IED ID | IndEnz0010000891 |
Enzyme Type ID | esterase000891 |
Protein Name |
Pectinesterase PE EC 3.1.1.11 Pectin methylesterase |
Gene Name | |
Organism | Actinidia deliciosa (Kiwi) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae asterids Ericales Actinidiaceae Actinidia Actinidia deliciosa (Kiwi) |
Enzyme Sequence | TAVTDIVPDVVVAKDGSGNFTTVGAAVAAAKDSSTARFVIYIKEGAYFEYVDVDKKKTNLMFIGDGIGKTWIKGNRSVVDGWTTFRSSTVAVVGTGFIARGISFENYAGPSKHQAVALRSGADFSAFYQCSFVGYQDTLYVHSLRQFYSECDVYGTIDFIFGNAAAVLQKCNLYARKPNENQKNIFTAQGRDDPNQNTGISILNCKVAAAADLIPVLSSFKTYLGRPWKEYSRTVFLLSQMESLIDPAGWLEWSGDFALTTLYYREYKNTGPGSNTTARVTWPGYAVTTNETEVIQFTVGNFIQGSQWLTSYNIPVYLNLT |
Enzyme Length | 321 |
Uniprot Accession Number | P85076 |
Absorption | |
Active Site | ACT_SITE 137; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10040; ACT_SITE 158; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10040 |
Activity Regulation | ACTIVITY REGULATION: Inhibited by PMEI. {ECO:0000269|PubMed:17932919}. |
Binding Site | BINDING 84; /note=Substrate; /evidence=ECO:0000250; BINDING 114; /note=Substrate; /evidence=ECO:0000250; BINDING 226; /note=Substrate; /evidence=ECO:0000250; BINDING 228; /note=Substrate; /evidence=ECO:0000250 |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=[(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol; Xref=Rhea:RHEA:22380, Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14573, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:140522, ChEBI:CHEBI:140523; EC=3.1.1.11; Evidence={ECO:0000269|PubMed:17932919}; |
DNA Binding | |
EC Number | 3.1.1.11 |
Enzyme Function | |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5. |
nucleotide Binding | |
Features | Active site (2); Binding site (4); Chain (1); Disulfide bond (1); Glycosylation (4); Modified residue (1); Site (2) |
Keywords | Acetylation;Aspartyl esterase;Cell wall biogenesis/degradation;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | MOD_RES 1; /note=N-acetylthreonine; /evidence=ECO:0000269|PubMed:17932919 |
Post Translational Modification | PTM: The N-glycans attached at Asn-75, Asn-275, Asn-290 and Asn-319 are complex oligosaccharides containing xylose, fucose, hexose and N-acetylglucosamine. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 35,368 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:22380 |
Cross Reference Brenda | 3.1.1.11; |