3.2.1.8: endo-1,4-beta-xylanase This is an abbreviated version! For detailed information about endo-1,4-beta-xylanase, go to the full flat file .
Reaction
(Xylbeta(1-4))n +
H2O =
(Xylbeta(1-4))n-m +
(Xylbeta(1-4))m
Synonyms (1--> 4)-beta-xylan 4-xylanohydrolase, (1-4)-beta-xylan 4-xylanohydrolase, 1,4-beta-D-xylan xylanohydrolase, 1,4-beta-D-xylan xylanohydrolase 22, 1,4-beta-D-xylan-xylanohydrolase, 1,4-beta-xylan xylanohydrolase, 1,4-beta-xylanase, 34 kDa xylanase, Abf51A, Abf62A-Axe6A, Acel_0180, acidophilic endo-1,4-beta-xylanase, AfXynA, AfXynB, alkaline active xylanase, alkaline xylanase, AMX-4 xylanase, AnxB, AxB8, Axy43A, basic xylanase, Bcx, beta-1, 4-endoxylanase, beta-1,4-D-xylanase, beta-1,4-endoxylanase, beta-1,4-xylan hydrolase, beta-1,4-xylan xylanohydrolase, beta-1,4-xylanase, beta-1,4endoxylanase, beta-D-xylanase, beta-endoxylanase, beta-xylanase, bifunctional cellulase/xylanase, bifunctional endoglucanase/xylanase, bifunctional xylanase/endoglucanase, BlxA, BSX, BSXY, Btx, Calow_0124, ctendo7, Cthe_3012, CTHT_0045780, CtXynGH30, EGXA, endo(1-4)beta-xylanase, endo-(1,4)-beta-xylanase, endo-(1--> 4)-beta-xylanase, endo-1,4-beta-D-xylanase, endo-1,4-beta-xylanase, endo-1,4-beta-xylanase II, endo-1,4-xylanase, endo-acting beta-1,4-xylanase, endo-beta-(1'4)-xylanase, endo-beta-(1,4)-xylanase, endo-beta-1, 4-xylanase, endo-beta-1,4-xylanase, endo-beta-1,4-xylanase 2, endo-beta-1,4-xylanase2, endo-xylanase, endoxylanase, endoxylanase I, endoxylanase NtSymX11, endoxylanase Xys1DELTA, EXY1, family 11 endoxylanase, family 11 xylanase, family 30 glycoside hydrolase subfamily 8 glucuronoxylan endo-beta-1,4-xylanase, family-10 endo-1,4-beta-xylanase, FIA-xylanase, FOTG_15646, G/11 endo-1,4-beta-xylanase, GC25 xylanase, GH 10 xylanase, GH 11 xylanase, GH-10 endo-1,4-beta-xylanase, GH-11 endo-1,4-beta-xylanase, GH10 endo-beta-1,4-xylanase, GH10 xylanase D, GH11 xylanase, GH43B6, GH7 endoglucanase, GHF 10 endoxylanase, GHF 11 endoxylanase, glycoside hydrolase family 11 endoxylanase, glycoside hydrolase family 8 domain protein, GXYN, KRICT PX1, MalAC0309_0409, More, MROS_2090, MROS_2091, MROS_2495, Mxyn10, MYCTH_49824, MYCTH_56237, ORF4, Pedsa_2704, PhX20, PhX33, PsGH10A, pXyl, RrXyn11A, RuCelA, Rut C-30, SCO5931, SipoEnXyn10A, SlxB, SoxB, SSO1354 protein, TAXI, TERTU_4506, Tfu_1213, TLX, TmxB, Tpet_0854, TRX II, TtGH8, Wxl1, X-I, X-II, X34, Xa, Xln-1, xlnA, xlnB, XT6, Xyl, Xyl I, Xyl II, XYL1, Xyl10A, Xyl10B, XYL10C, Xyl11, XYL1p, XYL2, Xyl2090, Xyl2091, Xyl2495, Xyl30, XYLA, xylanase, xylanase 1, xylanase 10A, xylanase 10B, xylanase 10C, xylanase 11 A, xylanase 11A, xylanase 11J, xylanase 2, Xylanase 22, xylanase 43A, xylanase A, xylanase B, xylanase bI, xylanase bII, xylanase C, xylanase I, xylanase II, xylanase III, xylanase J, xylanase LC9, xylanase Xyl10A, xylanase Xyl11A, xylanase XynZF-2, xylanase, endo-1,4-, XylB, XylB8, XylC, XYLD, XylE, XylF2, XylG, xylH, xylM, XylX, XYLY, Xyn II, Xyn III, Xyn-b39, Xyn-Lxy, Xyn1, Xyn10, Xyn10A, Xyn10B, Xyn10E, XYN10G5, XYN10Ks_480, Xyn11, Xyn11A, XYN11F63, XYN11Ks_480, Xyn11NX, Xyn12.2, Xyn162, Xyn2, Xyn3, Xyn30A, Xyn5, XynA, XynA119, XynA19, XynA4, XynAS27, XynAS9, XynB, XynB18, XynBS27, XynC, XynD, XynE15, XynE2, XynG1, XynGH30, XynGR40, XYNII, XynIII, XynJ, XynS14, XynS20, XynSW1, XynSW3, XynT, XynY, XynZ, Xys1, Xys1delta, xysA
ECTree
Posttranslational Modification
Posttranslational Modification on EC 3.2.1.8 - endo-1,4-beta-xylanase
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glycoprotein
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-
glycoprotein
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XynS14 is expressed in Pichia pastoris as glycoproteins with different glycosylation levels at four N-glycosylation sites
glycoprotein
-
XynS14 is expressed in Pichia pastoris as glycoproteins with different glycosylation levels at four N-glycosylation sites
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glycoprotein
-
contains 11% w/w carbohydrate
glycoprotein
-
xylanase I, about 56% carbohydtate content, xylanase II, about 62% carbohydrate
glycoprotein
-
contains 20% carbohydrate
glycoprotein
-
the degree of glycosylation is 74.1%
glycoprotein
-
contains 20% carbohydrate
-
glycoprotein
-
the degree of glycosylation is 74.1%
-
glycoprotein
-
14% carbohydrate content
glycoprotein
-
the enzyme is either a glycoprotein or possesses a tightly bound carbohydrate residue
glycoprotein
-
contains 35% carbohydrate
glycoprotein
the extracellular endoxylanase expressed in yeast shows an enhanced thermal stability due to the N-linked glycosylation, the native enzyme in Bacillus subtilis is not glycosylated
glycoprotein
-
contains 35% carbohydrate
-
glycoprotein
enzyme contains a predicted carbohydrate binding site
glycoprotein
-
N-glycosylated
glycoprotein
-
xylanase I contains 2.5% carbohydrate, xylanase III contains 8.0% carbohydrate
glycoprotein
-
xlanase IA contains 7% carbohydrate. Xylanase IIIA contains no detectable carbohydrate
glycoprotein
-
xylanase IA contains 7% carbohydrate, xylanase III contains detectable carbohydrate
glycoprotein
-
7% carbohydrate content, isoform xylanase IA
glycoprotein
-
contains 27% carbohydrate
glycoprotein
-
contains 27% carbohydrate
-
glycoprotein
the protein sequence contains one possible N-glycosylation site, consensus Asn-Xaa-Ser/Thr, at position 25 and two potential O-glycosylation sites at positions 26/27, respectively
glycoprotein
-
the protein sequence contains one possible N-glycosylation site, consensus Asn-Xaa-Ser/Thr, at position 25 and two potential O-glycosylation sites at positions 26/27, respectively
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glycoprotein
-
contains 4% carbohydrate w/w
glycoprotein
the recombinant extrecellular enzyme is highly glycosylated
glycoprotein
-
the recombinant extrecellular enzyme is highly glycosylated
-
glycoprotein
-
xylanase I and xylanase II
glycoprotein
-
Xyn3 has a carbohydrate content of 10.83%
glycoprotein
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Xyn3 has a carbohydrate content of 10.83%
-
glycoprotein
-
carbohydrate content of isozyme XA-1 is 6.7% and of isozyme Xa-2 3.58%
glycoprotein
-
carbohydrate content of isozyme XA-1 is 6.7% and of isozyme Xa-2 3.58%
-
glycoprotein
-
PHX20 and PhX33
glycoprotein
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PHX20 and PhX33
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glycoprotein
-
enzyme form X-a contains 36.6% carbohydrate, enzyme form X-b-I contains 31.5% carbohydrate, enzyme form X-a contains 14.2% carbohydrate
glycoprotein
-
xylanase a contains 36.6% carbohydrate w/w, xylanase bI contains 31.5% carbohydrate w/w, xylanase bII contains 14.2% carbohydrate w/w
glycoprotein
-
enzyme form X-a contains 36.6% carbohydrate, enzyme form X-b-I contains 31.5% carbohydrate, enzyme form X-a contains 14.2% carbohydrate
-
glycoprotein
-
73.97% carbohydrate content
glycoprotein
sequence contains six potential glycosylation sites
glycoprotein
-
73.97% carbohydrate content
-
glycoprotein
the recombinant protein is N- and O-glycosylated
glycoprotein
sequence contains one N-glycosylation site
glycoprotein
the recombinant enzyme may be glycosylated
glycoprotein
-
the recombinant enzyme may be glycosylated
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glycoprotein
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1.7% carbohydrate content
glycoprotein
Thermochaetoides thermophila
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glycoprotein
Thermochaetoides thermophila
predicted one N-linked glycosylation site (N261) and three O-linked glycosylation sites (T32, T312 and T332), respectively
glycoprotein
Thermochaetoides thermophila CBS 144.50
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-
-
glycoprotein
Thermochaetoides thermophila CBS 144.50
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predicted one N-linked glycosylation site (N261) and three O-linked glycosylation sites (T32, T312 and T332), respectively
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glycoprotein
Thermochaetoides thermophila DSM 1495
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-
-
glycoprotein
Thermochaetoides thermophila DSM 1495
-
predicted one N-linked glycosylation site (N261) and three O-linked glycosylation sites (T32, T312 and T332), respectively
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glycoprotein
Thermochaetoides thermophila IMI 039719
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-
-
glycoprotein
Thermochaetoides thermophila IMI 039719
-
predicted one N-linked glycosylation site (N261) and three O-linked glycosylation sites (T32, T312 and T332), respectively
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glycoprotein
-
xylanase A contains 19% carbohydrate, xylanase B contains 3% carbohydrate, xylanase C contains 4% carbohydrate
glycoprotein
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0.74% carbohydrate content of the wild-type enzyme, 11.8% of the mutant enzyme
glycoprotein
-
the N-glycosylation site Asn26, carrying GlcNAc(Man) as a glycan core structure, is located in a well-exposed loop, amino acids 21 to 28, between a beta-strand, amino acids 15 to 20, and alpha-helix, amino acids 29 to 37. Glycosylation can increase the thermostability. Glycosylation in a well-exposed loop in XYN10A xylanase can increase local mobility or destabilize the enzyme by affecting the local conformation
glycoprotein
MYCTH_49824 has one O-glycosylation site (at residue 40) and four N-glycosylation sites (resides 20, 33, 101, 107)
glycoprotein
MYCTH_56237 has two putative O-glycosylation sites (residues 35 and 37) and one N-glycosylation site (Asn22)
glycoprotein
-
MYCTH_49824 has one O-glycosylation site (at residue 40) and four N-glycosylation sites (resides 20, 33, 101, 107)
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glycoprotein
-
MYCTH_56237 has two putative O-glycosylation sites (residues 35 and 37) and one N-glycosylation site (Asn22)
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glycoprotein
-
MYCTH_49824 has one O-glycosylation site (at residue 40) and four N-glycosylation sites (resides 20, 33, 101, 107)
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glycoprotein
-
MYCTH_56237 has two putative O-glycosylation sites (residues 35 and 37) and one N-glycosylation site (Asn22)
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glycoprotein
-
MYCTH_49824 has one O-glycosylation site (at residue 40) and four N-glycosylation sites (resides 20, 33, 101, 107)
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glycoprotein
-
MYCTH_56237 has two putative O-glycosylation sites (residues 35 and 37) and one N-glycosylation site (Asn22)
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glycoprotein
-
about 20% of total mass are glycosyl residues
glycoprotein
-
carbohydrate content about 20%
glycoprotein
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about 20% of total mass are glycosyl residues
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glycoprotein
-
carbohydrate content about 20%
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glycoprotein
-
xylanase I contains 14% carbohydrate, xylanase II contains 8% carbohydrate
glycoprotein
-
glycoprotein, at least some of the sugar moieties are linked to Asn
no glycoprotein
no N- or O-glycosylations sites are detected by bioinformatic tools
no glycoprotein
-
isoform xylanase IIIA
no modification
-
contains no carbohydrate
no modification
-
contains carbohydrate in a covalent manner, is not a glycoprotein
no modification
-
although the pure enzyme preparation contains carbohydrate, the protein does not appear to be glycosylated, since the carbohydrate can be removed by treatment with 1% SDS
no modification
-
contains no carbohydrate
no modification
-
contains no carbohydrate
no modification
-
contains no carbohydrate
-
no modification
-
contains no carbohydrate
proteolytic modification
sequence contains a putative N-gnal peptide of 25 amino acids
proteolytic modification
-
sequence contains a putative N-gnal peptide of 25 amino acids
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proteolytic modification
the enzyme is post-translationally modified in the cell wall serving for regulation of the enzyme activity and cell wall-microdomain-specific hydrolysis
proteolytic modification
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the protein contains a 38-amino-acid leader peptide with 6 Arg residues in its amino-terminal end, a catalytic domain and a cellulose-binding domain connected by a linker region rich in Pro and Gly. A 38000 Da enzyme form and a 48000 Da enzyme form are detected by SDS-PAGE. The 38000 Da enzyme form does not contain the cellulose-binding domain
proteolytic modification
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the protein contains a 38-amino-acid leader peptide with 6 Arg residues in its amino-terminal end, a catalytic domain and a cellulose-binding domain connected by a linker region rich in Pro and Gly. A 38000 Da enzyme form and a 48000 Da enzyme form are detected by SDS-PAGE. The 38000 Da enzyme form does not contain the cellulose-binding domain
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proteolytic modification
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32 amino acids are removed from the N-terminus of Xyn B by proteolysis, resulting in the formation of a protein species with a predicted molecular weight of 40805 Da
additional information
no N- or O-glycosylations sites are detected by bioinformatics tools
additional information
-
no N- or O-glycosylations sites are detected by bioinformatics tools
additional information
-
no N-glycosylation observed
additional information
sequence contains a presumed prepropeptide of 27 amino acids
additional information
-
sequence contains a presumed prepropeptide of 27 amino acids
additional information
-
sequence contains a presumed prepropeptide of 27 amino acids
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additional information
-
sequences contain several potential O-glycosylation sites, sequence of xynB contains addtitionally a potential N-glycosylation site
additional information
sequence does not contain any potential N-glycosylation sites
additional information
the enzyme is not glycosylated
additional information
-
the enzyme is not glycosylated
additional information
-
the enzyme is not glycosylated
-
additional information
sequence contains no putative N-glycosylation site
additional information
-
sequence contains no putative N-glycosylation site