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Protein

Endo-1,4-beta-xylanase 2

Gene

XYL2

Organism
Magnaporthe grisea (Crabgrass-specific blast fungus) (Pyricularia grisea)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Accounts for approximately 70 percent of the endoxylanase activity in the culture filtrate.1 Publication

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.1 Publication

Pathwayi: xylan degradation

This protein is involved in the pathway xylan degradation, which is part of Glycan degradation.
View all proteins of this organism that are known to be involved in the pathway xylan degradation and in Glycan degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei159Proton donorBy similarity1
Active sitei266NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

UniPathwayi
UPA00114

Protein family/group databases

CAZyiGH10 Glycoside Hydrolase Family 10
mycoCLAPiXYN10B_MAGGR

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase 2 (EC:3.2.1.8)
Short name:
Xylanase 2
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase 2
Gene namesi
Name:XYL2
Synonyms:XYN33
OrganismiMagnaporthe grisea (Crabgrass-specific blast fungus) (Pyricularia grisea)
Taxonomic identifieri148305 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeMagnaporthalesMagnaporthaceaeMagnaporthe

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

Retains 39 percent of the catalytic activity. Double xyl1/xyl2 deletion mutant retains 19 percent of the activity and exhibits a 50 percent reduction in accumulation of total mycelial mass.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
ChainiPRO_500014262418 – 331Endo-1,4-beta-xylanase 2Add BLAST314

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi105N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi284 ↔ 290By similarity
Glycosylationi301N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Inductioni

Expressed in presence of rice cell walls or on oat spelt xylan, but not when grown on sucrose.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ01176
SMRiQ01176
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 329GH10PROSITE-ProRule annotationAdd BLAST299

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi210 – 280Gly-richAdd BLAST71

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

InterProiView protein in InterPro
IPR001000 GH10
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF00331 Glyco_hydro_10, 1 hit
PRINTSiPR00134 GLHYDRLASE10
SMARTiView protein in SMART
SM00633 Glyco_10, 1 hit
SUPFAMiSSF51445 SSF51445, 1 hit
PROSITEiView protein in PROSITE
PS51760 GH10_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q01176-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKASSVLLGL APLAALAAPT PEAELSARQA QQSIDALMKA KGKLYFGTAT
60 70 80 90 100
DQGLLNTGKN SAIIKADFGQ VTPENSMKCQ SLENTRGQYN WAPADALVNF
110 120 130 140 150
AVSNNKSIRG HTLIWHSQLP GWVNNINDRN QLTTVIQNHV ATVMGRWKGK
160 170 180 190 200
IRAWDVVNEI FNEDGTMRQS VFSRVLGEDF VRIAFEAARK ADPNAKLYIN
210 220 230 240 250
DYNLDRPNAG KLTKGMVGHV KKWVGAGVPI DGIGRQGHLQ SGQGNGLGQG
260 270 280 290 300
IKGLGDSGVK EVGGNELDIQ GNNGNEFGGG NKACLPVPAC VGIPAWGVRD
310 320 330
NDSWRPQGNP LLFDSNYNPK PAYNSVVQAL K
Length:331
Mass (Da):35,570
Last modified:November 1, 1996 - v1
Checksum:i002C380713232AEE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L37530 Genomic DNA Translation: AAC41684.1

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L37530 Genomic DNA Translation: AAC41684.1

3D structure databases

ProteinModelPortaliQ01176
SMRiQ01176
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH10 Glycoside Hydrolase Family 10
mycoCLAPiXYN10B_MAGGR

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayi
UPA00114

Family and domain databases

InterProiView protein in InterPro
IPR001000 GH10
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF00331 Glyco_hydro_10, 1 hit
PRINTSiPR00134 GLHYDRLASE10
SMARTiView protein in SMART
SM00633 Glyco_10, 1 hit
SUPFAMiSSF51445 SSF51445, 1 hit
PROSITEiView protein in PROSITE
PS51760 GH10_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiXYN2_MAGGR
AccessioniPrimary (citable) accession number: Q01176
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 9, 2014
Last sequence update: November 1, 1996
Last modified: May 10, 2017
This is version 77 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
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Main funding by: National Institutes of Health

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