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Protein

Endo-1,4-beta-xylanase A

Gene

xynA

Organism
Aspergillus tubingensis
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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.

Catalytic activityi

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

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 sitei106NucleophilePROSITE-ProRule annotation1
Active sitei197Proton donorPROSITE-ProRule annotation1

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

CAZyiGH11 Glycoside Hydrolase Family 11
mycoCLAPiXYN11A_ASPTU

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase A (EC:3.2.1.8)
Short name:
Xylanase A
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase A
Endo-1,4-beta-xylanase I
Short name:
Xylanase I
Gene namesi
Name:xynA
Synonyms:xlnA
OrganismiAspergillus tubingensis
Taxonomic identifieri5068 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27By similarityAdd BLAST27
ChainiPRO_000000799528 – 211Endo-1,4-beta-xylanase AAdd BLAST184

Structurei

3D structure databases

ProteinModelPortaliP55331
SMRiP55331
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini28 – 210GH11PROSITE-ProRule annotationAdd BLAST183

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.120.180, 1 hit
InterProiView protein in InterPro
IPR013320 ConA-like_dom_sf
IPR013319 GH11/12
IPR018208 GH11_AS_1
IPR033119 GH11_AS_2
IPR033123 GH11_dom
IPR001137 Glyco_hydro_11
PfamiView protein in Pfam
PF00457 Glyco_hydro_11, 1 hit
PRINTSiPR00911 GLHYDRLASE11
SUPFAMiSSF49899 SSF49899, 1 hit
PROSITEiView protein in PROSITE
PS00776 GH11_1, 1 hit
PS00777 GH11_2, 1 hit
PS51761 GH11_3, 1 hit

Sequencei

Sequence statusi: Complete.

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

P55331-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKVTAAFAGL LVTAFAAPAP EPDLVSRSAG INYVQNYNGN LGDFTYDESA
60 70 80 90 100
GTFSMYWEDG VSSDFVVGLG WTTGSSNAIT YSAEYSASGS ASYLAVYGWV
110 120 130 140 150
NYPQAEYYIV EDYGDYNPCS SATSLGTVYS DGSTYQVCTD TRTNEPSITG
160 170 180 190 200
TSTFTQYFSV RESTRTSGTV TVANHFNFWA HHGFGNSDFN YQVVAVEAWS
210
GAGSASVTIS S
Length:211
Mass (Da):22,576
Last modified:July 15, 1998 - v2
Checksum:i1A88D060C67080D4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26988 Genomic DNA Translation: AAB05996.1
PIRiS49542

Similar proteinsi

Entry informationi

Entry nameiXYNA_ASPTU
AccessioniPrimary (citable) accession number: P55331
Secondary accession number(s): Q12568
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 15, 1998
Last modified: November 22, 2017
This is version 81 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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