SJ, Poole DM, Henrissat B, Hazlewood GP, Clarke JH, Gilbert HJ
Title Evidence for a general role for high-affinity non-catalytic cellulose binding domains in microbial plant cell wall hydrolases.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 7717975
Journal Biochem J
Year 1995
Volume 307
Pages 191-5
Authors Black GW, Hazlewood GP, Millward-Sadler SJ, Laurie JI, Gilbert HJ
Title A modular xylanase containing a novel non-catalytic xylan-specific binding domain.
Related PDB
Related UniProtKB
[4]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10425686
Journal Structure Fold Des
Year 1999
Volume 7
Pages 853-64
Authors Simpson PJ, Bolam DN, Cooper A, Ciruela A, Hazlewood GP, Gilbert HJ, Williamson MP
Title A family IIb xylan-binding domain has a similar secondary structure to a homologous family IIa cellulose-binding domain but different ligand specificity.
Related PDB 1xbd 2xbd
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 11327868
Journal Biochemistry
Year 2001
Volume 40
Pages 2468-77
Authors Bolam DN, Xie H, White P, Simpson PJ, Hancock SM, Williamson MP, Gilbert HJ
Title Evidence for synergy between family 2b carbohydrate binding modules in Cellulomonas fimi xylanase 11A.
Related PDB 1heh 1hej
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 11341835
Journal Biochemistry
Year 2001
Volume 40
Pages 5700-7
Authors Xie H, Bolam DN, Nagy T, Szabo L, Cooper A, Simpson PJ, Lakey JH, Williamson MP, Gilbert HJ
Title Role of hydrogen bonding in the interaction between a xylan binding module and xylan.
Related PDB
Related UniProtKB

Comments
This enzyme belongs to glycosidase family-11.
This enzyme is composed of four domains: the N-terminal catalytic domain, another catalytic domain, which is located between two xylan domains. However, the structures of the catalytic domains have not been determined yet, although those of its homologous enzymes have been solved.
Moreover, this enzyme is a bifunctional enzyme with deacetylase activity for acetylated xylan (E.C. 3.5.1.-), according to the Uniprot information. However, the E.C. number seems to be for amide hydrolysis, although it is for ester bonds.
The N-terminal catalytic domain is for endo-1,4-beta-xylanase (3.2.1.8), whereas the other catalytic domain seems to be for deacetylase (3.5.1.-).

Created Updated
2003-08-29 2012-02-03