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P36217 (XYN2_HYPJE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endo-1,4-beta-xylanase 2

Short name=Xylanase 2
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase 2
Gene names
Name:xyn2
OrganismHypocrea jecorina (Trichoderma reesei)
Taxonomic identifier51453 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Protein attributes

Sequence length222 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Pathway

Glycan degradation; xylan degradation.

Sequence similarities

Belongs to the glycosyl hydrolase 11 (cellulase G) family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
Pyrrolidone carboxylic acid
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionendo-1,4-beta-xylanase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232
Chain33 – 222190Endo-1,4-beta-xylanase 2
PRO_0000008014

Sites

Active site1181Nucleophile
Active site2091Proton donor

Amino acid modifications

Modified residue331Pyrrolidone carboxylic acid
Glycosylation701N-linked (GlcNAc...) Potential
Glycosylation931N-linked (GlcNAc...) Potential
Glycosylation1291N-linked (GlcNAc...) Potential

Secondary structure

............................. 222
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P36217 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 15F7032FACF963FF

FASTA22224,172
        10         20         30         40         50         60 
MVSFTSLLAA SPPSRASCRP AAEVESVAVE KRQTIQPGTG YNNGYFYSYW NDGHGGVTYT 

        70         80         90        100        110        120 
NGPGGQFSVN WSNSGNFVGG KGWQPGTKNK VINFSGSYNP NGNSYLSVYG WSRNPLIEYY 

       130        140        150        160        170        180 
IVENFGTYNP STGATKLGEV TSDGSVYDIY RTQRVNQPSI IGTATFYQYW SVRRNHRSSG 

       190        200        210        220 
SVNTANHFNA WAQQGLTLGT MDYQIVAVEG YFSSGSASIT VS 

« Hide

References

[1]"The two major xylanases from Trichoderma reesei: characterization of both enzymes and genes."
Toerroenen A., Mach R.L., Messner R., Gonzalez R., Kalkkinen N., Harkki A., Kubicek C.P.
Biotechnology (N.Y.) 10:1461-1465(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, PYROGLUTAMATE FORMATION AT GLN-33.
Strain: C30.
[2]"Three-dimensional structure of endo-1,4-beta-xylanase II from Trichoderma reesei: two conformational states in the active site."
Toerroenen A., Harkki A., Rouvinen J.
EMBO J. 13:2493-2501(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
Strain: C30.
[3]"Structural comparison of two major endo-1,4-xylanases from Trichoderma reesei."
Toerroenen A., Rouvinen J.
Biochemistry 34:847-856(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
Strain: C30.
[4]"Covalent binding of three epoxyalkyl xylosides to the active site of endo-1,4-xylanase II from Trichoderma reesei."
Havukainen R., Toerroenen A., Laitinen T., Rouvinen J.
Biochemistry 35:9617-9624(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
Strain: C30.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X69573 Genomic DNA. Translation: CAA49293.1.
PIRS39154.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ENXX-ray1.50A/B34-222[»]
1REDX-ray1.60A/B34-222[»]
1REEX-ray1.60A/B34-222[»]
1REFX-ray1.80A/B34-222[»]
1XYOX-ray1.50A/B34-222[»]
1XYPX-ray1.50A/B34-222[»]
2D97X-ray2.01A34-222[»]
2D98X-ray2.00A34-222[»]
2DFBX-ray1.11A33-222[»]
2DFCX-ray1.19A33-222[»]
3LGRX-ray1.64A34-222[»]
4HK8X-ray1.15A34-222[»]
4HK9X-ray1.55A35-222[»]
4HKLX-ray1.10A34-222[»]
4HKOX-ray1.50A34-222[»]
4HKWX-ray1.65A34-222[»]
ProteinModelPortalP36217.
SMRP36217. Positions 34-222.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH11. Glycoside Hydrolase Family 11.
mycoCLAPXYN11B_TRIRE.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG05353.

Enzyme and pathway databases

UniPathwayUPA00114.

Family and domain databases

Gene3D2.60.120.180. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
PfamPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSPR00911. GLHYDRLASE11.
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP36217.

Entry information

Entry nameXYN2_HYPJE
AccessionPrimary (citable) accession number: P36217
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries