EzCatDB: M00219
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DB codeM00219
CATH domainDomain 12.60.120.- : Jelly RollsCatalytic domain
Domain 22.60.40.290 : Immunoglobulin-like
Domain 33.-.-.-Catalytic domain
Domain 42.60.40.290 : Immunoglobulin-like
E.C.3.2.1.8,3.5.1.-

CATH domainRelated DB codes (homologues)
2.60.40.290 : Immunoglobulin-likeD00479,D00502,D00504,M00026,M00192

Enzyme Name
UniProtKBKEGG

P54865
Protein nameBifunctional xylanase/deacetylaseendo-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)

SynonymsNone
IncludesEndo-1,4-beta-xylanase D
(Xylanase D)
(XYLD)
   EC 3.2.1.8
Acetylated xylan deacetylase
   EC 3.5.1.-
PfamPF00553 (CBM_2)
PF00457 (Glyco_hydro_11)
PF01522 (Polysacc_deac_1)
[Graphical view]
CAZyGH11 (Glycoside Hydrolase Family)


UniProtKB:Accession NumberP54865
Entry nameXYND_CELFI
ActivityEndohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Subunit
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00707L00032C00001C00707C00033
E.C.3.2.1.83.5.1.-3.2.1.8,3.5.1.-3.2.1.8,3.5.1.-3.5.1.-
CompoundXylanAcetyl xylanH2OXylanAcetate
Typepolysaccharidecarbohydrate,polysaccharideH2Opolysaccharidecarboxyl group
ChEBI

15377

15366
PubChem

962
22247451

21980959
176
             
1e5bAUnboundUnbound UnboundUnbound
1e5cAUnboundUnbound UnboundUnbound
1xbdAUnboundUnbound UnboundUnbound
2xbdAUnboundUnbound UnboundUnbound
1hehCUnboundUnbound UnboundUnbound
1hejCUnboundUnbound UnboundUnbound

Active-site residues
pdbcomment
         
1e5bAmutant R262G
1e5cAmutant R262G
1xbdA 
2xbdA 
1hehC 
1hejC 


references
[1]
PubMed ID1886523
JournalMicrobiol Rev
Year1991
Volume55
Pages303-15
AuthorsGilkes NR, Henrissat B, Kilburn DG, Miller RC Jr, Warren RA
TitleDomains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families.
[2]
PubMed ID8170399
JournalMol Microbiol
Year1994
Volume11
Pages375-82
AuthorsMillward-Sadler SJ, Poole DM, Henrissat B, Hazlewood GP, Clarke JH, Gilbert HJ
TitleEvidence for a general role for high-affinity non-catalytic cellulose binding domains in microbial plant cell wall hydrolases.
[3]
PubMed ID7717975
JournalBiochem J
Year1995
Volume307
Pages191-5
AuthorsBlack GW, Hazlewood GP, Millward-Sadler SJ, Laurie JI, Gilbert HJ
TitleA modular xylanase containing a novel non-catalytic xylan-specific binding domain.
[4]
CommentsX-ray crystallography
PubMed ID10425686
JournalStructure Fold Des
Year1999
Volume7
Pages853-64
AuthorsSimpson PJ, Bolam DN, Cooper A, Ciruela A, Hazlewood GP, Gilbert HJ, Williamson MP
TitleA family IIb xylan-binding domain has a similar secondary structure to a homologous family IIa cellulose-binding domain but different ligand specificity.
Related PDB1xbd,2xbd
[5]
PubMed ID11327868
JournalBiochemistry
Year2001
Volume40
Pages2468-77
AuthorsBolam DN, Xie H, White P, Simpson PJ, Hancock SM, Williamson MP, Gilbert HJ
TitleEvidence for synergy between family 2b carbohydrate binding modules in Cellulomonas fimi xylanase 11A.
Related PDB1heh,1hej
[6]
PubMed ID11341835
JournalBiochemistry
Year2001
Volume40
Pages5700-7
AuthorsXie H, Bolam DN, Nagy T, Szabo L, Cooper A, Simpson PJ, Lakey JH, Williamson MP, Gilbert HJ
TitleRole of hydrogen bonding in the interaction between a xylan binding module and xylan.

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.-).

createdupdated
2003-08-292012-02-03


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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