| IED ID | IndEnz0005000698 |
| Enzyme Type ID | lipase000698 |
| Protein Name |
Rhamnogalacturonan acetylesterase RGAE EC 3.1.1.86 |
| Gene Name | rha1 |
| 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 | MKTAALAPLFFLPSALATTVYLAGDSTMAKNGGGSGTNGWGEYLASYLSATVVNDAVAGRSARSYTREGRFENIADVVTAGDYVIVEFGHNDGGSLSTDNGRTDCSGTGAEVCYSVYDGVNETILTFPAYLENAAKLFTAKGAKVILSSQTPNNPWETGTFVNSPTRFVEYAELAAEVAGVEYVDHWSYVDSIYETLGNATVNSYFPIDHTHTSPAGAEVVAEAFLKAVVCTGTSLKSVLTTTSFEGTCL |
| Enzyme Length | 250 |
| Uniprot Accession Number | Q00017 |
| Absorption | |
| Active Site | ACT_SITE 26; /note=Nucleophile; /evidence=ECO:0000305|PubMed:10801485; ACT_SITE 209; /evidence=ECO:0000269|PubMed:10801485; ACT_SITE 212; /evidence=ECO:0000269|PubMed:10801485 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolytic cleavage of 2-O-acetyl- or 3-O-acetyl groups of alpha-D-galacturonic acid in rhamnogalacturonan I.; EC=3.1.1.86; Evidence={ECO:0000269|PubMed:7592973}; |
| DNA Binding | |
| EC Number | 3.1.1.86 |
| Enzyme Function | FUNCTION: Plays a key role in the degradation of rhamnogalacturonan in the cell wall. Acts in synergy together with rhamnogalacturonase A (RGase A) and rhamnogalacturonase B (RGase B). {ECO:0000269|PubMed:7592973}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (9); Chain (1); Disulfide bond (2); Glycosylation (2); Helix (11); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: Carbohydrate at Asn-199 is composed of GlcNAc and Man. |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000269|PubMed:7592973 |
| Structure 3D | X-ray crystallography (5) |
| Cross Reference PDB | 1DEO; 1DEX; 1K7C; 1PP4; 3C1U; |
| Mapped Pubmed ID | 14993671; |
| Motif | |
| Gene Encoded By | |
| Mass | 26,351 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.1.1.86; |