IED ID | IndEnz0010000511 |
Enzyme Type ID | esterase000511 |
Protein Name |
Probable pectinesterase A EC 3.1.1.11 Pectin methylesterase A |
Gene Name | pmeA AFLA_001410 |
Organism | Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus flavus Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) |
Enzyme Sequence | MHGSLLKLALLSFSLASSAAVLPRDTGRTSAPSGCSTVGTSGDYSTIGDALTALGSSTADACIYIAAGTYEEQLVINYAGHLTLYGETTDTQTYKQNTVTITHTISSPEAGSLDNSATVNIKSDLVSVYNINIANGYGSGAQAVALVANADQLGFYACQFTGYQDTLYAKAGHQYYINSRIEGAVDYIFGDASAWFENCDIVSNGAGYITAMSRETTSDTAWYAIDHCNIKAASGVDLTGDVYLGRPWRVLARVIYQYSVLPDIINAKGWHSMADGATPLYYEFNNTGAGSDTSDREYLSTIDAPVAKETVLGDDYKNWVDSSY |
Enzyme Length | 324 |
Uniprot Accession Number | B8NPS7 |
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 (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..19; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 34,576 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:22380 |
Cross Reference Brenda |