Detail Information for IndEnz0010000495
IED ID IndEnz0010000495
Enzyme Type ID esterase000495
Protein Name Pectinesterase A
EC 3.1.1.11
Pectin methylesterase A
Gene Name pmeA AN3390
Organism Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Enzyme Sequence MRVQSYLSLFSLVGAALCAPREHFKRTARTSAPAGCLTVGGSGTYSTIGAAFAALGSSSSEACIYISAGTYKEQLTFQYAGPLTLYGETTDTSSYKKNTVTITHTISSPEAGSLVASATVNAAMDNFTMYNINVVNGYGKGAQAVALAASGERQGYYGCQFLGYQDTLYARVGVQYYSNCYIEGAVDYIFGDASAWFGECDIVSNGAGYITAMSRETASDPAWYCFDHCNIYGKSGLDLTGDVYLGRPWRVLARVIYQNSELSDIINAAGWTTMAEGATPLYYEIGNTGDGADTSKRLYLSEISAAVTKATVLGSDWTDWLDWSY
Enzyme Length 325
Uniprot Accession Number Q5B7U0
Absorption
Active Site ACT_SITE 166; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10040; ACT_SITE 187; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10040
Activity Regulation
Binding Site BINDING 143; /note=Substrate; /evidence=ECO:0000250; BINDING 247; /note=Substrate; /evidence=ECO:0000250; BINDING 249; /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:16844780};
DNA Binding
EC Number 3.1.1.11
Enzyme Function FUNCTION: Involved in maceration and soft-rotting of plant tissue. Active against citrus pectin. {ECO:0000269|PubMed:16844780}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:16844780};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:16844780};
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 (1); 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..18; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 34,859
Kinetics
Metal Binding
Rhea ID RHEA:22380
Cross Reference Brenda