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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)DescriptionActionsGraphical viewLength
    Binding sitei44Inhibitor XIP-I1 Publication1
    Active sitei119NucleophilePROSITE-ProRule annotation1
    Binding sitei170Inhibitor XIP-I1 Publication1
    Binding sitei176Inhibitor XIP-I1 Publication1
    Active sitei210Proton donorBy similarity1

    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)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 17Sequence analysisAdd BLAST17
    ChainiPRO_500006609218 – 223Endo-1,4-beta-xylanase CAdd BLAST206

    Interactioni

    Subunit structurei

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

    Structurei

    Secondary structure

    1223
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi40 – 44Combined sources5
    Beta strandi47 – 53Combined sources7
    Beta strandi57 – 63Combined sources7
    Beta strandi68 – 75Combined sources8
    Beta strandi77 – 87Combined sources11
    Beta strandi92 – 114Combined sources23
    Turni115 – 117Combined sources3
    Beta strandi118 – 128Combined sources11
    Turni131 – 134Combined sources4
    Beta strandi135 – 143Combined sources9
    Beta strandi146 – 158Combined sources13
    Beta strandi163 – 176Combined sources14
    Beta strandi179 – 184Combined sources6
    Helixi185 – 194Combined sources10
    Beta strandi201 – 213Combined sources13
    Beta strandi216 – 223Combined sources8

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ9HFH0.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini35 – 223GH11PROSITE-ProRule annotationAdd BLAST189

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni5 – 7Interaction with inhibitor XIP-I3
    Regioni18 – 23Interaction with inhibitor XIP-I6
    Regioni85 – 87Interaction with inhibitor XIP-I3
    Regioni123 – 130Interaction with inhibitor XIP-I8

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1TE1X-ray2.50B34-223[»]
    3WP3X-ray1.98A/B28-223[»]
    ProteinModelPortaliQ9HFH0.
    SMRiQ9HFH0.
    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...

    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: November 2, 2016
    This is version 71 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.