Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

B3A0S5

- XYNA_FUSO4

UniProt

B3A0S5 - XYNA_FUSO4

Protein

Endo-1,4-beta-xylanase A

Gene

FOXG_17421

Organism
Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935 / NRRL 34936) (Fusarium vascular wilt of tomato)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 19 (01 Oct 2014)
      Sequence version 1 (25 Jan 2012)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the hydrolysis of the internal glycosidic bonds in heteroxylans, releasing mainly xylobiose and xylotriose. Most active on oat-spelt xylan.1 Publication

    Catalytic activityi

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

    Kineticsi

      Vmax=1.22 mmol/min/mg enzyme1 Publication

      pH dependencei

      Optimum pH is 6-8.1 Publication

      Temperature dependencei

      Optimum temperature is 40-50 degrees Celsius.1 Publication

      Pathwayi

      Sites

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Active sitei131 – 1311Proton donor1 Publication
      Active sitei245 – 2451Nucleophile1 PublicationPROSITE-ProRule annotation

      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

      Hydrolase

      Keywords - Biological processi

      Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

      Enzyme and pathway databases

      UniPathwayiUPA00114.

      Names & Taxonomyi

      Protein namesi
      Recommended name:
      Endo-1,4-beta-xylanase A (EC:3.2.1.8)
      Short name:
      Xylanase A
      Alternative name(s):
      1,4-beta-D-xylan xylanohydrolase A
      Endo-1,4-beta-xylanase GH10 A
      Short name:
      FoXyn10a
      Xylanase III
      Gene namesi
      ORF Names:FOXG_17421
      OrganismiFusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935 / NRRL 34936) (Fusarium vascular wilt of tomato)
      Taxonomic identifieri426428 [NCBI]
      Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusariumFusarium oxysporum species complex
      ProteomesiUP000009097: Unplaced

      Subcellular locationi

      Secretedextracellular space 1 Publication

      GO - Cellular componenti

      1. extracellular space Source: UniProtKB-SubCell

      Keywords - Cellular componenti

      Secreted

      PTM / Processingi

      Molecule processing

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Chaini1 – 327327Endo-1,4-beta-xylanase APRO_0000415231Add
      BLAST

      Amino acid modifications

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Disulfide bondi81 ↔ 1231 Publication
      Glycosylationi101 – 1011N-linked (GlcNAc...)1 Publication
      Disulfide bondi273 ↔ 2791 Publication

      Keywords - PTMi

      Disulfide bond, Glycoprotein

      Interactioni

      Subunit structurei

      Monomer.1 Publication

      Structurei

      Secondary structure

      1
      327
      Legend: HelixTurnBeta strand
      Show more details
      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Helixi5 – 117
      Beta strandi16 – 216
      Helixi28 – 336
      Turni36 – 383
      Beta strandi41 – 466
      Helixi50 – 534
      Helixi63 – 7311
      Turni74 – 763
      Beta strandi78 – 8710
      Helixi92 – 954
      Helixi101 – 11818
      Turni119 – 1224
      Beta strandi124 – 1307
      Beta strandi137 – 1393
      Helixi143 – 1486
      Helixi152 – 16312
      Beta strandi167 – 1759
      Helixi181 – 19515
      Beta strandi202 – 2054
      Beta strandi208 – 2125
      Helixi224 – 23512
      Turni236 – 2383
      Beta strandi240 – 25314
      Helixi256 – 27520
      Beta strandi279 – 2857
      Helixi289 – 2913
      Helixi294 – 2974
      Beta strandi305 – 3073
      Helixi315 – 32511

      3D structure databases

      Select the link destinations:
      PDBe
      RCSB PDB
      PDBj
      Links Updated
      EntryMethodResolution (Å)ChainPositionsPDBsum
      3U7BX-ray1.94A/B/C/D/E1-327[»]
      ModBaseiSearch...
      MobiDBiSearch...

      Family & Domainsi

      Sequence similaritiesi

      Belongs to the glycosyl hydrolase 10 (cellulase F) family.Sequence Analysis

      Phylogenomic databases

      OrthoDBiEOG7GJ6PM.

      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.

      Sequencei

      Sequence statusi: Complete.

      B3A0S5-1 [UniParc]FASTAAdd to Basket

      « Hide

      AASGLEAAMK AAGKQYFGTA LTVRNDQGEI DIINNKNEIG SITPENAMKW    50
      EAIQPNRGQF NWGPADQHAA AATSRGYELR CHTLVWHSQL PSWVANGNWN 100
      NQTLQAVMRD HINAVMGRYR GKCTHWDVVN EALNEDGTYR DSVFLRVIGE 150
      AYIPIAFRMA LAADPTTKLY YNDYNLEYGN AKTEGAKRIA RLVKSYGLRI 200
      DGIGLQAHMT SESTPTQNTP TPSRAKLASV LQGLADLGVD VAYTELDIRM 250
      NTPATQQKLQ TNADAYARIV GSCMDVKRCV GITVWGISDK YSWVPGTFPG 300
      EGSALLWNDN FQKKPSYTST LNTINRR 327
      Length:327
      Mass (Da):36,198
      Last modified:January 25, 2012 - v1
      Checksum:iDC4D2D291A37E7A0
      GO

      Sequence databases

      Select the link destinations:
      EMBL
      GenBank
      DDBJ
      Links Updated
      AAXH01001232 Genomic DNA. No translation available.

      Genome annotation databases

      EnsemblFungiiFOXG_17421T0; FOXG_17421P0; FOXG_17421.

      Cross-referencesi

      Sequence databases

      Select the link destinations:
      EMBL
      GenBank
      DDBJ
      Links Updated
      AAXH01001232 Genomic DNA. No translation available.

      3D structure databases

      Select the link destinations:
      PDBe
      RCSB PDB
      PDBj
      Links Updated
      Entry Method Resolution (Å) Chain Positions PDBsum
      3U7B X-ray 1.94 A/B/C/D/E 1-327 [» ]
      ModBasei Search...
      MobiDBi Search...

      Protocols and materials databases

      Structural Biology Knowledgebase Search...

      Genome annotation databases

      EnsemblFungii FOXG_17421T0 ; FOXG_17421P0 ; FOXG_17421 .

      Phylogenomic databases

      OrthoDBi EOG7GJ6PM.

      Enzyme and pathway databases

      UniPathwayi UPA00114 .

      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.
      ProtoNeti Search...

      Publicationsi

      1. "Comparative genomics reveals mobile pathogenicity chromosomes in Fusarium."
        Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J., Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B., Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R., Antoniw J., Baker S.E.
        , Bluhm B.H., Breakspear A., Brown D.W., Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J., Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E., Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M., Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A., Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A., Kistler H.C., Rep M.
        Nature 464:367-373(2010) [PubMed] [Europe PMC] [Abstract]
        Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 25-327.
        Strain: 4287 / CBS 123668 / FGSC 9935 / NRRL 34936.
      2. "The alkaline xylanase III from Fusarium oxysporum F3 belongs to family F/10."
        Christakopoulos P., Nerinckx W., Kekos D., Macris B., Claeyssens M.
        Carbohydr. Res. 302:191-195(1997) [PubMed] [Europe PMC] [Abstract]
        Cited for: PROTEIN SEQUENCE OF 168-182 AND 290-313, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION.
        Strain: F3.
      3. "The structure of a GH10 xylanase from Fusarium oxysporum reveals the presence of an extended loop on top of the catalytic cleft."
        Dimarogona M., Topakas E., Christakopoulos P., Chrysina E.D.
        Acta Crystallogr. 68:735-742(2012) [PubMed] [Europe PMC] [Abstract]
        Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS), PROTEIN SEQUENCE OF 1-24, GLYCOSYLATION AT ASN-101, ACTIVE SITES, DISULFIDE BONDS.
        Strain: F3.

      Entry informationi

      Entry nameiXYNA_FUSO4
      AccessioniPrimary (citable) accession number: B3A0S5
      Secondary accession number(s): J9NQE2
      Entry historyi
      Integrated into UniProtKB/Swiss-Prot: January 25, 2012
      Last sequence update: January 25, 2012
      Last modified: October 1, 2014
      This is version 19 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, 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