ID   TWMA_TALWO              Reviewed;         348 AA.
AC   A0A2L0P0K1;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   25-APR-2018, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Thioesterase-like protein TwmA {ECO:0000303|PubMed:29343058};
DE            EC=3.1.2.- {ECO:0000305|PubMed:29343058};
DE   AltName: Full=Wortmanamides biosynthesis cluster protein A {ECO:0000303|PubMed:29343058};
GN   Name=TwmA {ECO:0000303|PubMed:29343058};
GN   Synonyms=TwnA {ECO:0000303|PubMed:29343058};
OS   Talaromyces wortmannii (Penicillium wortmannii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Islandici.
OX   NCBI_TaxID=28567;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC   STRAIN=ATCC 26942 / CBS 387.67 / CCM F-175 / VKM F-2091;
RX   PubMed=29343058; DOI=10.1021/jacs.7b13350;
RA   Hai Y., Tang Y.;
RT   "Biosynthesis of long-chain N-acyl amide by a truncated polyketide
RT   synthase-nonribosomal peptide synthetase hybrid megasynthase in fungi.";
RL   J. Am. Chem. Soc. 140:1271-1274(2018).
CC   -!- FUNCTION: Thioesterase-like protein; part of the gene cluster that
CC       mediates the biosynthesis of wortmanamides A and B, reduced long-chain
CC       polyketides amidated with a specific omega-amino acid, 5-aminopentanoic
CC       acid (5PA) (PubMed:29343058). The PKS modules of TwmB are involved in
CC       the synthesis of the polyketide backbone, whereas the non-canonical C
CC       domain of TwmB is a bonafide condensation domain that specifically
CC       selects 5PA and catalyzes amidation to release polyketide chain
CC       (PubMed:29343058). The C domain clearly prefers C16 and C18 fatty acyl
CC       substrates, which is consistent with simultaneous formation of both
CC       octaketide and nonaketide acyl amides wortmanamides A and B
CC       (PubMed:29343058). Because TwmB lacks a designated enoylreductase (ER)
CC       domain, the required activity is provided the enoyl reductase TwmE
CC       (PubMed:29343058). The roles of the remaining enzymes have still to be
CC       clarified (Probable). {ECO:0000269|PubMed:29343058,
CC       ECO:0000305|PubMed:29343058}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:29343058}.
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DR   EMBL; MG837518; AUY61969.1; -; Genomic_DNA.
DR   EMBL; MH399766; QBC19709.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2L0P0K1; -.
DR   SMR; A0A2L0P0K1; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.160.210; -; 2.
DR   InterPro; IPR042171; Acyl-CoA_hotdog.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   SUPFAM; SSF54637; SSF54637; 2.
PE   4: Predicted;
KW   Hydrolase.
FT   CHAIN           1..348
FT                   /note="Thioesterase-like protein TwmA"
FT                   /id="PRO_0000452487"
SQ   SEQUENCE   348 AA;  37955 MW;  934AE70677C43A01 CRC64;
     MASGKAGGAS ALFSEATQAE QLDSHTYRVN LNQGFCIGAV PNGGYTSACM LAAASKHLGP
     RGQPDTLTAH FEYPNRTSTG PAIVVIEDVK LGRQISTLHL TLWQGGLLSQ APWIDRSVSR
     RIVLAYTTHT NLRTFSGISM PTGYEVTPAA ELPSVSDFEA LKTHGADDAW AESKLPKGWA
     AMMLSLTQWR FYVPRKEPLS PGVLDMWIRL ASGEKITQGA LAYVVDSFPH NMHTFLAAPA
     LRELLNASPE RSGDSEVKDV RKKDQQRAEM WFPTVVMNIE AKTALPEEGV EWLSVRVSSK
     QIKEGKFDLE VLVRDTDGEM VALSNHVAMI LSVERNTGKK SGSSKASL