IED ID | IndEnz0002019043 |
Enzyme Type ID | protease019043 |
Protein Name |
Serine-type carboxypeptidase acuI EC 3.4.16.- Aculin biosynthesis cluster protein I |
Gene Name | acuI ASPACDRAFT_1904405 |
Organism | Aspergillus aculeatus (strain ATCC 16872 / CBS 172.66 / WB 5094) |
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 aculeatus Aspergillus aculeatus (strain ATCC 16872 / CBS 172.66 / WB 5094) |
Enzyme Sequence | MLLPSFPVTGVATALLLRNAVHASQPGSSVQKARAYDRFSSRPTRDHAPRVQSSNTSTYRFWNDKTKPHLVESLPDVHFDLGEMYSGSINITSHRNESRSLFYIFQPKIGEPSDDLTIYLNGGPGCSSEQAFFQENGRFTWQPGTYAPVINQYSWVNLTNMLWVDQPVGTGYSVGTPTATNEAEVAADFLEFFSKFQDLYGIKNFRIFVSGESYAGRYVPYISSAMLDKNDTTHFNLSGKPAHPLHHLAPTNAVCTGALLYDACIGQWDWVQAELPAYPFVQQHASLFNFNETFMTSLATTYEECGYQAYFDEYFTFPASGIQPPKYMNYSECDIYNAIYNEAFSPNPCFNPYRVIDECPLLWDVLGFPTDLAYEPAPTTYFNRADVKRALHAPQNIEWELCSTDPVLVGGDGVSGPEQVGDDSPNPTEGSLPRVIEATNRVLIANGDWDYLIITNGTLLAIQNMTWHGQLGFAAAPATPIDIRMPDLQWAGVFDAQEGYGDLDGPQGVMGVQHYERGLMWAETFQAGHKQAQDQGRVSYRHLQWLLGEVDSL |
Enzyme Length | 553 |
Uniprot Accession Number | A0A1L9WN42 |
Absorption | |
Active Site | ACT_SITE 213; /evidence=ECO:0000250|UniProtKB:P52719; ACT_SITE 450; /evidence=ECO:0000250|UniProtKB:P52719; ACT_SITE 529; /evidence=ECO:0000250|UniProtKB:P52719 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.16.- |
Enzyme Function | FUNCTION: Serine-type carboxypeptidase; part of the gene cluster that mediates the biosynthesis of aculins (PubMed:26374386). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) acuA via condensation of acetate and malonate units (PubMed:26374386). The 6-methylsalicylic acid decarboxylase acuB then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol) (Probable). 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 acuC converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase acuD (Probable). Gentisyl alcohol is further oxidized by the oxidoreductase acuE that probably catalyzes hydroxylation of the aromatic ring (Probable). The aromatic system might then be opened by oxidation through a Baeyer-Villiger type of oxidation, which could be catalyzed by acuF, with the carboxylic acid at C-1 subsequently reduced to an aldehyde by acuG (Probable). Subsequently, a hemiacetal is formed, before the dehydrogenase acuH would reduce the double bond between C-4 and C-6 (Probable). Finally, keto-enol tautomerism results in formation of aculinic acid, which exists as two diastereomers (both R/S configurations at C-1) by non-enzymatic hemiacetal formation (Probable). The carboxypeptidase acuI could be involved in the linking of aculinic acid to an aculene A moiety produced by the aculene biosynthesis cluster and which leads to the production of aculin A (Probable). AcuI may also be involved in the attachment of proline to aculinic acid to form epi-aculins A and B (Probable). {ECO:0000250|UniProtKB:A0A075TRC0, ECO:0000269|PubMed:26374386, ECO:0000305|PubMed:26374386}. |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305|PubMed:26374386}. |
nucleotide Binding | |
Features | Active site (3); Chain (1); Glycosylation (10); Region (2); Signal peptide (1) |
Keywords | Carboxypeptidase;Glycoprotein;Hydrolase;Protease;Reference proteome;Signal |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 61,789 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |