Detail Information for IndEnz0010000891
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;