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P07529 (XYNA_CRYAL) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Short name=Xylanase
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase
OrganismCryptococcus albidus (Filobasidium floriforme)
Taxonomic identifier100951 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaTremellomycetesFilobasidialesmitosporic FilobasidialesCryptococcus

Protein attributes

Sequence length332 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Requires at least three xylose residues for catalytic activity. Does not have activity against xylobiose.

Catalytic activity

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

Subcellular location

Secreted.

Sequence similarities

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

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   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

Signal peptide1 – 2121 Ref.2
Chain22 – 332311Endo-1,4-beta-xylanase
PRO_0000007971

Sites

Active site1201Proton donor By similarity
Active site2141Nucleophile By similarity

Amino acid modifications

Disulfide bond128 ↔ 160 By similarity
Disulfide bond247 ↔ 253 By similarity

Experimental info

Sequence conflict88 – 903TGT → AGL AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P07529 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: 1814FD823E48306A

FASTA33235,776
        10         20         30         40         50         60 
MLSSTTLLAI LSALALTSVQ AAPADKNSLD YLANKAGKRY LGTAVQSPQL VPGSQYVQIL 

        70         80         90        100        110        120 
ESQFDAITPE NEMKWEVVEP TEGNFDFTGT DKIVAEAKKT GSLLRGHNIC WDSQLRYAHE 

       130        140        150        160        170        180 
VAPKMKLCIN DYNIETVNAK SQAMAKVAAG LLAKGAPLHC IGMFKNAKRR SSGLLIRTAS 

       190        200        210        220        230        240 
SGLESHFIGG STPKDIPAAM NLFSDQGLEV PMTELDVRIP VNGNDMPANA TVAKEQVDDY 

       250        260        270        280        290        300 
YTSVSACLGN DLCPGVSIWQ FADPTSWIPG VFKGKLIAVS CTFSGCLLQY CVGYGAALLY 

       310        320        330 
DAQYQPKSTY YVVQQALKDG KNSGSKFHGI KL 

« Hide

References

[1]"Complete nucleotide sequence of the xylanase gene from the yeast Cryptococcus albidus."
Boucher F., Morosoli R., Durand S.
Nucleic Acids Res. 16:9874-9874(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: CCY 17-4-4.
[2]"Isolation and partial primary sequence of a xylanase from the yeast Cryptococcus albidus."
Morosoli R., Roy C., Yaguchi M.
Biochim. Biophys. Acta 870:473-478(1986)
Cited for: PROTEIN SEQUENCE OF 22-93.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X12596 Genomic DNA. Translation: CAA31109.1.
PIRJS0734.

3D structure databases

ProteinModelPortalP07529.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH10. Glycoside Hydrolase Family 10.
mycoCLAPXYN10A_CRYAL.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.80. 2 hits.
InterProIPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00331. Glyco_hydro_10. 2 hits.
[Graphical view]
SMARTSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYNA_CRYAL
AccessionPrimary (citable) accession number: P07529
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: July 1, 1989
Last modified: November 13, 2013
This is version 82 of the entry and version 2 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries