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P33557

- XYN3_ASPKW

UniProt

P33557 - XYN3_ASPKW

Protein

Endo-1,4-beta-xylanase 3

Gene

xynC

Organism
Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus awamori var. kawachi)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (21 Mar 2012)
      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 sitei106 – 1061NucleophilePROSITE-ProRule annotation
    Active sitei197 – 1971Proton 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.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endo-1,4-beta-xylanase 3 (EC:3.2.1.8)
    Short name:
    Xylanase 3
    Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase 3
    Xylanase C
    Gene namesi
    Name:xynC
    ORF Names:AKAW_07136
    OrganismiAspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus awamori var. kawachi)
    Taxonomic identifieri1033177 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006812: Unassembled WGS sequence

    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 – 27271 PublicationAdd
    BLAST
    Chaini28 – 211184Endo-1,4-beta-xylanase 3PRO_0000007991Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi119 ↔ 138

    Keywords - PTMi

    Disulfide bond

    Structurei

    Secondary structure

    1
    211
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi33 – 386
    Helixi39 – 413
    Beta strandi42 – 476
    Helixi48 – 503
    Beta strandi52 – 6312
    Beta strandi65 – 739
    Beta strandi79 – 868
    Beta strandi90 – 10011
    Turni101 – 1044
    Beta strandi105 – 11511
    Turni118 – 1214
    Beta strandi122 – 1309
    Beta strandi133 – 14715
    Beta strandi150 – 16314
    Beta strandi166 – 1705
    Helixi172 – 1798
    Helixi180 – 1823
    Beta strandi187 – 21024

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BK1X-ray2.00A28-211[»]
    3RI8X-ray2.00A28-211[»]
    3RI9X-ray2.00A28-211[»]
    ProteinModelPortaliP33557.
    SMRiP33557. Positions 29-210.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP33557.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    OrthoDBiEOG7VQJQX.

    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.

    P33557-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKVTAAFAGL LVTAFAAPVP EPVLVSRSAG INYVQNYNGN LGDFTYDESA    50
    GTFSMYWEDG VSSDFVVGLG WTTGSSNAIT YSAEYSASGS SSYLAVYGWV 100
    NYPQAEYYIV EDYGDYNPCS SATSLGTVYS DGSTYQVCTD TRTNEPSITG 150
    TSTFTQYFSV RESTRTSGTV TVANHFNFWA QHGFGNSDFN YQVMAVEAWS 200
    GAGSASVTIS S 211
    Length:211
    Mass (Da):22,627
    Last modified:March 21, 2012 - v2
    Checksum:i86EFBEE12A869022
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 71F → S in AAC60542. (PubMed:1368843)Curated
    Sequence conflicti7 – 71F → S in BAA03576. (PubMed:1368843)Curated
    Sequence conflicti12 – 132VT → GH in AAC60542. (PubMed:1368843)Curated
    Sequence conflicti12 – 132VT → GH in BAA03576. (PubMed:1368843)Curated
    Sequence conflicti21 – 211E → Q in AAC60542. (PubMed:1368843)Curated
    Sequence conflicti21 – 211E → Q in BAA03576. (PubMed:1368843)Curated
    Sequence conflicti42 – 421G → A in AAC60542. (PubMed:1368843)Curated
    Sequence conflicti42 – 421G → A in BAA03576. (PubMed:1368843)Curated
    Sequence conflicti80 – 801T → S in AAC60542. (PubMed:1368843)Curated
    Sequence conflicti80 – 801T → S in BAA03576. (PubMed:1368843)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S45138 Genomic DNA. Translation: AAC60542.1.
    D14848 Genomic DNA. Translation: BAA03576.1.
    DF126466 Genomic DNA. Translation: GAA89022.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S45138 Genomic DNA. Translation: AAC60542.1 .
    D14848 Genomic DNA. Translation: BAA03576.1 .
    DF126466 Genomic DNA. Translation: GAA89022.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BK1 X-ray 2.00 A 28-211 [» ]
    3RI8 X-ray 2.00 A 28-211 [» ]
    3RI9 X-ray 2.00 A 28-211 [» ]
    ProteinModelPortali P33557.
    SMRi P33557. Positions 29-210.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH11. Glycoside Hydrolase Family 11.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    OrthoDBi EOG7VQJQX.

    Enzyme and pathway databases

    UniPathwayi UPA00114 .

    Miscellaneous databases

    EvolutionaryTracei P33557.

    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. "Cloning and sequencing of the xynC gene encoding acid xylanase of Aspergillus kawachii."
      Ito K., Iwashita K., Iwano K.
      Biosci. Biotechnol. Biochem. 56:1338-1340(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-34.
      Strain: NBRC 4308.
    2. "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used for brewing the Japanese distilled spirit shochu."
      Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H., Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.
      Eukaryot. Cell 10:1586-1587(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NBRC 4308.
    3. "Crystallographic and mutational analyses of an extremely acidophilic and acid-stable xylanase: biased distribution of acidic residues and importance of Asp-37 for catalysis at low pH."
      Fushinobu S., Ito K., Konno M., Wakagi T., Matsuzawa H.
      Protein Eng. 11:1121-1128(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 29-210.
      Strain: NBRC 4308.

    Entry informationi

    Entry nameiXYN3_ASPKW
    AccessioniPrimary (citable) accession number: P33557
    Secondary accession number(s): G7XQI2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: March 21, 2012
    Last modified: October 1, 2014
    This is version 94 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    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