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 |