Q6PRW6 · XYN_PENCH

Function

function

Cold active endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.

Catalytic activity

  • Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
    EC:3.2.1.8 (UniProtKB | ENZYME | Rhea)

pH Dependence

Optimum pH is 5.5.

Temperature Dependence

Optimum temperature is 15 degrees Celsius.

Pathway

Glycan degradation; xylan degradation.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site161Proton donor
Active site267Nucleophile

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functionendo-1,4-beta-xylanase activity
Biological Processxylan catabolic process

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Endo-1,4-beta-xylanase
  • EC number
  • Short names
    Xylanase
  • Alternative names
    • 1,4-beta-D-xylan xylanohydrolase

Gene names

    • Name
      Xyn
    • Synonyms
      xyl

Organism names

  • Taxonomic identifier
  • Strains
    • A3969.2
    • FS010
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Penicillium > Penicillium chrysogenum species complex

Accessions

  • Primary accession
    Q6PRW6
  • Secondary accessions
    • Q2PS23

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variant153in strain: A3969.2
Natural variant274in strain: A3969.2

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 2 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for signal, glycosylation, chain, disulfide bond.

TypeIDPosition(s)Description
Signal1-23
Glycosylation4N-linked (GlcNAc...) asparagine
ChainPRO_000042966324-353Endo-1,4-beta-xylanase
Disulfide bond285↔291
Glycosylation325N-linked (GlcNAc...) asparagine

Keywords

PTM databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain50-330GH10

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    353
  • Mass (Da)
    38,165
  • Last updated
    2004-07-05 v1
  • Checksum
    8C40976394FABD8E
MIPNITQLKTAALVMLFAGQALSGPVESRQASESIDAKFKAHGKKYLGNIADQGTLNGNPKTPAIIKANFGQLSPENSMKWDATEPSQGQFSFAGSDYFVEFAETNGKLIRGHTLVWHSQLPSWVSSITDKTTLTDVMKNHITTVMKQYKGKVYAWDVVNEIFEEDGTLRDSVFSRVLGEDFVRIAFETAREADPEAKLYINDYNLDSATSAKLQGMVSHVKKWIAAGVPIDGIGSQTHLGAGAGAAASGALNALASAGTEEVAVTELDIAGASSTDYVDVVNACLDQPKCVGITVWGVADPDSWRADESPLLFDASYNPKEAYNVSQLLSRQHAFDLYLKLGNLLLSRLHSD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY583585
EMBL· GenBank· DDBJ
AAS93681.1
EMBL· GenBank· DDBJ
mRNA
DQ304546
EMBL· GenBank· DDBJ
ABC18330.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

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