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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: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

    1. 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: 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
    Active sitei131Proton donor1 Publication1
    Active sitei245NucleophilePROSITE-ProRule annotation1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    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
    Proteomesi
    • UP000009097 Componentsi: Unassembled WGS sequence, Unplaced

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004152311 – 327Endo-1,4-beta-xylanase AAdd BLAST327

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi81 ↔ 1231 Publication
    Glycosylationi101N-linked (GlcNAc...)1 Publication1
    Disulfide bondi273 ↔ 2791 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    Secondary structure

    1327
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi5 – 11Combined sources7
    Beta strandi16 – 21Combined sources6
    Helixi28 – 33Combined sources6
    Turni36 – 38Combined sources3
    Beta strandi41 – 46Combined sources6
    Helixi50 – 53Combined sources4
    Helixi63 – 73Combined sources11
    Turni74 – 76Combined sources3
    Beta strandi78 – 87Combined sources10
    Helixi92 – 95Combined sources4
    Helixi101 – 118Combined sources18
    Turni119 – 122Combined sources4
    Beta strandi124 – 130Combined sources7
    Beta strandi137 – 139Combined sources3
    Helixi143 – 148Combined sources6
    Helixi152 – 163Combined sources12
    Beta strandi167 – 175Combined sources9
    Helixi181 – 195Combined sources15
    Beta strandi202 – 205Combined sources4
    Beta strandi208 – 212Combined sources5
    Helixi224 – 235Combined sources12
    Turni236 – 238Combined sources3
    Beta strandi240 – 253Combined sources14
    Helixi256 – 275Combined sources20
    Beta strandi279 – 285Combined sources7
    Helixi289 – 291Combined sources3
    Helixi294 – 297Combined sources4
    Beta strandi305 – 307Combined sources3
    Helixi315 – 325Combined sources11

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3U7BX-ray1.94A/B/C/D/E1-327[»]
    SMRiB3A0S5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini1 – 323GH10PROSITE-ProRule annotationAdd BLAST323

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 10 (cellulase F) family.Sequence analysis
    Contains 1 GH10 (glycosyl hydrolase family 10) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    OrthoDBiEOG092C45ID.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001000. GH10.
    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.
    PROSITEiPS51760. GH10_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    B3A0S5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    AASGLEAAMK AAGKQYFGTA LTVRNDQGEI DIINNKNEIG SITPENAMKW
    60 70 80 90 100
    EAIQPNRGQF NWGPADQHAA AATSRGYELR CHTLVWHSQL PSWVANGNWN
    110 120 130 140 150
    NQTLQAVMRD HINAVMGRYR GKCTHWDVVN EALNEDGTYR DSVFLRVIGE
    160 170 180 190 200
    AYIPIAFRMA LAADPTTKLY YNDYNLEYGN AKTEGAKRIA RLVKSYGLRI
    210 220 230 240 250
    DGIGLQAHMT SESTPTQNTP TPSRAKLASV LQGLADLGVD VAYTELDIRM
    260 270 280 290 300
    NTPATQQKLQ TNADAYARIV GSCMDVKRCV GITVWGISDK YSWVPGTFPG
    310 320
    EGSALLWNDN FQKKPSYTST LNTINRR
    Length:327
    Mass (Da):36,198
    Last modified:January 25, 2012 - v1
    Checksum:iDC4D2D291A37E7A0
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AAXH01001232 Genomic DNA. No translation available.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AAXH01001232 Genomic DNA. No translation available.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3U7BX-ray1.94A/B/C/D/E1-327[»]
    SMRiB3A0S5.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    OrthoDBiEOG092C45ID.

    Enzyme and pathway databases

    UniPathwayiUPA00114.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001000. GH10.
    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.
    PROSITEiPS51760. GH10_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    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: November 2, 2016
    This is version 30 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

    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.