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P07529

- XYNA_CRYAL

UniProt

P07529 - XYNA_CRYAL

Protein

Endo-1,4-beta-xylanase

Gene
N/A
Organism
Cryptococcus albidus (Filobasidium floriforme)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 2 (01 Jul 1989)
      Previous versions | rss
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    • Comment

    Functioni

    Requires at least three xylose residues for catalytic activity. Does not have activity against xylobiose.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei120 – 1201Proton donorBy similarity
    Active sitei214 – 2141NucleophilePROSITE-ProRule annotation

    GO - Molecular functioni

    1. endo-1,4-beta-xylanase activity Source: UniProtKB-EC

    GO - Biological processi

    1. xylan catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

    Protein family/group databases

    CAZyiGH10. Glycoside Hydrolase Family 10.
    mycoCLAPiXYN10A_CRYAL.

    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
    OrganismiCryptococcus albidus (Filobasidium floriforme)
    Taxonomic identifieri100951 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaTremellomycetesFilobasidialesmitosporic FilobasidialesCryptococcus

    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 – 21211 PublicationAdd
    BLAST
    Chaini22 – 332311Endo-1,4-beta-xylanasePRO_0000007971Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi128 ↔ 160By similarity
    Disulfide bondi247 ↔ 253By similarity

    Keywords - PTMi

    Disulfide bond

    Structurei

    3D structure databases

    ProteinModelPortaliP07529.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.20.20.80. 2 hits.
    InterProiIPR001000. Glyco_hydro_10.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00331. Glyco_hydro_10. 2 hits.
    [Graphical view]
    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.

    P07529-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSSTTLLAI LSALALTSVQ AAPADKNSLD YLANKAGKRY LGTAVQSPQL    50
    VPGSQYVQIL ESQFDAITPE NEMKWEVVEP TEGNFDFTGT DKIVAEAKKT 100
    GSLLRGHNIC WDSQLRYAHE VAPKMKLCIN DYNIETVNAK SQAMAKVAAG 150
    LLAKGAPLHC IGMFKNAKRR SSGLLIRTAS SGLESHFIGG STPKDIPAAM 200
    NLFSDQGLEV PMTELDVRIP VNGNDMPANA TVAKEQVDDY YTSVSACLGN 250
    DLCPGVSIWQ FADPTSWIPG VFKGKLIAVS CTFSGCLLQY CVGYGAALLY 300
    DAQYQPKSTY YVVQQALKDG KNSGSKFHGI KL 332
    Length:332
    Mass (Da):35,776
    Last modified:July 1, 1989 - v2
    Checksum:i1814FD823E48306A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti88 – 903TGT → AGL AA sequence 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12596 Genomic DNA. Translation: CAA31109.1.
    PIRiJS0734.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12596 Genomic DNA. Translation: CAA31109.1 .
    PIRi JS0734.

    3D structure databases

    ProteinModelPortali P07529.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH10. Glycoside Hydrolase Family 10.
    mycoCLAPi XYN10A_CRYAL.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.20.20.80. 2 hits.
    InterProi IPR001000. Glyco_hydro_10.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00331. Glyco_hydro_10. 2 hits.
    [Graphical view ]
    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. "Complete nucleotide sequence of the xylanase gene from the yeast Cryptococcus albidus."
      Boucher F., Morosoli R., Durand S.
      Nucleic Acids Res. 16:9874-9874(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: CCY 17-4-4.
    2. "Isolation and partial primary sequence of a xylanase from the yeast Cryptococcus albidus."
      Morosoli R., Roy C., Yaguchi M.
      Biochim. Biophys. Acta 870:473-478(1986)
      Cited for: PROTEIN SEQUENCE OF 22-93.

    Entry informationi

    Entry nameiXYNA_CRYAL
    AccessioniPrimary (citable) accession number: P07529
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 83 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3