Detail Information for IndEnz0010000450
IED ID IndEnz0010000450
Enzyme Type ID esterase000450
Protein Name Probable pectinesterase A
EC 3.1.1.11
Pectin methylesterase A
Gene Name pmeA NFIA_099600
Organism Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Aspergillus fischeri Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus)
Enzyme Sequence MHLPSLVLGLLGLGLTASASPIEERSNRSKAPDGCLTVGSSGKYSTIGAALDALGDSKSDACIFIGAGTYKEQITIDYKGKLTMYGETTDTSSYKKNQVTITHTISSPQAGTLDKSATVNVRSDGFKMYNINVINGYGKGSQAVALVANADKLGFYGCSFVGYQDTLYAKAGRQYYSNCYIEGATDYIFGNASAWFGECDIMSVGPGYITAMSRTTADQTTWYAIDNCNIYGKPGVDLTAKVYLGRPWRVLARVIYQNSQLSNIINPKGWTTMAEGATPLYYEYNNKGAGADTSKREYESSISGAVSMNTVLGSGWNSWIDTTY
Enzyme Length 324
Uniprot Accession Number A1DBT4
Absorption
Active Site ACT_SITE 165; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10040; ACT_SITE 186; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10040
Activity Regulation
Binding Site BINDING 142; /note=Substrate; /evidence=ECO:0000250; BINDING 246; /note=Substrate; /evidence=ECO:0000250; BINDING 248; /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 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); Binding site (3); Chain (1); Glycosylation (2); Signal peptide (1); Site (1)
Keywords Aspartyl esterase;Cell wall biogenesis/degradation;Glycoprotein;Hydrolase;Reference proteome;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..19; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 34,873
Kinetics
Metal Binding
Rhea ID RHEA:22380
Cross Reference Brenda