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P29417 (XYNA_PENCH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 79. 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

Short name=Xylanase
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase
Gene names
Name:XYLP
OrganismPenicillium chrysogenum (Penicillium notatum)
Taxonomic identifier5076 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicilliumPenicillium chrysogenum complex

Protein attributes

Sequence length353 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes oat spelt and birchwood xylan randomly, yielding xylose and xylobiose as major end products.

Catalytic activity

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

Pathway

Glycan degradation; xylan degradation.

Subunit structure

Monomer.

Subcellular location

Secreted.

Post-translational modification

The N-terminus is blocked.

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
   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

Signal peptide1 – 2323 Potential
Chain24 – 353330Endo-1,4-beta-xylanase
PRO_0000007975

Sites

Active site1611Proton donor By similarity
Active site2671Nucleophile By similarity

Experimental info

Sequence conflict1531L → F AA sequence Ref.2
Sequence conflict1801E → S AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P29417 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: BF445C5E72FE2F94

FASTA35338,193
        10         20         30         40         50         60 
MIPNITQLKT AALVMLFAGQ ALSGPVESRQ ASESIDAKFK AHGKKYLGNI ADQGTLNGNP 

        70         80         90        100        110        120 
KTPAIIKANF GQLSPENSMK WDATEPSQGQ FSFAGSDYFV EFAETNGKLI RGHTLVWHSQ 

       130        140        150        160        170        180 
LPSWVSSITD KTTLTDVMKN HITTVMKQYK GKLYAWDVVN EIFEEDGTLR DSVFSRVLGE 

       190        200        210        220        230        240 
DFVRIAFETA READPEAKLY INDYNLDSAT SAKLQGMVSH VKKWIAAGVP IDGIGSQTHL 

       250        260        270        280        290        300 
GAGAGAAASG ALNALASAGT EEVAVTELDI AGATSTDYVD VVNACLDQPK CVGITVWGVA 

       310        320        330        340        350 
DPDSWRADES PLLFDASYNP KEAYNVSQLL SRQHAFDLYL KLGNLLLSRL HSD 

« Hide

References

[1]"Cloning and structural organization of a xylanase-encoding gene from Penicillium chrysogenum."
Haas H., Friedlin E., Stoeffler G., Redl B.
Gene 126:237-242(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 10002 / CBS 277.47 / NBRC 4626 / Wis. Q-176.
[2]"Purification, characterization and partial amino acid sequences of a xylanase produced by Penicillium chrysogenum."
Haas H., Herfurth E., Stoeffler G., Redl B.
Biochim. Biophys. Acta 1117:279-286(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 61-107; 109-123; 140-146; 153-180; 199-212 AND 228-237, CHARACTERIZATION.
Strain: ATCC 10002 / CBS 277.47 / NBRC 4626 / Wis. Q-176.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M98458 Genomic DNA. Translation: AAA16427.1.
PIRJN0575.

3D structure databases

ProteinModelPortalP29417.
SMRP29417. Positions 30-325.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH10. Glycoside Hydrolase Family 10.
mycoCLAPXYN10P_PENCH.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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.
PROSITEPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYNA_PENCH
AccessionPrimary (citable) accession number: P29417
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 79 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries