IED ID | IndEnz0010001031 |
Enzyme Type ID | esterase001031 |
Protein Name |
Pectinesterase B PE B EC 3.1.1.11 Pectin methylesterase B |
Gene Name | pemB W5S_4605 |
Organism | Pectobacterium parmentieri |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Pectobacteriaceae Pectobacterium Pectobacterium parmentieri |
Enzyme Sequence | MTKTTYPGTAYRPILSEQEADRFTLPHYFTRRGHDGHSDTDVWQPTSIEVDPATPWVVGPQVGVDGATHGTVQQAVNAALRAQQDRPCIDIKLLPGIYTGAVYIPADAPPLTLFGTGEQPNDVVIQLALDSMFSPATYRETVNSHGEYQPGDPAWYMYDLCASKQNATIDTICAAVVWSQSDNLQMKNLTVVNALLDSVDGRAHQAVALRTDGDKIQLERVRLIGRQDTFFVNTSNLRNEYVTDRYSRAYIKDSYIEGDVDYVFGRATAVFDRVHFHTVSSRGAKDIHVFAPDSMPWAQYGFLAVSCRFTGDEGFSGGRKAKLGRAWDQGARQTGYQPNKTANGQLVIRDSTIDASYDREQPWGVAATTARPFAGNVDSARNLDDVQFNRLWEYNNIDEV |
Enzyme Length | 400 |
Uniprot Accession Number | P55743 |
Absorption | |
Active Site | ACT_SITE 228; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10040; ACT_SITE 261; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10040 |
Activity Regulation | |
Binding Site | BINDING 171; /note=Substrate; /evidence=ECO:0000250; BINDING 205; /note=Substrate; /evidence=ECO:0000250; BINDING 325; /note=Substrate; /evidence=ECO:0000250; BINDING 327; /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 | |
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); Sequence conflict (1); Site (1) |
Keywords | Aspartyl esterase;Hydrolase |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 44,446 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:22380 |
Cross Reference Brenda |