ID   DRTE_ASPCI              Reviewed;         308 AA.
AC   A0A0U5CNN8;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   16-MAR-2016, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Acyltransferase drtE {ECO:0000303|PubMed:34468074};
DE            EC=2.3.-.- {ECO:0000269|PubMed:34468074};
DE   AltName: Full=Drimane-type sesquiterpene ester biosynthesis cluster protein E {ECO:0000303|PubMed:34468074};
DE   AltName: Full=Polyketide transferase drtE {ECO:0000305};
GN   Name=drtE {ECO:0000303|PubMed:34468074}; ORFNames=ASPCAL02981;
OS   Aspergillus calidoustus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=454130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SF006504;
RX   PubMed=26966204; DOI=10.1128/genomea.00102-16;
RA   Horn F., Linde J., Mattern D.J., Walther G., Guthke R., Scherlach K.,
RA   Martin K., Brakhage A.A., Petzke L., Valiante V.;
RT   "Draft genome sequences of fungus Aspergillus calidoustus.";
RL   Genome Announc. 4:0-0(2016).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=34468074; DOI=10.1002/anie.202108970;
RA   Huang Y., Hoefgen S., Valiante V.;
RT   "Biosynthesis of fungal drimane-type sesquiterpene esters.";
RL   Angew. Chem. Int. Ed. 60:23763-23770(2021).
CC   -!- FUNCTION: Acyltransferase; part of the gene cluster that mediates the
CC       biosynthesis of various drimane-type sesquiterpene esters, compounds
CC       that exhibit diverse biological activities and are widely present in
CC       eukaryotes (PubMed:34468074). The pathway begins with the synthesis of
CC       the backbone drimenol by the terpene cyclase drtB using farnesyl
CC       pyrophosphate (FPP) as substrate (PubMed:34468074). The cytochrome P450
CC       monooxygenase drtD is then responsible for the hydroxylations at C-6,
CC       C-9 and C-12, as well as the oxidation of hydroxyl groups at C-6 and C-
CC       11 to a ketone and an aldehyde, respectively (PubMed:34468074). Then,
CC       the biosynthesis can go in two directions, either the hydroxylated
CC       drimenol is further hydroxylated at C-2 and C-3 by an enzyme(s) not
CC       associated with the drt cluster, or the FAD-binding oxidoreductase drtC
CC       further oxidizes C-11 or C-12 to form the butyrolactone ring
CC       (PubMed:34468074). DrtB, drtD and drtC are solely responsible for the
CC       formation of the different drimane structures observed during drimane
CC       sesquiterpenes biosynthesis (PubMed:34468074). The polyketide synthase
CC       drtA synthesizes different lengths (C6 and C8) of PKS chains, which are
CC       then oxidized to varying degrees by the short-chain dehydrogenase drtF
CC       (PubMed:34468074). Finally, these PKS chains are transferred onto
CC       drimane sesquiterpenes by the acyltransferase drtE, forming the
CC       sesquiterpene esters (PubMed:34468074). In addition to the different
CC       fatty acyl-CoA chains produced by drtA, drtE is also able to use
CC       cinnamoyl-CoA as a substrate (PubMed:34468074).
CC       {ECO:0000269|PubMed:34468074}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:34468074}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes the production of all the sesquiterpene
CC       ester compounds. {ECO:0000269|PubMed:34468074}.
CC   -!- MISCELLANEOUS: The various drimane-type sesquiterpene esters produced
CC       by the A.calidoustus drt cluster include asperiene C, asperiene A, (6-
CC       Strobilactone-B) ester of (E,E)-6-carbonyl-7-hydroxy-2,4-octadienoic
CC       acid, ustusolate A, ustusolate C, ustusolide E, ustusoic acid A,
CC       (2'E,4'E)-6-(1'-carboxyhexa-2',4',-diene)-9-hydroxy-drim-7-ene-11,12-
CC       olide, RES-1149-2, as well as the 3 newly identified compounds
CC       calidoustene A, calidoustene B and calidoustene C.
CC       {ECO:0000269|PubMed:34468074}.
CC   -!- SIMILARITY: Belongs to the polyketide transferase af380 family.
CC       {ECO:0000305}.
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DR   EMBL; CDMC01000002; CEN60545.1; -; Genomic_DNA.
DR   ESTHER; 9euro-a0a0u5cnn8; Thiohydrolase.
DR   EnsemblFungi; CEN60545; CEN60545; ASPCAL02981.
DR   OrthoDB; 990069at2759; -.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000054771; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Reference proteome; Transferase.
FT   CHAIN           1..308
FT                   /note="Acyltransferase drtE"
FT                   /id="PRO_0000454534"
FT   DOMAIN          35..159
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   308 AA;  34562 MW;  54CBD533B6AB9A6E CRC64;
     MSFAFSKVEF EEVEFQTLDK LTLKARLYSA AKRGPALVMN PGYNCTKEIS APSAAAYFQS
     KGITCLIYDP RNCGQSDGTP RREIDPHRQV DDYLDAMTYM SGLDIVDPDQ IGFWGVSFSA
     SIALAAACYD PRAKCIITVS PWTFDFGITA AEAKDNFSRL VAEREAQALG NEPFYTAMVD
     EEGNNPIHVN VDWGDEVRAA VNEFVSLSAD GFVPTVTFQS YYKLFTFSPY LSLKFLGDTP
     LMMVVPEHDT VCPVEQQVKL YDAVEGPKEI YHAEGKRHLN MLAEDKFFEP MMKPQVEFFF
     KVMRGEAI