IED ID | IndEnz0003000001 |
Enzyme Type ID | pectinase000001 |
Protein Name |
Endopolygalacturonase I EC 3.2.1.15 Pectinase 1 Polygalacturonase I PG-I |
Gene Name | pgaI pg1 pga1 |
Organism | Aspergillus niger |
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 niger |
Enzyme Sequence | MHSYQLLGLAAVGSLVSAAPAPSRVSEFAKKASTCTFTSASEASESISSCSDVVLSSIEVPAGETLDLSDAADGSTITFEGTTSFGYKEWKGPLIRFGGKDLTVTMADGAVIDGDGSRWWDSKGTNGGKTKPKFMYIHDVEDSTFKGINIKNTPVQAISVQATNVHLNDFTIDNSDGDDNGGHNTDGFDISESTGVYISGATVKNQDDCIAINSGESISFTGGTCSGGHGLSIGSVGGRDDNTVKNVTISDSTVSNSANGVRIKTIYKETGDVSEITYSNIQLSGITDYGIVIEQDYENGSPTGTPSTGIPITDVTVDGVTGTLEDDATQVYILCGDGSCSDWTWSGVDLSGGKTSDKCENVPSGASC |
Enzyme Length | 368 |
Uniprot Accession Number | P26213 |
Absorption | |
Active Site | ACT_SITE 207; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10052; ACT_SITE 229; /evidence=ECO:0000305 |
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. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Beta strand (23); Chain (1); Disulfide bond (4); Glycosylation (3); Helix (4); Propeptide (1); Repeat (6); Signal peptide (1); Turn (1) |
Keywords | 3D-structure;Cell wall biogenesis/degradation;Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Repeat;Secreted;Signal;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 1NHC; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 38,108 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.2.1.15; |