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P29417

- XYNA_PENCH

UniProt

P29417 - XYNA_PENCH

Protein

Endo-1,4-beta-xylanase

Gene

XYLP

Organism
Penicillium chrysogenum (Penicillium notatum)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 2 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Hydrolyzes oat spelt and birchwood xylan randomly, yielding xylose and xylobiose as major end products.

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei161 – 1611Proton donorBy similarity
    Active sitei267 – 2671NucleophilePROSITE-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

    CAZyiGH10. Glycoside Hydrolase Family 10.
    mycoCLAPiXYN10P_PENCH.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endo-1,4-beta-xylanase (EC:3.2.1.8)
    Short name:
    Xylanase
    Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase
    Gene namesi
    Name:XYLP
    OrganismiPenicillium chrysogenum (Penicillium notatum)
    Taxonomic identifieri5076 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicilliumPenicillium chrysogenum complex

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 353330Endo-1,4-beta-xylanasePRO_0000007975Add
    BLAST

    Post-translational modificationi

    The N-terminus is blocked.

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    3D structure databases

    ProteinModelPortaliP29417.
    SMRiP29417. Positions 30-325.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001000. Glyco_hydro_10.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00331. Glyco_hydro_10. 1 hit.
    [Graphical view]
    PRINTSiPR00134. GLHYDRLASE10.
    SMARTiSM00633. Glyco_10. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P29417-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIPNITQLKT AALVMLFAGQ ALSGPVESRQ ASESIDAKFK AHGKKYLGNI    50
    ADQGTLNGNP KTPAIIKANF GQLSPENSMK WDATEPSQGQ FSFAGSDYFV 100
    EFAETNGKLI RGHTLVWHSQ LPSWVSSITD KTTLTDVMKN HITTVMKQYK 150
    GKLYAWDVVN EIFEEDGTLR DSVFSRVLGE DFVRIAFETA READPEAKLY 200
    INDYNLDSAT SAKLQGMVSH VKKWIAAGVP IDGIGSQTHL GAGAGAAASG 250
    ALNALASAGT EEVAVTELDI AGATSTDYVD VVNACLDQPK CVGITVWGVA 300
    DPDSWRADES PLLFDASYNP KEAYNVSQLL SRQHAFDLYL KLGNLLLSRL 350
    HSD 353
    Length:353
    Mass (Da):38,193
    Last modified:February 1, 1995 - v2
    Checksum:iBF445C5E72FE2F94
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti153 – 1531L → F AA sequence (PubMed:1420277)Curated
    Sequence conflicti180 – 1801E → S AA sequence (PubMed:1420277)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M98458 Genomic DNA. Translation: AAA16427.1.
    PIRiJN0575.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M98458 Genomic DNA. Translation: AAA16427.1 .
    PIRi JN0575.

    3D structure databases

    ProteinModelPortali P29417.
    SMRi P29417. Positions 30-325.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH10. Glycoside Hydrolase Family 10.
    mycoCLAPi XYN10P_PENCH.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00114 .

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001000. Glyco_hydro_10.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00331. Glyco_hydro_10. 1 hit.
    [Graphical view ]
    PRINTSi PR00134. GLHYDRLASE10.
    SMARTi SM00633. Glyco_10. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and structural organization of a xylanase-encoding gene from Penicillium chrysogenum."
      Haas H., Friedlin E., Stoeffler G., Redl B.
      Gene 126:237-242(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 10002 / CBS 277.47 / NBRC 4626 / Wis. Q-176.
    2. "Purification, characterization and partial amino acid sequences of a xylanase produced by Penicillium chrysogenum."
      Haas H., Herfurth E., Stoeffler G., Redl B.
      Biochim. Biophys. Acta 1117:279-286(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 61-107; 109-123; 140-146; 153-180; 199-212 AND 228-237, CHARACTERIZATION.
      Strain: ATCC 10002 / CBS 277.47 / NBRC 4626 / Wis. Q-176.

    Entry informationi

    Entry nameiXYNA_PENCH
    AccessioniPrimary (citable) accession number: P29417
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 80 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3