Detail Information for IndEnz0010000766
IED ID IndEnz0010000766
Enzyme Type ID esterase000766
Protein Name Pectinesterase 31
PE 31
EC 3.1.1.11
Pectin methylesterase 31
AtPME31
Gene Name PME31 ARATH31 At3g29090 MXE2.5
Organism Arabidopsis thaliana (Mouse-ear cress)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress)
Enzyme Sequence MATTRMVRVSQDGSGDYCSVQDAIDSVPLGNTCRTVIRLSPGIYRQPVYVPKRKNFITFAGISPEITVLTWNNTASKIEHHQASRVIGTGTFGCGSVIVEGEDFIAENITFENSAPEGSGQAVAIRVTADRCAFYNCRFLGWQDTLYLHHGKQYLKDCYIEGSVDFIFGNSTALLEHCHIHCKSQGFITAQSRKSSQESTGYVFLRCVITGNGQSGYMYLGRPWGPFGRVVLAYTYMDACIRNVGWHNWGNAENERSACFYEYRCFGPGSCSSERVPWSRELMDDEAGHFVHHSFVDPEQDRPWLCLRMGVKTPYSA
Enzyme Length 317
Uniprot Accession Number Q9LVQ0
Absorption
Active Site ACT_SITE 144; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10040; ACT_SITE 165; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10040
Activity Regulation ACTIVITY REGULATION: Does not require salt for activity. Not inhibited by kiwi pectin methylesterase inhibitor (PMEI). {ECO:0000269|PubMed:18936961}.
Binding Site BINDING 91; /note=Substrate; /evidence=ECO:0000250; BINDING 121; /note=Substrate; /evidence=ECO:0000250; BINDING 222; /note=Substrate; /evidence=ECO:0000250; BINDING 224; /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:18936961};
DNA Binding
EC Number 3.1.1.11
Enzyme Function FUNCTION: Acts in the modification of cell walls via demethylesterification of cell wall pectin (PubMed:18936961). Acts in a blockwise manner, resulting in a cell wall rigidification. {ECO:0000250, ECO:0000269|PubMed:18936961}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Fully active at 0 or 30 degrees Celsius, inactive at 55 degrees Celsius. {ECO:0000269|PubMed:18936961};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-8.5. {ECO:0000269|PubMed:18936961};
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); Site (1)
Keywords Aspartyl esterase;Hydrolase;Reference proteome
Interact With Q93ZX1
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 18805951; 21798944; 24367018; 27605050; 29307824; 32771166;
Motif
Gene Encoded By
Mass 35,520
Kinetics
Metal Binding
Rhea ID RHEA:22380
Cross Reference Brenda 3.1.1.11;