Detail Information for IndEnz0010000510
IED ID IndEnz0010000510
Enzyme Type ID esterase000510
Protein Name Pectinesterase A
PE A
EC 3.1.1.11
Pectin methylesterase A
Gene Name pemA pem
Organism Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Pectobacteriaceae Dickeya Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi)
Enzyme Sequence MLKTISGTLALSLIIAASVHQAQAATTYNAVVSKSSSDGKTFKTIADAIASAPAGSTPFVILIKNGVYNERLTITRNNLLLKGESRNGAVIAAATAAGTLKSDGSKWGTAGSSTITISAKDFSAQSLTIRNDFDFPANQAKSDSDSSKIKDTQAVALYVTKSGDRAYFKDVSLVGYQDTLYVSGGRSFFSDCRISGTVDFIFGDGTALFNNCDLVSRYRADVKSGNVSGYLTAPSTNINQKYGLVITNSRVIRESDSVPAKSYGLGRPWHPTTTFSDGRYADPNAIGQTVFLNTSMDNHIYGWDKMSGKDKNGNTIWFNPEDSRFFEYKSYGAGAAVSKDRRQLTDAQAAEYTQSKVLGDWTPTLP
Enzyme Length 366
Uniprot Accession Number P0C1A8
Absorption
Active Site ACT_SITE 178; /note=Proton donor; ACT_SITE 199; /note=Nucleophile
Activity Regulation
Binding Site BINDING 109; /note=Substrate; /evidence=ECO:0000250; BINDING 153; /note=Substrate; /evidence=ECO:0000250; BINDING 219; /note=Substrate; /evidence=ECO:0000250; BINDING 226; /note=Substrate; /evidence=ECO:0000250; BINDING 230; /note=Substrate; /evidence=ECO:0000250; BINDING 267; /note=Substrate; /evidence=ECO:0000250; BINDING 269; /note=Substrate; /evidence=ECO:0000250; BINDING 272; /note=Substrate; via amide nitrogen and carbonyl oxygen; /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: Involved in maceration and soft-rotting of plant tissue. {ECO:0000250}.
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 (30); Binding site (8); Chain (1); Disulfide bond (1); Helix (7); Signal peptide (1); Site (1); Turn (1)
Keywords 3D-structure;Aspartyl esterase;Cell wall biogenesis/degradation;Disulfide bond;Hydrolase;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..24
Structure 3D X-ray crystallography (1)
Cross Reference PDB 1QJV;
Mapped Pubmed ID 1367534; 8370537;
Motif
Gene Encoded By
Mass 39,319
Kinetics
Metal Binding
Rhea ID RHEA:22380
Cross Reference Brenda 3.1.1.11;