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Protein

Endo-1,4-beta-xylanase A

Gene

xynA

Organism
Aspergillus niger
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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.

Catalytic activityi

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

pH dependencei

Optimum pH is 3.0.

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 sitei106Nucleophile1
Active sitei197Proton donor1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

BRENDAi3.2.1.8. 518.
UniPathwayiUPA00114.

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.

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
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Protein family/group databases

Allergomei980. Asp n Hemicellulase.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Add BLAST27
ChainiPRO_000000799228 – 211Endo-1,4-beta-xylanase AAdd BLAST184

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi119 ↔ 138

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1211
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi33 – 38Combined sources6
Helixi39 – 41Combined sources3
Beta strandi42 – 47Combined sources6
Turni48 – 51Combined sources4
Beta strandi52 – 63Combined sources12
Beta strandi65 – 73Combined sources9
Beta strandi79 – 86Combined sources8
Beta strandi90 – 100Combined sources11
Turni101 – 104Combined sources4
Beta strandi105 – 115Combined sources11
Beta strandi120 – 130Combined sources11
Beta strandi133 – 145Combined sources13
Beta strandi150 – 163Combined sources14
Beta strandi166 – 170Combined sources5
Helixi172 – 179Combined sources8
Helixi180 – 182Combined sources3
Beta strandi187 – 209Combined sources23

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1T6GX-ray1.80C/D28-211[»]
1UKRX-ray2.40A/B/C/D28-211[»]
2QZ2X-ray2.80A28-211[»]
ProteinModelPortaliP55329.
SMRiP55329.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55329.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 1 GH11 (glycosyl hydrolase family 11) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR013319. GH11/12.
IPR018208. GH11_AS_1.
IPR033119. GH11_AS_2.
IPR033123. GH11_dom.
IPR001137. Glyco_hydro_11.
[Graphical view]
PfamiPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00776. GH11_1. 1 hit.
PS00777. GH11_2. 1 hit.
PS51761. GH11_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P55329-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVTAAFAGL LVTAFAAPVP EPVLVSRSAG INYVQNYNGN LGDFTYDESA
60 70 80 90 100
GTFSMYWEDG VSSDFVVGLG WTTGSSKAIT YSAEYSASGS SSYLAVYGWV
110 120 130 140 150
NYPQAEYYIV EDYGDYNPCS SATSLGTVYS DGSTYQVCTD TRTNEPSITG
160 170 180 190 200
TSTFTQYFSV RESTRTSGTV TVANHFNFWA QHGFGNSDFN YQVMAVEAWS
210
GAGSASVTIS S
Length:211
Mass (Da):22,642
Last modified:October 1, 1996 - v1
Checksum:i82BEBEE12ED79303
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
A19535 Unassigned DNA. Translation: CAA01470.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
A19535 Unassigned DNA. Translation: CAA01470.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1T6GX-ray1.80C/D28-211[»]
1UKRX-ray2.40A/B/C/D28-211[»]
2QZ2X-ray2.80A28-211[»]
ProteinModelPortaliP55329.
SMRiP55329.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei980. Asp n Hemicellulase.
CAZyiGH11. Glycoside Hydrolase Family 11.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.
BRENDAi3.2.1.8. 518.

Miscellaneous databases

EvolutionaryTraceiP55329.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR013319. GH11/12.
IPR018208. GH11_AS_1.
IPR033119. GH11_AS_2.
IPR033123. GH11_dom.
IPR001137. Glyco_hydro_11.
[Graphical view]
PfamiPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00776. GH11_1. 1 hit.
PS00777. GH11_2. 1 hit.
PS51761. GH11_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiXYNA_ASPNG
AccessioniPrimary (citable) accession number: P55329
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.