Q5BA93 · PLYL_EMENI

Function

function

Presents an endo-cleaving activity on the homogalacturonan (HG) region in pectin (PubMed:35802235).
Active on homogalacturonan with a degree of polymerization above 4, and does not appear to be affected by the degree of methylation of the substrate (PubMed:35802235).
Does not degrade linear rhamnogalacturonan (PubMed:35802235).

Catalytic activity

  • Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
    EC:4.2.2.2 (UniProtKB | ENZYME | Rhea)

Cofactor

Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Activity regulation

Inhibited by iron ions (PubMed:35802235).
Activated in presence of the surfactant polysorbate 20, while inhibited in the presence of Triton X-100 and sodium dodecyl sulfate (PubMed:35802235).
Inhibited in presence of the organic solvents methanol, ethanol, propan-2-ol and acetone (PubMed:35802235).

Kinetics

kcat is 280 sec-1 for homogalacturonan (HG) (at 45 degrees Celsius and at pH 8) (PubMed:35802235).
kcat is 357 sec-1 for apple pectin (at 45 degrees Celsius and at pH 8) (PubMed:35802235).
kcat is 272 sec-1 for citrus peel pectin (at 45 degrees Celsius and at pH 8) (PubMed:35802235).
kcat is 236 sec-1 for rhamnogalacturonan type I (at 45 degrees Celsius and at pH 8) (PubMed:35802235).

pH Dependence

Optimum pH is 8.

Temperature Dependence

Optimum temperature is 45 degrees Celsius.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site191Ca2+ (UniProtKB | ChEBI)
Binding site215Ca2+ (UniProtKB | ChEBI)
Binding site216Ca2+ (UniProtKB | ChEBI)
Binding site219Ca2+ (UniProtKB | ChEBI)
Active site271Proton acceptor

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functioncarbon-oxygen lyase activity, acting on polysaccharides
Molecular Functionmetal ion binding
Molecular Functionpectate lyase activity
Biological Processsymbiont-mediated disruption of host cell wall

Keywords

Enzyme and pathway databases

Protein family/group databases

    • PL9Polysaccharide Lyase Family 9

Names & Taxonomy

Protein names

  • Recommended name
    Pectate lyase PEL9
  • EC number
  • Alternative names
    • AnPL9

Gene names

    • Name
      PEL9
    • Synonyms
      PL9
    • ORF names
      ANIA_02537

Organism names

Accessions

  • Primary accession
    Q5BA93
  • Secondary accessions
    • C8VPM0

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-18
ChainPRO_501016854019-410Pectate lyase PEL9
Glycosylation234N-linked (GlcNAc...) asparagine

Keywords

Expression

Induction

Induced during growth on homogalacturonan (HG).

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region342-361Disordered
Region381-410Disordered

Sequence similarities

Belongs to the polysaccharide lyase 9 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    410
  • Mass (Da)
    43,891
  • Last updated
    2005-04-26 v1
  • Checksum
    1BF619F86AB51CE6
MMGKSVWVFAALFPAVLAADIYVSPDGSDDAAGTIDAPLQSIQLAVDQATAGSTIYLRGGTYTPTSNIQITKSGTASAPYVLRAYEGESVIIDGEELPGTPADLDASLDNADRGILHIQDAEYWEFYDLELINGPYGVYARDASNNHYERITTRNNYETGFQLQGESSNNVVLYLDSYGNRDPRKNGESADGFACKEGSGEGNILRGARLWNNVDDGLDLWYAVNPVHPRISANTSREFKSAVTIEDTIAWGNGFNRWDFTPFEGDGNGFKLGGGDDTDIGPADHIITNCIAFSNAKDGFTDNSQPGNFVLTRNTAWDNTAVGFKFGTAVATLTGNIAASNGEAPTSLSDEQISDGNSWDGDEDWDDGSFVSVDVSLVQGERNADGTIEPSGFLLPADGEEIGATTDWSA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BN001307
EMBL· GenBank· DDBJ
CBF87052.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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