ID   THNE_TRIHA              Reviewed;         368 AA.
AC   A0A0F9XJT1;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2015, sequence version 1.
DT   03-AUG-2022, entry version 17.
DE   RecName: Full=Trans-enoyl reductase thnE {ECO:0000303|PubMed:33570538};
DE            EC=1.-.-.- {ECO:0000269|PubMed:33570538};
DE   AltName: Full=Trihazone biosynthesis cluster protein E {ECO:0000303|PubMed:33570538};
GN   Name=thnE {ECO:0000303|PubMed:33570538}; ORFNames=THAR02_03175;
OS   Trichoderma harzianum (Hypocrea lixii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=5544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6776;
RX   PubMed=26067977; DOI=10.1128/genomea.00647-15;
RA   Baroncelli R., Piaggeschi G., Fiorini L., Bertolini E., Zapparata A.,
RA   Pe M.E., Sarrocco S., Vannacci G.;
RT   "Draft whole-genome sequence of the biocontrol agent Trichoderma harzianum
RT   T6776.";
RL   Genome Announc. 3:E0064715-E0064715(2015).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=33570538; DOI=10.1039/d0ob02545c;
RA   Zhu Y., Wang J., Mou P., Yan Y., Chen M., Tang Y.;
RT   "Genome mining of cryptic tetronate natural products from a PKS-NRPS
RT   encoding gene cluster in Trichoderma harzianum t-22.";
RL   Org. Biomol. Chem. 19:1985-1990(2021).
CC   -!- FUNCTION: Trans-enoyl reductase; part of the gene cluster that produces
CC       the tetronate natural products trihazones (PubMed:33570538). The PKS-
CC       NRPS synthetase thnA with the help of the trans-enoyl reductase thnE
CC       are responsible for the synthesis of the carboxylmethyl containing
CC       trihazone A (PubMed:33570538). The PKS portion of thnA synthesizes
CC       beta-keto-triene chain from one acetyl-CoA and 6 equivalents of
CC       malonyl-CoA, in collaboration with thnE, which selectively reduces the
CC       enoyl intermediate during the first and fourth iteration of the PKS
CC       (PubMed:33570538). The NRPS domain selects and activates malate, of
CC       which the alpha-hydroxyl group attacks the completed polyketide acyl-S-
CC       ACP chain to form the ester product (PubMed:33570538). Intramolecular
CC       Dieckmann cyclization catalyzed by the terminal reductase domain
CC       releases the product as trihazone A from the PKS-NPRS
CC       (PubMed:33570538). The pathway begins with the formation of trihazone A
CC       by the hybrid PKS-NRPS synthetase thnA and the trans-enoyl reductase
CC       thnE. Trihazone A is further decarboxylated by the 2-oxoglutarate-
CC       dependent dioxygenase thnC to produce trihazone D. The function of the
CC       FAD-dependent monooxygenase thnD has still to be identified
CC       (PubMed:33570538). {ECO:0000269|PubMed:33570538}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:33570538}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9Y7D0}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; JOKZ01000069; KKP04695.1; -; Genomic_DNA.
DR   EnsemblFungi; KKP04695; KKP04695; THAR02_03175.
DR   OMA; KPDWILG; -.
DR   OrthoDB; 727365at2759; -.
DR   Proteomes; UP000034112; Unassembled WGS sequence.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   NADP; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..368
FT                   /note="Trans-enoyl reductase thnE"
FT                   /id="PRO_0000455680"
FT   BINDING         53..56
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         140..147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         179..182
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         202..205
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         220
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         267..268
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         289..293
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         358..359
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
SQ   SEQUENCE   368 AA;  38776 MW;  2B8DF8B7D34F10A4 CRC64;
     MSSATTMGQL PQHQTAIVAQ GPGQMTIQKD APVPALAHDM VLVKTATVAI NPVDVKSLDY
     SPAPGAIIGF DFAGTIVALG SDAVKEGRLA VGDRVAGVVY GMDRLQPDVG AFAQYVGALA
     DLVLKLPDHI SLEDAAALGL ATATAAYGLF KEMELPGALD RLSSSVPDRG DFVLVAGGST
     ATGTRAIELL KTAGFRPVAT SSPSNFELVK KFGAEAVFDY HDPGCADAIK AYTNNELDYA
     LDCIAEAETT QLCYAAIGRA GGRYVAVEPF RESIAQSRIN TVKASWFNVM TVWGRKVELG
     GEYAREASLE DREFGARSFA AVQALLDRGY VTTHPIKLMS GGWEGVVEGV AKIRSQPPSG
     YKLVCQVA