Q5B7Z3 · PLYE_EMENI
- ProteinPectate lyase E
- GeneplyE
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids254 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester.
Catalytic activity
Cofactor
Note: Binds 1 Ca2+ ion per subunit.
pH Dependence
Optimum pH is 9.2.
Temperature Dependence
Optimum temperature is 37 degrees Celsius.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | pectate lyase activity | |
Biological Process | cell wall organization | |
Biological Process | pectin catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePectate lyase E
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Nidulantes
Accessions
- Primary accessionQ5B7Z3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-17 | |||||
Sequence: MYQPLLLLPLLLTSAFA | ||||||
Chain | PRO_0000394585 | 18-254 | Pectate lyase E | |||
Sequence: NPHDPHIHHSLEKRASFPIPSSKGSVTFSSPKTISGTFDGGMKTYGRGVKCTGQDEGGDEDAVFILKDGATLKNAIIGADQIEGVHCEGSCTIENVWWTDVCEDALSLKGSGSGTHKIIGGGARNADDKVIQHNSGGKVIIQDFTVQNFGKLYRACGNCKKQFKRTVKISGVKASSGKALVGINSNYGDTASIKGCATSVKEICVEYEGTNNNSKEPKKKSSGPSSYCKYSEPLSKC | ||||||
Glycosylation | 229 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 227-246 | Polar residues | ||||
Sequence: TNNNSKEPKKKSSGPSSYCK | ||||||
Region | 227-254 | Disordered | ||||
Sequence: TNNNSKEPKKKSSGPSSYCKYSEPLSKC |
Sequence similarities
Belongs to the polysaccharide lyase 3 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length254
- Mass (Da)27,015
- Last updated2005-04-26 v1
- ChecksumF79401531CA1C715
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 227-246 | Polar residues | ||||
Sequence: TNNNSKEPKKKSSGPSSYCK |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DQ490486 EMBL· GenBank· DDBJ | ABF50862.1 EMBL· GenBank· DDBJ | mRNA | ||
AACD01000055 EMBL· GenBank· DDBJ | EAA63305.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BN001306 EMBL· GenBank· DDBJ | CBF82916.1 EMBL· GenBank· DDBJ | Genomic DNA |