| IED ID | IndEnz0010000746 |
| Enzyme Type ID | esterase000746 |
| Protein Name |
Pectinesterase/pectinesterase inhibitor 18 AtPMEpcrA Cleaved into: Pectinesterase inhibitor 18 Pectin methylesterase inhibitor 18 ; Bifunctional pectinesterase 18/rRNA N-glycosylase PE 18 EC 3.1.1.11 EC 3.2.2.22 Pectin methylesterase 18 Pectin methylesterase 4 AtPME4 Ribosome-inactivating protein |
| Gene Name | PME18 ARATH4 At1g11580 T23J18.23 T23J18.24 T23J18.33 |
| 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 | MSNSNQPLLSKPKSLKHKNLCLVLSFVAILGSVAFFTAQLISVNTNNNDDSLLTTSQICHGAHDQDSCQALLSEFTTLSLSKLNRLDLLHVFLKNSVWRLESTMTMVSEARIRSNGVRDKAGFADCEEMMDVSKDRMMSSMEELRGGNYNLESYSNVHTWLSSVLTNYMTCLESISDVSVNSKQIVKPQLEDLVSRARVALAIFVSVLPARDDLKMIISNRFPSWLTALDRKLLESSPKTLKVTANVVVAKDGTGKFKTVNEAVAAAPENSNTRYVIYVKKGVYKETIDIGKKKKNLMLVGDGKDATIITGSLNVIDGSTTFRSATVAANGDGFMAQDIWFQNTAGPAKHQAVALRVSADQTVINRCRIDAYQDTLYTHTLRQFYRDSYITGTVDFIFGNSAVVFQNCDIVARNPGAGQKNMLTAQGREDQNQNTAISIQKCKITASSDLAPVKGSVKTFLGRPWKLYSRTVIMQSFIDNHIDPAGWFPWDGEFALSTLYYGEYANTGPGADTSKRVNWKGFKVIKDSKEAEQFTVAKLIQGGLWLKPTGVTFQEWL |
| Enzyme Length | 557 |
| Uniprot Accession Number | Q1JPL7 |
| Absorption | |
| Active Site | ACT_SITE 374; /note=Proton donor; for pectinesterase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU10040; ACT_SITE 395; /note=Nucleophile; for pectinesterase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU10040 |
| Activity Regulation | |
| Binding Site | BINDING 321; /note=Substrate; for pectinesterase activity; /evidence=ECO:0000250; BINDING 351; /note=Substrate; for pectinesterase activity; /evidence=ECO:0000250; BINDING 463; /note=Substrate; for pectinesterase activity; /evidence=ECO:0000250; BINDING 465; /note=Substrate; for pectinesterase activity; /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; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.; EC=3.2.2.22; |
| DNA Binding | |
| EC Number | 3.1.1.11; 3.2.2.22 |
| Enzyme Function | FUNCTION: Acts in the modification of cell walls via demethylesterification of cell wall pectin. Inhibits the elongation phase of protein synthesis. {ECO:0000269|PubMed:18222123}. |
| 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 (3); Erroneous gene model prediction (2); Region (2); Sequence conflict (3); Signal peptide (1); Site (1) |
| Keywords | Antimicrobial;Aspartyl esterase;Cell wall;Cell wall biogenesis/degradation;Direct protein sequencing;Fungicide;Hydrolase;Plant defense;Protein synthesis inhibitor;Reference proteome;Secreted;Signal;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..34; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12368499; 12535341; 12753585; 12805628; 14595688; 15215502; 15272873; 16299171; 16489130; 16920880; 17151019; 17153927; 17172353; 18650403; 18796151; 18854047; 23289948; 24367018; 27247031; 28082716; |
| Motif | |
| Gene Encoded By | |
| Mass | 61,687 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:22380 |
| Cross Reference Brenda |