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; |