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Protein

Endo-1,4-beta-xylanase 2

Gene

xyn2

Organism
Hypocrea jecorina (Trichoderma reesei)
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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei118 – 1181Nucleophile
Active sitei209 – 2091Proton donor

GO - Molecular functioni

  1. endo-1,4-beta-xylanase activity Source: UniProtKB-EC

GO - Biological processi

  1. xylan catabolic process Source: UniProtKB-UniPathway
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. 6451.
UniPathwayiUPA00114.

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11B_TRIRE.

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:xyn2
OrganismiHypocrea jecorina (Trichoderma reesei)
Taxonomic identifieri51453 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232Add
BLAST
Chaini33 – 222190Endo-1,4-beta-xylanase 2PRO_0000008014Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei33 – 331Pyrrolidone carboxylic acid1 Publication
Glycosylationi70 – 701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi93 – 931N-linked (GlcNAc...)Sequence Analysis
Glycosylationi129 – 1291N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein, Pyrrolidone carboxylic acid

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi37 – 426Combined sources
Beta strandi45 – 517Combined sources
Beta strandi57 – 615Combined sources
Beta strandi66 – 738Combined sources
Beta strandi76 – 8510Combined sources
Beta strandi91 – 11323Combined sources
Turni114 – 1163Combined sources
Beta strandi117 – 12711Combined sources
Turni130 – 1334Combined sources
Beta strandi135 – 1428Combined sources
Beta strandi145 – 15713Combined sources
Beta strandi162 – 17514Combined sources
Beta strandi178 – 1836Combined sources
Helixi184 – 19310Combined sources
Beta strandi200 – 21213Combined sources
Beta strandi214 – 2229Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP36217.
SMRiP36217. Positions 34-222.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36217.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG05353.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
PfamiPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P36217-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSFTSLLAA SPPSRASCRP AAEVESVAVE KRQTIQPGTG YNNGYFYSYW
60 70 80 90 100
NDGHGGVTYT NGPGGQFSVN WSNSGNFVGG KGWQPGTKNK VINFSGSYNP
110 120 130 140 150
NGNSYLSVYG WSRNPLIEYY IVENFGTYNP STGATKLGEV TSDGSVYDIY
160 170 180 190 200
RTQRVNQPSI IGTATFYQYW SVRRNHRSSG SVNTANHFNA WAQQGLTLGT
210 220
MDYQIVAVEG YFSSGSASIT VS
Length:222
Mass (Da):24,172
Last modified:May 31, 1994 - v1
Checksum:i15F7032FACF963FF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69573 Genomic DNA. Translation: CAA49293.1.
PIRiS39154.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69573 Genomic DNA. Translation: CAA49293.1.
PIRiS39154.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP36217.
SMRiP36217. Positions 34-222.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11B_TRIRE.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiNOG05353.

Enzyme and pathway databases

UniPathwayiUPA00114.
BRENDAi3.2.1.8. 6451.

Miscellaneous databases

EvolutionaryTraceiP36217.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
PfamiPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1991) [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(1993) [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(1994) [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(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
    Strain: C30.

Entry informationi

Entry nameiXYN2_HYPJE
AccessioniPrimary (citable) accession number: P36217
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 31, 1994
Last sequence update: May 31, 1994
Last modified: March 31, 2015
This is version 98 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

External Data

Dasty 3

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 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.