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P23360

- XYNA_THEAU

UniProt

P23360 - XYNA_THEAU

Protein

Endo-1,4-beta-xylanase

Gene

XYNA

Organism
Thermoascus aurantiacus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 4 (27 Apr 2001)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei157 – 1571Proton donor
    Active sitei263 – 2631Nucleophile

    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_THEAU.

    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
    TAXI
    Gene namesi
    Name:XYNA
    OrganismiThermoascus aurantiacus
    Taxonomic identifieri5087 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesThermoascaceaeThermoascus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 26263 PublicationsAdd
    BLAST
    Chaini27 – 329303Endo-1,4-beta-xylanasePRO_0000007985Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei27 – 271Pyrrolidone carboxylic acid
    Disulfide bondi281 ↔ 287

    Keywords - PTMi

    Disulfide bond, Pyrrolidone carboxylic acid

    Structurei

    Secondary structure

    1
    329
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi27 – 293
    Helixi32 – 376
    Turni38 – 403
    Beta strandi42 – 487
    Helixi50 – 534
    Helixi58 – 658
    Beta strandi67 – 737
    Helixi77 – 804
    Helixi90 – 10213
    Beta strandi105 – 1128
    Beta strandi114 – 1163
    Helixi119 – 1224
    Helixi127 – 14418
    Turni145 – 1473
    Beta strandi150 – 1578
    Beta strandi163 – 1653
    Helixi169 – 1735
    Helixi178 – 18912
    Beta strandi193 – 2019
    Beta strandi205 – 2073
    Helixi208 – 22215
    Beta strandi229 – 2324
    Turni238 – 2403
    Helixi241 – 25212
    Beta strandi257 – 26610
    Helixi271 – 28313
    Beta strandi287 – 2937
    Helixi297 – 2993
    Helixi303 – 3053
    Beta strandi308 – 3103
    Helixi318 – 32710

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GOKX-ray1.14A28-329[»]
    1GOMX-ray1.92A28-329[»]
    1GOOX-ray1.87A28-329[»]
    1GOQX-ray1.80A28-329[»]
    1GORX-ray1.70A28-329[»]
    1I1WX-ray0.89A28-329[»]
    1I1XX-ray1.11A27-329[»]
    1K6AX-ray1.14A27-329[»]
    1TUXX-ray1.80A28-325[»]
    2BNJX-ray1.60A28-329[»]
    3NYDX-ray1.23A/B27-329[»]
    3O2LX-ray2.00A27-329[»]
    4BS0X-ray1.09A/B28-329[»]
    ProteinModelPortaliP23360.
    SMRiP23360. Positions 27-328.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23360.

    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.

    P23360-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVRPTILLTS LLLAPFAAAS PILEERQAAQ SVDQLIKARG KVYFGVATDQ    50
    NRLTTGKNAA IIQADFGQVT PENSMKWDAT EPSQGNFNFA GADYLVNWAQ 100
    QNGKLIRGHT LVWHSQLPSW VSSITDKNTL TNVMKNHITT LMTRYKGKIR 150
    AWDVVNEAFN EDGSLRQTVF LNVIGEDYIP IAFQTARAAD PNAKLYINDY 200
    NLDSASYPKT QAIVNRVKQW RAAGVPIDGI GSQTHLSAGQ GAGVLQALPL 250
    LASAGTPEVA ITELDVAGAS PTDYVNVVNA CLNVQSCVGI TVWGVADPDS 300
    WRASTTPLLF DGNFNPKPAY NAIVQDLQQ 329
    Length:329
    Mass (Da):35,686
    Last modified:April 27, 2001 - v4
    Checksum:i8FE2F3D1A9F89815
    GO

    Sequence cautioni

    The sequence described in 1 Publication differs from that shown. Reason: Sequencing errors.
    The sequence described in 1 Publication differs from that shown. Reason: Sequencing errors.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti243 – 2431G → S in CAB65468. 1 PublicationCurated
    Sequence conflicti243 – 2431G → S in AAF24127. 1 PublicationCurated
    Sequence conflicti271 – 2711P → S in CAB65468. 1 PublicationCurated
    Sequence conflicti271 – 2711P → S in AAF24127. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ132635 Genomic DNA. Translation: CAB65468.1.
    AF127529 Genomic DNA. Translation: AAF24127.1.
    PIRiA59381.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ132635 Genomic DNA. Translation: CAB65468.1 .
    AF127529 Genomic DNA. Translation: AAF24127.1 .
    PIRi A59381.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GOK X-ray 1.14 A 28-329 [» ]
    1GOM X-ray 1.92 A 28-329 [» ]
    1GOO X-ray 1.87 A 28-329 [» ]
    1GOQ X-ray 1.80 A 28-329 [» ]
    1GOR X-ray 1.70 A 28-329 [» ]
    1I1W X-ray 0.89 A 28-329 [» ]
    1I1X X-ray 1.11 A 27-329 [» ]
    1K6A X-ray 1.14 A 27-329 [» ]
    1TUX X-ray 1.80 A 28-325 [» ]
    2BNJ X-ray 1.60 A 28-329 [» ]
    3NYD X-ray 1.23 A/B 27-329 [» ]
    3O2L X-ray 2.00 A 27-329 [» ]
    4BS0 X-ray 1.09 A/B 28-329 [» ]
    ProteinModelPortali P23360.
    SMRi P23360. Positions 27-328.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH10. Glycoside Hydrolase Family 10.
    mycoCLAPi XYN10A_THEAU.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P23360.

    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, sequencing and overexpression of Thermoascus aurantiacus xylanase A (xynA)."
      Bousson J.-C., Parriche M.
      Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Significance of structural homology of Thermoascus aurantiacus xylanase with the exoglucanase of Cellulomonas fimi."
      Srinivasa B.R., Vithayathil P.J., Roy R.P., Swaminathan K.R.
      J. Protein Chem. 9:337-338(1990)
      Cited for: PROTEIN SEQUENCE OF 27-328.
    3. "The primary structure of xylanase from Thermoascus aurantiacus."
      Srinivasa B.R., Swaminathan K.R., Ganapathy C., Roy R.P., Murthy S.K., Vithayathil P.J.
      Protein Seq. Data Anal. 4:15-20(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-328.
    4. "Anisotropic refinement of the structure of Thermoascus aurantiacus xylanase I."
      Teixeira S., Lo Leggio L., Pickersgill R.W., Cardin C.
      Acta Crystallogr. D 57:385-392(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-328, X-RAY CRYSTALLOGRAPHY (1.14 ANGSTROMS).
      Strain: IMI 216529.
    5. "High resolution structure and sequence of T. aurantiacus xylanase I: implications for the evolution of thermostability in family 10 xylanases and enzymes with (beta)alpha-barrel architecture."
      Lo Leggio L., Kalogiannis S., Bhat M.K., Pickersgill R.W.
      Proteins 36:295-306(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.14 ANGSTROMS).
      Strain: IMI 216529.

    Entry informationi

    Entry nameiXYNA_THEAU
    AccessioniPrimary (citable) accession number: P23360
    Secondary accession number(s): Q9UQZ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: April 27, 2001
    Last modified: October 1, 2014
    This is version 95 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Caution

    PubMed:1924265, PubMed:1924265 and PubMed:10409823 N-terminal modification was incorrect. X-ray structure has cyclic pyroglutamic acid.Curated

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3