Detail Information for IndEnz0003000075
IED ID IndEnz0003000075
Enzyme Type ID pectinase000075
Protein Name Probable endopolygalacturonase II
EPG-II
EC 3.2.1.15
Pectinase 2
Polygalacturonase II
PG-II
Polygalacturonase X2
Gene Name pgaII pg2
Organism Aspergillus aculeatus
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus aculeatus
Enzyme Sequence MHSFQLLGLAAVGSVVSAAPTASRVSDLVKKSSSTCTFTSASEASETSSSCSNVVLSNIEVPAGETLDLSDAADGATITFEGTTSFGYEEWDGPLIRFGGKQLTITQSDGAVIDGDGSRWWDSEGTNGGKTKPKFMYVHDVEDSTIKGLQIKNTPVQAISVQATNVYLTDITIDNSDGDDNGGHNTDGFDISESTGVYISGATVKNQDDCIAINSGENILFTGGTCSGGHGLSIGSVGGRDDNTVKNVTISDSTVTDSANGVRIKTIYGDTGDVSEITYSNIQLSGITDYGIVIEQDYENGSPTGTPSTGVPITDVTVDGVTGSIEDDAVQVYILCGDGSCSDWTWSGVDITGGETSSDCENVPSGASC
Enzyme Length 369
Uniprot Accession Number Q70HJ4
Absorption
Active Site ACT_SITE 208; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10052; ACT_SITE 230; /evidence=ECO:0000255|PROSITE-ProRule:PRU10052
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=(1,4-alpha-D-galacturonosyl)(n+m) + H(2)O = (1,4-alpha-D-galacturonosyl)(n) + (1,4-alpha-D-galacturonosyl)(m).; EC=3.2.1.15;
DNA Binding
EC Number 3.2.1.15
Enzyme Function FUNCTION: Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Disulfide bond (4); Glycosylation (1); Propeptide (1); Repeat (7); Signal peptide (1)
Keywords Cell wall biogenesis/degradation;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Repeat;Secreted;Signal;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..18; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 38,064
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda