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Protein

Endo-1,4-beta-xylanase

Gene
N/A
Organism
Byssochlamys spectabilis (Paecilomyces variotii)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Temperature dependencei

Thermostable.

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 sitei86NucleophilePROSITE-ProRule annotation1
Active sitei178Proton donorPROSITE-ProRule annotation1

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

UniPathwayiUPA00114.

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11A_BYSSP.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase (EC:3.2.1.8)
Short name:
Xylanase
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase
PVX
OrganismiByssochlamys spectabilis (Paecilomyces variotii)
Taxonomic identifieri264951 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesThermoascaceaeByssochlamys

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001840691 – 194Endo-1,4-beta-xylanaseAdd BLAST194

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylglycine1 Publication1
Disulfide bondi110 ↔ 154

Keywords - PTMi

Acetylation, Disulfide bond

Structurei

Secondary structure

1194
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 10Combined sources5
Beta strandi13 – 19Combined sources7
Beta strandi25 – 29Combined sources5
Beta strandi34 – 39Combined sources6
Beta strandi41 – 53Combined sources13
Beta strandi59 – 81Combined sources23
Turni82 – 84Combined sources3
Beta strandi85 – 96Combined sources12
Turni98 – 101Combined sources4
Beta strandi102 – 110Combined sources9
Beta strandi113 – 127Combined sources15
Beta strandi130 – 143Combined sources14
Beta strandi146 – 151Combined sources6
Helixi152 – 161Combined sources10
Beta strandi168 – 182Combined sources15
Beta strandi184 – 192Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PVXX-ray1.59A1-194[»]
ProteinModelPortaliP81536.
SMRiP81536.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP81536.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 191GH11PROSITE-ProRule annotationAdd BLAST191

Sequence similaritiesi

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

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.

P81536-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
GTTPNSEGWH DGYYYSWWSD GGGDSTYTNN SGGTYEITWG NGGNLVGGKG
60 70 80 90 100
WNPGLNARAI HFTGVYQPNG TSYLSVYGWT RNPLVEYYIV ENFGSSNPSS
110 120 130 140 150
GSTDLGTVSC DGSTYTLGQS TRYNAPSIDG TQTFNQYWSV RQDKRSSGTV
160 170 180 190
QTGCHFDAWA SAGLNVTGDH YYQIVATEGY FSSGYARITV ADVG
Length:194
Mass (Da):20,947
Last modified:June 1, 2000 - v1
Checksum:i1D5C50AA4F6EDB90
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PVXX-ray1.59A1-194[»]
ProteinModelPortaliP81536.
SMRiP81536.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11A_BYSSP.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.

Miscellaneous databases

EvolutionaryTraceiP81536.

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_BYSSP
AccessioniPrimary (citable) accession number: P81536
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 1, 2000
Last modified: November 2, 2016
This is version 75 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, Direct protein sequencing

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.