ID   PYTI_ASPTE              Reviewed;         310 AA.
AC   P9WEZ1; A0A5M3YSX7;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   12-AUG-2020, sequence version 1.
DT   25-MAY-2022, entry version 8.
DE   RecName: Full=Thioesterase pytI {ECO:0000303|PubMed:32077283};
DE            EC=3.1.-.- {ECO:0000305|PubMed:32077283};
DE   AltName: Full=Pyranterreones biosynthesis cluster protein I {ECO:0000303|PubMed:32077283};
GN   Name=pytI {ECO:0000303|PubMed:32077283};
GN   ORFNames=ATETN484_0003083900, g7163;
OS   Aspergillus terreus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=33178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=TN-484;
RA   Kanamasa S., Takahashi H.;
RT   "Aspergillus terreus TN-484 whole genome shotgun sequence.";
RL   Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, FUNCTION, DISRUPTION
RP   PHENOTYPE, AND PATHWAY.
RC   STRAIN=MEFC01;
RX   PubMed=32077283; DOI=10.1021/acs.jnatprod.9b01140;
RA   Tang S., Zhang W., Li Z., Li H., Geng C., Huang X., Lu X.;
RT   "Discovery and characterization of a PKS-NRPS hybrid in Aspergillus terreus
RT   by genome mining.";
RL   J. Nat. Prod. 83:473-480(2020).
CC   -!- FUNCTION: Thioesterase; part of the gene cluster that mediates the
CC       biosynthesis of pyranterreones, a family of antioxidative compounds
CC       (PubMed:32077283). The first step of pyranonigrins biosynthesis is
CC       performed by the hybrid PKS-NRPS synthetase pytA that condenses 4
CC       malonyl-CoA units ato the acetyl starter unit by the modular PKS of
CC       pytA (PubMed:32077283). The acyl chain is then connected to an L-serine
CC       through the amide bond by the modular NRPS of pytA (PubMed:32077283). A
CC       tetramic acid is formed and released from the PKS-NRPS pytA to give
CC       pyranterreone 5 with the help of the thioesterase pytI
CC       (PubMed:32077283). Pyranterreone 5 could be methylated by pytC to
CC       afford pyranterreone 6 (Probable). Both pyranterreones 5 and 6 are
CC       subsequently oxidized by the FAD-linked oxidoreductase pytB and the
CC       cytochrome P450 monooxygenase pytD to form the fused gamma-pyrone core,
CC       resulting in pyranterreones 7 and 11, respectively (PubMed:32077283).
CC       The hydroxy group at C-8 of pyranterreones 7 and 11 are dehydrated by
CC       the aspartyl protease pytH to form a delta-7 double bond to give
CC       pyranterreones 3 and 1, 2 accordingly (PubMed:32077283). The exo-
CC       methylene of pyranterreone 3 could be reduced into a pendant methyl by
CC       reductase pytE to provide pyranterreone 4, also known as cordylactam
CC       (Probable). Pyranterreone 4 can be reconverted to pyranterreone 3
CC       through pytB-catalyzed dehydrogenation or further oxidized to
CC       pyranterreones 9 and 10 (Probable). {ECO:0000269|PubMed:32077283,
CC       ECO:0000305|PubMed:32077283}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:32077283}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC       transcription factor pytR. {ECO:0000269|PubMed:32077283}.
CC   -!- DISRUPTION PHENOTYPE: Impairs the production of pyranterreones.
CC       {ECO:0000269|PubMed:32077283}.
CC   -!- SIMILARITY: Belongs to the AMT4 thioesterase family. {ECO:0000305}.
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DR   EMBL; BKZM02000003; GES59613.1; -; Genomic_DNA.
DR   EMBL; MN699960; QIH14018.1; -; Genomic_DNA.
DR   AlphaFoldDB; P9WEZ1; -.
DR   SMR; P9WEZ1; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001031; Thioesterase.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..310
FT                   /note="Thioesterase pytI"
FT                   /id="PRO_0000450473"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          168..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   310 AA;  34383 MW;  D079A09A5874C994 CRC64;
     MDIVAHIQGD PGSSLTPLIL IHAISGLALP YFALRPLSTD SDDGDSDKSR PVYGLSSPIF
     ESVSAFRRHG KSLPSLALEY VRIIRREIQP RGPYLLGGWS MGGMLAIEMA AIFVAQGETV
     KHVVMIDSLN PEVYPPFQDS QEHQVLSTIM YNAIAWRVEG LEEACMPTLS DDASTTTSSD
     NSRASTDHGA DSEVESEADL DDFMQQLREH VHQGMRMLAS YHTLHRHIYL PDTAVTLIKC
     TMLGNLSPLL RASRKVFAKK NLLDPHNGWR TEQFRSFRSV PFASTHDACF DAEASEELTT
     ILRGVLKDID