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P36217

- XYN2_HYPJE

UniProt

P36217 - XYN2_HYPJE

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Protein
Endo-1,4-beta-xylanase 2
Gene
xyn2
Organism
Hypocrea jecorina (Trichoderma reesei)
Status
Reviewed - 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

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 – 3232
Add
BLAST
Chaini33 – 222190Endo-1,4-beta-xylanase 2
PRO_0000008014Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei33 – 331Pyrrolidone carboxylic acid
Glycosylationi70 – 701N-linked (GlcNAc...) Reviewed prediction
Glycosylationi93 – 931N-linked (GlcNAc...) Reviewed prediction
Glycosylationi129 – 1291N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein, Pyrrolidone carboxylic acid

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP36217.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG05353.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR008985. ConA-like_lec_gl_sf.
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

MVSFTSLLAA SPPSRASCRP AAEVESVAVE KRQTIQPGTG YNNGYFYSYW    50
NDGHGGVTYT NGPGGQFSVN WSNSGNFVGG KGWQPGTKNK VINFSGSYNP 100
NGNSYLSVYG WSRNPLIEYY IVENFGTYNP STGATKLGEV TSDGSVYDIY 150
RTQRVNQPSI IGTATFYQYW SVRRNHRSSG SVNTANHFNA WAQQGLTLGT 200
MDYQIVAVEG YFSSGSASIT VS 222
Length:222
Mass (Da):24,172
Last modified:June 1, 1994 - v1
Checksum:i15F7032FACF963FF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X69573 Genomic DNA. Translation: CAA49293.1.
PIRiS39154.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X69573 Genomic DNA. Translation: CAA49293.1 .
PIRi S39154.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ENX X-ray 1.50 A/B 34-222 [» ]
1RED X-ray 1.60 A/B 34-222 [» ]
1REE X-ray 1.60 A/B 34-222 [» ]
1REF X-ray 1.80 A/B 34-222 [» ]
1XYO X-ray 1.50 A/B 34-222 [» ]
1XYP X-ray 1.50 A/B 34-222 [» ]
2D97 X-ray 2.01 A 34-222 [» ]
2D98 X-ray 2.00 A 34-222 [» ]
2DFB X-ray 1.11 A 33-222 [» ]
2DFC X-ray 1.19 A 33-222 [» ]
3LGR X-ray 1.64 A 34-222 [» ]
4HK8 X-ray 1.15 A 34-222 [» ]
4HK9 X-ray 1.55 A 35-222 [» ]
4HKL X-ray 1.10 A 34-222 [» ]
4HKO X-ray 1.50 A 34-222 [» ]
4HKW X-ray 1.65 A 34-222 [» ]
ProteinModelPortali P36217.
SMRi P36217. Positions 34-222.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH11. Glycoside Hydrolase Family 11.
mycoCLAPi XYN11B_TRIRE.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi NOG05353.

Enzyme and pathway databases

UniPathwayi UPA00114 .

Miscellaneous databases

EvolutionaryTracei P36217.

Family and domain databases

Gene3Di 2.60.120.180. 1 hit.
InterProi IPR008985. ConA-like_lec_gl_sf.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view ]
Pfami PF00457. Glyco_hydro_11. 1 hit.
[Graphical view ]
PRINTSi PR00911. GLHYDRLASE11.
SUPFAMi SSF49899. SSF49899. 1 hit.
PROSITEi PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(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.

Entry informationi

Entry nameiXYN2_HYPJE
AccessioniPrimary (citable) accession number: P36217
Entry historyi
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 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

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