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P35809 (XYNA_SCHCO) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Gene names
Name:XYNA
OrganismSchizophyllum commune (Split gill fungus)
Taxonomic identifier5334 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesSchizophyllaceaeSchizophyllum

Protein attributes

Sequence length197 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes xylans into xylobiose and xylose.

Catalytic activity

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

Pathway

Glycan degradation; xylan degradation.

Subcellular location

Secreted.

Sequence similarities

Belongs to the glycosyl hydrolase 11 (cellulase G) family.

Biophysicochemical properties

pH dependence:

Active over a very broad pH range.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   Cellular componentSecreted
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentextracellular region

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 – 197197Endo-1,4-beta-xylanase A
PRO_0000184071

Sites

Active site871Nucleophile Probable
Active site1841Proton donor By similarity

Amino acid modifications

Disulfide bond111 ↔ 160 Ref.2

Sequences

Sequence LengthMass (Da)Tools
P35809 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 42C8074E67C1FBE9

FASTA19720,979
        10         20         30         40         50         60 
SGTPSSTGTD GGYYYSWWTD GAGDATYQNN GGGSYTLTWS GNNGNLVGGK GWNPGAASRS 

        70         80         90        100        110        120 
ISYSGTYQPN GNSYLSVYGW TRSSLIEYYI VESYGSYDPS SAASHKGSVT CNGATYDILS 

       130        140        150        160        170        180 
TWRYNAPSID GTQTFEQFWS VRNPKKAPGG SISGTVDVQC HFDAWKGLGM NLGSEHNYQI 

       190 
VATEGYQSSG TATITVT 

« Hide

References

[1]Yaguchi M., Roy C., Ujiie M., Watson D.C., Wakarchuk W.
(In) Visser J., Beldman G., Kusters-van Someren M.A., Voragen A.G.J. (eds.); Xylans and xylanases, pp.149-154, Elsevier, Amsterdam (1992)
Cited for: PROTEIN SEQUENCE.
Strain: ATCC 38548 / Delmar / 13 / IHEM 5263.
[2]"Amino acid sequence and thermostability of xylanase A from Schizophyllum commune."
Oku T., Roy C., Watson D.C., Wakarchuk W., Campbell R., Yaguchi M., Jurasek L., Paice M.G.
FEBS Lett. 334:296-300(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, DISULFIDE BONDS.
Strain: ATCC 38548 / Delmar / 13 / IHEM 5263.
[3]"Identification of a glutamate residue at the active site of xylanase A from Schizophyllum commune."
Bray M.R., Clarke A.J.
Eur. J. Biochem. 219:821-827(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, ACTIVE SITE GLU-87.
Strain: ATCC 38548 / Delmar / 13 / IHEM 5263.

Cross-references

Sequence databases

PIRA44597.

3D structure databases

ProteinModelPortalP35809.
SMRP35809. Positions 3-196.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH11. Glycoside Hydrolase Family 11.
mycoCLAPXYN11A_SCHCO.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00114.

Family and domain databases

Gene3D2.60.120.180. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
PfamPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSPR00911. GLHYDRLASE11.
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYNA_SCHCO
AccessionPrimary (citable) accession number: P35809
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 13, 2013
This is version 75 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries