1IA5
POLYGALACTURONASE FROM ASPERGILLUS ACULEATUS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004650 | molecular_function | polygalacturonase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0045490 | biological_process | pectin catabolic process |
| A | 0047911 | molecular_function | galacturan 1,4-alpha-galacturonidase activity |
| A | 0071555 | biological_process | cell wall organization |
Functional Information from PROSITE/UniProt
| site_id | PS00502 |
| Number of Residues | 14 |
| Details | POLYGALACTURONASE Polygalacturonase active site. GgyCsgGHGLs.IGS |
| Chain | Residue | Details |
| A | GLY195-SER208 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 30 |
| Details | Repeat: {"description":"PbH1 1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 21 |
| Details | Repeat: {"description":"PbH1 2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Repeat: {"description":"PbH1 3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 21 |
| Details | Repeat: {"description":"PbH1 4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 22 |
| Details | Repeat: {"description":"PbH1 5","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"11518536","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"11518536","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"O-linked (Man...) threonine","evidences":[{"source":"PubMed","id":"11518536","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IA5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1IB4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 8 |
| Details | Glycosylation: {"description":"O-linked (Man...) serine","evidences":[{"source":"PubMed","id":"11518536","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IA5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1IB4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"11518536","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IA5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1IB4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1czf |
| Chain | Residue | Details |
| A | ASP181 | |
| A | ASP180 | |
| A | ASP159 | |
| A | HIS202 |
