Endo-1,4-beta-xylanase A - Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935 / NRRL 34936) (Fusarium vascular wilt of tomato)

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B3A0S5 (XYNA_FUSO4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 12. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Gene names

ORF Names:

FOXG_17421

Organism

Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935 / NRRL 34936) (Fusarium vascular wilt of tomato) [Complete proteome]

Taxonomic identifier

426428 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › Nectriaceae › mitosporic Nectriaceae › Fusarium › Fusarium oxysporum species complex ›

Protein attributes

Sequence length	327 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Has xylanase activity. Ref.2
Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. Ref.2
Pathway	Glycan degradation; xylan degradation. Ref.2
Subunit structure	Monomer. Ref.2
Subcellular location	Secreted › extracellular space Ref.2.
Sequence similarities	Belongs to the glycosyl hydrolase 10 (cellulase F) family.
Biophysicochemical properties	Kinetic parameters: V_max=1.22 mmol/min/mg enzyme Ref.2 pH dependence: Optimum pH is 6-8. Ref.2 Temperature dependence: Optimum temperature is 40-50 degrees Celsius. Ref.2

Ontologies

Keywords
Biological process	Xylan degradation
Cellular component	Secreted
Molecular function	Hydrolase
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological_process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	endo-1,4-beta-xylanase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 327

327

Endo-1,4-beta-xylanase A

PRO_0000415231

Sites

Active site

131

Proton donor Ref.2

Active site

245

Nucleophile Ref.2

Amino acid modifications

Glycosylation

101

N-linked (GlcNAc...) Ref.2

Secondary structure

327

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

B3A0S5 [UniParc].

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

327

36,198

        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' referencesShow '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. Rep M. Nature 464:367-373(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 25-327.
[2]	"A new crystal structure of a Fusarium oxysporum GH10 xylanase reveals the presence of an extended loop on top of the catalytic cleft." Dimarogona M., Topakas E., Christakopoulos P., Chrysina E.D. Submitted (NOV-2011) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-24, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-101, X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AAXH01001232 Genomic DNA. No translation available.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3U7B	X-ray	1.94	A/B/C/D/E	1-327	[»]

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

UniPathway

UPA00114.

Family and domain databases

Gene3D

3.20.20.80. 1 hit.

InterPro

IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Pfam

PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]

PRINTS

PR00134. GLHYDRLASE10.

SMART

SM00633. Glyco_10. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS00591. GLYCOSYL_HYDROL_F10. Partial match.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

XYNA_FUSO4

Accession

Primary (citable) accession number: B3A0S5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 25, 2012
Last sequence update:	January 25, 2012
Last modified:	May 1, 2013
This is version 12 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program