| IED ID | IndEnz0005000625 |
| Enzyme Type ID | lipase000625 |
| Protein Name |
Carboxylesterase patB EC 3.1.1.1 Patulin synthesis protein B |
| Gene Name | patB ACLA_093570 |
| Organism | Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) |
| 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 clavatus Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) |
| Enzyme Sequence | MLFTASLLLLLPWASAAPANLPIVDLGYQRHQAISFNSTGQYYSFTNIRYAEPPLGSRRFAPPVAPHGRSKNIVNGTGLGYKCPQALACWFNVQNKFTSAAAAGTPFDFNAAYEEVYTKDACTEPAKQDPLQSEDCLFLDVYVPQDVWQKGPQAAHQKGGAPVLVYLQDGAYVGGSKSDQNPAGLIARSREEGSSGMIYVGINYRLGVFGWLSGRKFTSSGGKPNAGLLDQRLALEWIQRHIHLFGGDPSRVTVMGVSAGGGSIIMQMTAYGRGISPPFAQVITQSPAWEPGTKTPAIEDDLFDTFLASLNVTSLDQARRLPSHALTDANYRLVASRPYGAGVLGPAIDGDFIPDSPKRLLLQGKANPGVRVLTSYTAAEGFGIAPANITDEASFQRYVGLMLAGTDASVRTHAATVLYPAVFDGSMPYRTQHDRASLLWADLAASCNTRYLHAAVRTPGYAIEYSVPPALHLSDTPSVFYNGPVADPTVNGTIAELLQRQIVRFVKTGNPNGEPDPEVPVYDGRDLLDLGDDGVLVRPDSTDNARCEYWQKVHF |
| Enzyme Length | 555 |
| Uniprot Accession Number | A1CFK9 |
| Absorption | |
| Active Site | ACT_SITE 258; /note=Acyl-ester intermediate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10039; ACT_SITE 380; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P22303 |
| Activity Regulation | |
| Binding Site | BINDING 258; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P22303 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+); Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10039}; |
| DNA Binding | |
| EC Number | 3.1.1.1 |
| Enzyme Function | FUNCTION: Carboxylesterase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:19383676, PubMed:24334092). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units (PubMed:19383676). The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol) (PubMed:24334092). These first reactions occur in the cytosol (By similarity). The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI (By similarity). The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole (By similarity). PatN catalyzes then the transformation of isoepoxydon into phyllostine (By similarity). The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol (By similarity). The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM (By similarity). Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (By similarity). The role of the carboxylesterase patB in the patulin pathway was not determined yet and requires further study (By similarity). {ECO:0000250|UniProtKB:A0A075TXZ3, ECO:0000269|PubMed:19383676, ECO:0000269|PubMed:24334092}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000305|PubMed:19383676}. |
| nucleotide Binding | |
| Features | Active site (2); Binding site (1); Chain (1); Glycosylation (5); Signal peptide (1) |
| Keywords | Cytoplasm;Glycoprotein;Hydrolase;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:A0A075TXZ3}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 59,936 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:21164 |
| Cross Reference Brenda |