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Protein

Endo-1,4-beta-xylanase C

Gene

xynC

Organism
Talaromyces funiculosus (Fruitlet core rot fungus) (Penicillium funiculosum)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.2 Publications

Enzyme regulationi

Strongly inhibited by wheat xylanase inhibiting protein I (XIP-I), and by proteinaceous endoxylanase Triticum aestivum xylanase inhibitors I and II (TAXI-I and TAXI-II).2 Publications

Kineticsi

    1. Vmax=2540 µmol/min/mg enzyme toward birchwood xylan at pH 5.5 and 30 degrees Celsius2 Publications
    2. Vmax=7190 µmol/min/mg enzyme toward soluble wheat arabinoxylans at pH 5.5 and 30 degrees Celsius2 Publications

    pH dependencei

    Optimum pH is 5.0.2 Publications

    Temperature dependencei

    Optimum temperature is 55 degrees Celsius.2 Publications

    Pathwayi: xylan degradation

    This protein is involved in the pathway xylan degradation, which is part of Glycan degradation.
    View all proteins of this organism that are known to be involved in the pathway xylan degradation and in Glycan degradation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei44 – 441Inhibitor XIP-I1 Publication
    Active sitei119 – 1191NucleophilePROSITE-ProRule annotation
    Binding sitei170 – 1701Inhibitor XIP-I1 Publication
    Binding sitei176 – 1761Inhibitor XIP-I1 Publication
    Active sitei210 – 2101Proton donorBy similarity

    GO - Molecular functioni

    GO - Biological processi

    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. 4616.
    UniPathwayiUPA00114.

    Protein family/group databases

    CAZyiGH11. Glycoside Hydrolase Family 11.
    mycoCLAPiXYN11C_PENFN.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endo-1,4-beta-xylanase C (EC:3.2.1.8)
    Short name:
    Xylanase C
    Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase C
    Gene namesi
    Name:xynC
    OrganismiTalaromyces funiculosus (Fruitlet core rot fungus) (Penicillium funiculosum)
    Taxonomic identifieri28572 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeTalaromyces

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence analysisAdd
    BLAST
    Chaini18 – 223206Endo-1,4-beta-xylanase CPRO_5000066092Add
    BLAST

    Interactioni

    Subunit structurei

    Interacts directly with the wheat xylanase inhibiting protein I (XIP-I).1 Publication

    Structurei

    Secondary structure

    1
    223
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi40 – 445Combined sources
    Beta strandi47 – 537Combined sources
    Beta strandi57 – 637Combined sources
    Beta strandi68 – 758Combined sources
    Beta strandi77 – 8711Combined sources
    Beta strandi92 – 11423Combined sources
    Turni115 – 1173Combined sources
    Beta strandi118 – 12811Combined sources
    Turni131 – 1344Combined sources
    Beta strandi135 – 1439Combined sources
    Beta strandi146 – 15813Combined sources
    Beta strandi163 – 17614Combined sources
    Beta strandi179 – 1846Combined sources
    Helixi185 – 19410Combined sources
    Beta strandi201 – 21313Combined sources
    Beta strandi216 – 2238Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TE1X-ray2.50B34-223[»]
    3WP3X-ray1.98A/B28-223[»]
    ProteinModelPortaliQ9HFH0.
    SMRiQ9HFH0. Positions 34-223.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9HFH0.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 223189GH11PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni5 – 73Interaction with inhibitor XIP-I
    Regioni18 – 236Interaction with inhibitor XIP-I
    Regioni85 – 873Interaction with inhibitor XIP-I
    Regioni123 – 1308Interaction with inhibitor XIP-I

    Sequence similaritiesi

    Contains 1 GH11 (glycosyl hydrolase family 11) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.60.120.180. 1 hit.
    InterProiIPR013320. ConA-like_dom.
    IPR013319. GH11/12.
    IPR018208. GH11_AS_1.
    IPR033123. GH11_dom.
    IPR001137. Glyco_hydro_11.
    [Graphical view]
    PfamiPF00457. Glyco_hydro_11. 1 hit.
    [Graphical view]
    PRINTSiPR00911. GLHYDRLASE11.
    SUPFAMiSSF49899. SSF49899. 1 hit.
    PROSITEiPS00776. GH11_1. 1 hit.
    PS51761. GH11_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9HFH0-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKLFLAAIVL CATAATAFPS ELAQRAAGDL SKRQSITTSQ TGTNNGYYYS
    60 70 80 90 100
    FWTNGGGEVT YTNGDNGEYS VTWVDCGDFT SGKGWNPANA QTVTYSGEFN
    110 120 130 140 150
    PSGNAYLAVY GWTTDPLVEY YILESYGTYN PSSGLTSLGQ VTSDGGTYDI
    160 170 180 190 200
    YSTQRVNQPS IEGTSTFNQY WSVRTEKRVG GTVTTANHFA AWKALGLEMG
    210 220
    TYNYMIVSTE GYESSGSSTI TVS
    Length:223
    Mass (Da):24,045
    Last modified:March 1, 2001 - v1
    Checksum:i428CD224C8F13C77
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ278385 Genomic DNA. Translation: CAC15487.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ278385 Genomic DNA. Translation: CAC15487.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TE1X-ray2.50B34-223[»]
    3WP3X-ray1.98A/B28-223[»]
    ProteinModelPortaliQ9HFH0.
    SMRiQ9HFH0. Positions 34-223.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiGH11. Glycoside Hydrolase Family 11.
    mycoCLAPiXYN11C_PENFN.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00114.
    BRENDAi3.2.1.8. 4616.

    Miscellaneous databases

    EvolutionaryTraceiQ9HFH0.

    Family and domain databases

    Gene3Di2.60.120.180. 1 hit.
    InterProiIPR013320. ConA-like_dom.
    IPR013319. GH11/12.
    IPR018208. GH11_AS_1.
    IPR033123. GH11_dom.
    IPR001137. Glyco_hydro_11.
    [Graphical view]
    PfamiPF00457. Glyco_hydro_11. 1 hit.
    [Graphical view]
    PRINTSiPR00911. GLHYDRLASE11.
    SUPFAMiSSF49899. SSF49899. 1 hit.
    PROSITEiPS00776. GH11_1. 1 hit.
    PS51761. GH11_3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "A family 11 xylanase from Penicillium funiculosum is strongly inhibited by three wheat xylanase inhibitors."
      Furniss C.S., Belshaw N.J., Alcocer M.J., Williamson G., Elliott G.O., Gebruers K., Haigh N.P., Fish N.M., Kroon P.A.
      Biochim. Biophys. Acta 1598:24-29(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    2. "Substrate and product hydrolysis specificity in family 11 glycoside hydrolases: an analysis of Penicillium funiculosum and Penicillium griseofulvum xylanases."
      Berrin J.G., Ajandouz el H., Georis J., Arnaut F., Juge N.
      Appl. Microbiol. Biotechnol. 74:1001-1010(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    3. "The dual nature of the wheat xylanase protein inhibitor XIP-I: structural basis for the inhibition of family 10 and family 11 xylanases."
      Payan F., Leone P., Porciero S., Furniss C., Tahir T., Williamson G., Durand A., Manzanares P., Gilbert H.J., Juge N., Roussel A.
      J. Biol. Chem. 279:36029-36037(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 34-223 IN COMPLEX WITH INHIBITOR XIP-I.

    Entry informationi

    Entry nameiXYNC_TALFU
    AccessioniPrimary (citable) accession number: Q9HFH0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 9, 2014
    Last sequence update: March 1, 2001
    Last modified: April 13, 2016
    This is version 69 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

    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

    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 one 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.