| IED ID | IndEnz0010001001 |
| Enzyme Type ID | esterase001001 |
| Protein Name |
Pectinesterase B PE B EC 3.1.1.11 Pectin methylesterase B |
| Gene Name | pemB Dda3937_03435 |
| Organism | Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Pectobacteriaceae Dickeya Dickeya dadantii Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)) |
| Enzyme Sequence | MSLTHYSGLAAAVSMSLILTACGGQTPNSARFQPVFPGTVSRPVLSAQEAGRFTPQHYFAHGGEYAKPVADGWTPTPIDTSRVTAAYVVGPRAGVAGATHTSIQQAVNAALRQHPGQTRVYIKLLPGTYTGTVYVPEGAPPLTLFGAGDRPEQVVVSLALDSMMSPADYRARVNPHGQYQPADPAWYMYNACATKAGATINTTCSAVMWSQSNDFQLKNLTVVNALLDTVDSGTHQAVALRTDGDRVQLENVRLLSRQDTFFVNTSDRQNSYVTDHYSRAYIKDSYIEGDVDYVFGRATAVFDRVRFHTVSSRGSKEAYVFAPDSIPSVKYGFLVINSQLTGDNGYRGAQKAKLGRAWDQGAKQTGYLPGKTANGQLVIRDSTIDSSYDLANPWGAAATTDRPFKGNISPQRDLDDIHFNRLWEYNTQVLLHE |
| Enzyme Length | 433 |
| Uniprot Accession Number | Q47474 |
| Absorption | |
| Active Site | ACT_SITE 259; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10040; ACT_SITE 292; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10040 |
| Activity Regulation | |
| Binding Site | BINDING 202; /note=Substrate; /evidence=ECO:0000250; BINDING 236; /note=Substrate; /evidence=ECO:0000250; BINDING 356; /note=Substrate; /evidence=ECO:0000250; BINDING 358; /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:8830237}; |
| DNA Binding | |
| EC Number | 3.1.1.11 |
| Enzyme Function | FUNCTION: Probably involved in the degradation of methylated oligogalacturonides present in the periplasm. More active on methylated oligogalacturides than on pectin. {ECO:0000269|PubMed:8830237}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:8830237}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:8830237}; |
| 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); Lipidation (2); Sequence conflict (1); Signal peptide (1); Topological domain (1) |
| Keywords | Aspartyl esterase;Cell outer membrane;Hydrolase;Lipoprotein;Membrane;Palmitate;Reference proteome;Signal |
| Interact With | |
| Induction | INDUCTION: By polygalacturonates and galacturonate. Repressed by kdgR. {ECO:0000269|PubMed:8830237}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:8830237}; Lipid-anchor {ECO:0000269|PubMed:8830237}. Note=Probably active in the periplasm. {ECO:0000305|PubMed:8830237}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 47,190 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:22380 |
| Cross Reference Brenda |