ID   TWME_TALWO              Reviewed;         368 AA.
AC   A0A2L0P0L5;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   25-APR-2018, sequence version 1.
DT   03-AUG-2022, entry version 11.
DE   RecName: Full=Trans-enoyl reductase TwmE {ECO:0000303|PubMed:29343058};
DE            EC=1.-.-.- {ECO:0000269|PubMed:29343058};
DE   AltName: Full=Wortmanamides biosynthesis cluster protein E {ECO:0000303|PubMed:29343058};
GN   Name=TwmE {ECO:0000303|PubMed:29343058};
GN   Synonyms=TwnE {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, CATALYTIC ACTIVITY, AND
RP   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: Trans-enoyl reductase; part of the gene cluster that mediates
CC       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:0000269|PubMed:29343058}.
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; MG837522; AUY61973.1; -; Genomic_DNA.
DR   EMBL; MH399766; QBC19713.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2L0P0L5; -.
DR   SMR; A0A2L0P0L5; -.
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.
FT   CHAIN           1..368
FT                   /note="Trans-enoyl reductase TwmE"
FT                   /id="PRO_0000452491"
FT   BINDING         49..52
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         135..142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         204..207
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         222
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         269..270
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         290..294
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         360..361
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
SQ   SEQUENCE   368 AA;  39204 MW;  DDCAB17FC18CCC5A CRC64;
     MTPTTLPTSQ RAVQQDGNGK LHVANNAAIP SLLPGHVLVK TYAVALNPSD YKIQKNFPIP
     GAYVGIDFSG TVVQVANDVD SINPGTEVFG AAFTFSSAHR LANGAFAEYV RVRADLLFRI
     PSEQQCQNDG DLTLFKAATL GTAMSTCLLS LWSPDALGLV GKPEEPVLSE KPIPVLVYGG
     STSVGTIAIQ LLKLSGYDPI ATCSPRSFDL VRSRGASNVF DYSSADVALK IKTHTGGRLK
     YALDCISDVA SVATCYAAIQ RPGGRYVSLE YIPDELLAQR RAVRPNFVLS AELYGEEIVL
     GEEAYDRPAN REKHQLAVQN VGMLQRLIDS GGLKTHPTEE IEGGLEGVVK GLVALAGGGH
     PRKLVAVV