IED ID | IndEnz0010000898 |
Enzyme Type ID | esterase000898 |
Protein Name |
Pectinesterase PE EC 3.1.1.11 Pectin methylesterase |
Gene Name | |
Organism | Daucus carota (Wild carrot) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae asterids campanulids Apiales Apiineae Apiaceae Apioideae Scandiceae Daucinae Daucus Daucus sect. Daucus Daucus carota (Wild carrot) |
Enzyme Sequence | QSSTVTPNVVVAADGSGDYKTVSEAVAAAPEDSKTRYVIRIKAGVYRENVDVPKKKKNIMFLGDGRTSTIITASKNVQDGSTTFNSATVAAVGAGFLARDITFQNTAGAAKHQAVALRVGSDLSAFYRCDILAYQDSLYVHSNRQFFINCFIAGTVDFIFGNAAVVLQDCDIHARRPGSGQKNMVTAQGRTDPNQNTGIVIQKSRIGATSDLQPVQSSFPTYLGRPWKEYSRTVVMQSSITNVINPAGWFPWDGNFALDTLYYGEYQNTGAGAATSGRVTWKGFKVITSSTEAQGFTPGSFIAGGSWLKATTFPFSLGL |
Enzyme Length | 319 |
Uniprot Accession Number | P83218 |
Absorption | |
Active Site | ACT_SITE 136; /note=Proton donor; ACT_SITE 157; /note=Nucleophile |
Activity Regulation | |
Binding Site | BINDING 83; /note=Substrate; /evidence=ECO:0000250; BINDING 113; /note=Substrate; /evidence=ECO:0000250; BINDING 225; /note=Substrate; /evidence=ECO:0000250; BINDING 227; /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; |
DNA Binding | |
EC Number | 3.1.1.11 |
Enzyme Function | FUNCTION: Catalyzes the deesterification of methyl-esterified D-galactosiduronic acid units in pectic compounds. It participates in modulating cell wall during fruit ripening, cell wall extension during pollen germination, and in defense mechanisms against pathogens. |
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); Beta strand (24); Binding site (4); Chain (1); Disulfide bond (1); Helix (9); Modified residue (1); Site (1); Turn (4) |
Keywords | 3D-structure;Aspartyl esterase;Cell wall;Cell wall biogenesis/degradation;Direct protein sequencing;Disulfide bond;Hydrolase;Pyrrolidone carboxylic acid;Secreted |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}. |
Modified Residue | MOD_RES 1; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:11964128 |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 1GQ8; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 34,254 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:22380 |
Cross Reference Brenda | 3.1.1.11; |