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B3A0S5 (XYNA_FUSO4) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 17. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endo-1,4-beta-xylanase A

Short name=Xylanase A
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase A
Endo-1,4-beta-xylanase GH10 A
Short name=FoXyn10a
Xylanase III
Gene names
ORF Names:FOXG_17421
OrganismFusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935 / NRRL 34936) (Fusarium vascular wilt of tomato) [Complete proteome]
Taxonomic identifier426428 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaemitosporic NectriaceaeFusariumFusarium oxysporum species complex

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the hydrolysis of the internal glycosidic bonds in heteroxylans, releasing mainly xylobiose and xylotriose. Most active on oat-spelt xylan. Ref.2

Catalytic activity

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. Ref.2 Ref.3

Pathway

Glycan degradation; xylan degradation. Ref.3

Subunit structure

Monomer. Ref.2 Ref.3

Subcellular location

Secretedextracellular space Ref.2 Ref.3.

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

Vmax=1.22 mmol/min/mg enzyme Ref.2 Ref.3

pH dependence:

Optimum pH is 6-8. Ref.3

Temperature dependence:

Optimum temperature is 40-50 degrees Celsius. Ref.3

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   Cellular componentSecreted
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionendo-1,4-beta-xylanase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 327327Endo-1,4-beta-xylanase A
PRO_0000415231

Sites

Active site1311Proton donor Ref.3
Active site2451Nucleophile Ref.3

Amino acid modifications

Glycosylation1011N-linked (GlcNAc...) Ref.3
Disulfide bond81 ↔ 123 Ref.3
Disulfide bond273 ↔ 279 Ref.3

Secondary structure

........................................................ 327
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
B3A0S5 [UniParc].

Last modified January 25, 2012. Version 1.
Checksum: DC4D2D291A37E7A0

FASTA32736,198
        10         20         30         40         50         60 
AASGLEAAMK AAGKQYFGTA LTVRNDQGEI DIINNKNEIG SITPENAMKW EAIQPNRGQF 

        70         80         90        100        110        120 
NWGPADQHAA AATSRGYELR CHTLVWHSQL PSWVANGNWN NQTLQAVMRD HINAVMGRYR 

       130        140        150        160        170        180 
GKCTHWDVVN EALNEDGTYR DSVFLRVIGE AYIPIAFRMA LAADPTTKLY YNDYNLEYGN 

       190        200        210        220        230        240 
AKTEGAKRIA RLVKSYGLRI DGIGLQAHMT SESTPTQNTP TPSRAKLASV LQGLADLGVD 

       250        260        270        280        290        300 
VAYTELDIRM NTPATQQKLQ TNADAYARIV GSCMDVKRCV GITVWGISDK YSWVPGTFPG 

       310        320 
EGSALLWNDN FQKKPSYTST LNTINRR 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAXH01001232 Genomic DNA. No translation available.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3U7BX-ray1.94A/B/C/D/E1-327[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiFOXG_17421T0; FOXG_17421P0; FOXG_17421.

Phylogenomic databases

OMARGQFNWG.
OrthoDBEOG7GJ6PM.

Enzyme and pathway databases

UniPathwayUPA00114.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSPR00134. GLHYDRLASE10.
SMARTSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameXYNA_FUSO4
AccessionPrimary (citable) accession number: B3A0S5
Secondary accession number(s): J9NQE2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: January 25, 2012
Last modified: April 16, 2014
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries