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 |