| IED ID | IndEnz0010001032 |
| Enzyme Type ID | esterase001032 |
| Protein Name |
Pectinesterase A PE A EC 3.1.1.11 Pectin methylesterase A PME |
| Gene Name | pemA pem Dda3937_03374 |
| 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 | MLKTISGTLALSLIIAASVHQAQAATTYNAVVSKSSSDGKTFKTIADAIASAPAGSTPFVILIKNGVYNERLTITRNNLHLKGESRNGAVIAAATAAGTLKSDGSKWGTAGSSTITISAKDFSAQSLTIRNDFDFPANQAKSDSDSSKIKDTQAVALYVTKSGDRAYFKDVSLVGYQDTLYVSGGRSFFSDCRISGTVDFIFGDGTALFNNCDLVSRYRADVKSGNVSGYLTAPSTNINQKYGLVITNSRVIRESDSVPAKSYGLGRPWHPTTTFSDGRYADPNAIGQTVFLNTSMDNHIYGWDKMSGKDKNGNTIWFNPEDSRFFEYKSYGAGATVSKDRRQLTDAQAAEYTQSKVLGDWTPTLP |
| Enzyme Length | 366 |
| Uniprot Accession Number | P0C1A9 |
| Absorption | |
| Active Site | ACT_SITE 178; /note=Proton donor; /evidence=ECO:0000269|PubMed:17717531; ACT_SITE 199; /note=Nucleophile; /evidence=ECO:0000269|PubMed:17717531 |
| Activity Regulation | |
| Binding Site | BINDING 109; /note=Substrate; /evidence=ECO:0000269|PubMed:17717531; BINDING 153; /note=Substrate; /evidence=ECO:0000269|PubMed:17717531; BINDING 219; /note=Substrate; /evidence=ECO:0000269|PubMed:17717531; BINDING 226; /note=Substrate; /evidence=ECO:0000269|PubMed:17717531; BINDING 230; /note=Substrate; /evidence=ECO:0000269|PubMed:17717531; BINDING 267; /note=Substrate; /evidence=ECO:0000269|PubMed:17717531; BINDING 269; /note=Substrate; /evidence=ECO:0000269|PubMed:17717531; BINDING 272; /note=Substrate; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000269|PubMed:17717531 |
| 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:17717531, ECO:0000269|PubMed:8370537}; |
| DNA Binding | |
| EC Number | 3.1.1.11 |
| Enzyme Function | FUNCTION: Catalyzes the first step in maceration and soft-rotting of plant tissue. {ECO:0000305|PubMed:17717531, ECO:0000305|PubMed:8370537}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5. {ECO:0000305|PubMed:17717531, ECO:0000305|PubMed:8370537}. |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (29); Binding site (8); Chain (1); Disulfide bond (1); Helix (7); Mutagenesis (9); Signal peptide (1); Site (1); Turn (1) |
| Keywords | 3D-structure;Aspartyl esterase;Cell wall biogenesis/degradation;Direct protein sequencing;Disulfide bond;Hydrolase;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8370537}. Note=Upon overexpression also accumulates in the periplasm. {ECO:0000269|PubMed:8370537}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000269|PubMed:8370537 |
| Structure 3D | X-ray crystallography (7) |
| Cross Reference PDB | 2NSP; 2NST; 2NT6; 2NT9; 2NTB; 2NTP; 2NTQ; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 39,373 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:22380 |
| Cross Reference Brenda |