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P36218

- XYN1_HYPJE

UniProt

P36218 - XYN1_HYPJE

Protein

Endo-1,4-beta-xylanase 1

Gene

xyn1

Organism
Hypocrea jecorina (Trichoderma reesei)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei126 – 1261NucleophilePROSITE-ProRule annotation
    Active sitei215 – 2151Proton donorPROSITE-ProRule annotation

    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.
    mycoCLAPiXYN11A_TRIRE.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endo-1,4-beta-xylanase 1 (EC:3.2.1.8)
    Short name:
    Xylanase 1
    Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase 1
    Gene namesi
    Name:xyn1
    OrganismiHypocrea jecorina (Trichoderma reesei)
    Taxonomic identifieri51453 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 5151Sequence AnalysisAdd
    BLAST
    Chaini52 – 229178Endo-1,4-beta-xylanase 1PRO_0000008013Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi51453.JGI74223.

    Structurei

    Secondary structure

    1
    229
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi56 – 616
    Beta strandi63 – 708
    Beta strandi72 – 8312
    Beta strandi85 – 939
    Beta strandi99 – 12123
    Turni122 – 1243
    Beta strandi125 – 13511
    Beta strandi140 – 1489
    Beta strandi151 – 16515
    Beta strandi168 – 18114
    Beta strandi184 – 1885
    Helixi190 – 19910
    Beta strandi206 – 22823

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XYNX-ray2.00A52-229[»]
    ProteinModelPortaliP36218.
    SMRiP36218. Positions 52-229.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP36218.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG05353.
    OMAiNQYISVR.

    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.

    P36218-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVAFSSLICA LTSIASTLAM PTGLEPESSV NVTERGMYDF VLGAHNDHRR    50
    RASINYDQNY QTGGQVSYSP SNTGFSVNWN TQDDFVVGVG WTTGSSAPIN 100
    FGGSFSVNSG TGLLSVYGWS TNPLVEYYIM EDNHNYPAQG TVKGTVTSDG 150
    ATYTIWENTR VNEPSIQGTA TFNQYISVRN SPRTSGTVTV QNHFNAWASL 200
    GLHLGQMNYQ VVAVEGWGGS GSASQSVSN 229
    Length:229
    Mass (Da):24,583
    Last modified:June 1, 1994 - v1
    Checksum:iF9E8BFE1607038DB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X69574 Genomic DNA. Translation: CAA49294.1.
    PIRiS39155.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X69574 Genomic DNA. Translation: CAA49294.1 .
    PIRi S39155.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XYN X-ray 2.00 A 52-229 [» ]
    ProteinModelPortali P36218.
    SMRi P36218. Positions 52-229.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 51453.JGI74223.

    Protein family/group databases

    CAZyi GH11. Glycoside Hydrolase Family 11.
    mycoCLAPi XYN11A_TRIRE.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi NOG05353.
    OMAi NQYISVR.

    Enzyme and pathway databases

    UniPathwayi UPA00114 .

    Miscellaneous databases

    EvolutionaryTracei P36218.

    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.
      Strain: ATCC 56765 / Rut C-30.
    2. "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 (2.0 ANGSTROMS).

    Entry informationi

    Entry nameiXYN1_HYPJE
    AccessioniPrimary (citable) accession number: P36218
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 88 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