IED ID | IndEnz0005000817 |
Enzyme Type ID | lipase000817 |
Protein Name |
Rhamnogalacturonan acetylesterase RGAE EC 3.1.1.86 |
Gene Name | AN2528 |
Organism | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
Enzyme Sequence | MKSIALTSLSLLPSALAQTIYLAGDSTMASSTPGWGDYIADSVSVEISNQAIGGRSARSYTREGRFQAIADVLQAGDYVVIEFGHNDGGSLSNDNGRTDCPGDGDETCETVYNGVAETVLTFPAYIENAALLFLEKGANVLISSQTPNNPWESGTFSYTPNRFVGYAELAAQRAGVDYVDHGAYTASIFEALGADTVNSFYPNDHTHTNAEGSSVVADAFLKAVVCSGVALNDVLTRTDFDGECL |
Enzyme Length | 245 |
Uniprot Accession Number | Q5BAA2 |
Absorption | |
Active Site | ACT_SITE 26; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q00017; ACT_SITE 204; /evidence=ECO:0000250|UniProtKB:Q00017; ACT_SITE 207; /evidence=ECO:0000250|UniProtKB:Q00017 |
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:16844780}; |
DNA Binding | |
EC Number | 3.1.1.86 |
Enzyme Function | FUNCTION: Plays a key role in the degradation of rhamnogalacturonan in the cell wall. Involved in degradation of pectin. {ECO:0000269|PubMed:16844780, ECO:0000269|PubMed:22589326}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Disulfide bond (2); Signal peptide (1) |
Keywords | Disulfide bond;Hydrolase;Reference proteome;Secreted;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:22589326}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 25,870 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |