Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P36217

- XYN2_HYPJE

UniProt

P36217 - XYN2_HYPJE

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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 – 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 – 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.
    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.
    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: October 1, 2014
    This is version 95 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