ID   PVHC_TALVA              Reviewed;         358 AA.
AC   A0A3Q9U4Z5;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   10-APR-2019, sequence version 1.
DT   03-AUG-2022, entry version 9.
DE   RecName: Full=Trans-enoyl reductase pvhC {ECO:0000303|PubMed:30609896};
DE            Short=ER pvhC {ECO:0000303|PubMed:30609896};
DE            EC=1.-.-.- {ECO:0000269|PubMed:30609896};
DE   AltName: Full=Varicidin biosynthesis cluster protein C {ECO:0000303|PubMed:30609896};
GN   Name=pvhC {ECO:0000303|PubMed:30609896};
OS   Talaromyces variabilis (Penicillium variabile).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces.
OX   NCBI_TaxID=28576;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RC   STRAIN=HXQ-H-1;
RX   PubMed=30609896; DOI=10.1021/jacs.8b12010;
RA   Tan D., Jamieson C.S., Ohashi M., Tang M.C., Houk K.N., Tang Y.;
RT   "Genome-mined Diels-Alderase catalyzes formation of the cis-
RT   octahydrodecalins of varicidin A and B.";
RL   J. Am. Chem. Soc. 141:769-773(2019).
CC   -!- FUNCTION: Trans-enoyl reductase; part of the gene cluster that mediates
CC       the biosynthesis of varicidin A, an antifungal natural product
CC       containing a cis-octahydrodecalin core (PubMed:30609896). The PKS
CC       module of pvhA together with the enoylreductase pvhC catalyze the
CC       formation of the polyketide unit which is then conjugated to L-
CC       isoleucine by the condensation domain of the NRPS module
CC       (PubMed:30609896). Activity of the Dieckmann cyclase domain (RED) of
CC       pvhA results in release of an acyclic tetramate (PubMed:30609896). The
CC       cytochrome P450 monooxygenase pvhE then catalyzes the oxidation of the
CC       C21 methyl group to a to carboxylate group (PubMed:30609896). The
CC       methyltransferase pvhD then further methylates the pvhE product
CC       (PubMed:30609896). The Diels-Alderase pvhB is able to catalyzes Diels-
CC       Alder cycloaddition using both pvhE and pvhD products as substrates to
CC       form the decalin ring, yielding varicidin B and A, respectively
CC       (PubMed:30609896). {ECO:0000269|PubMed:30609896}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:30609896}.
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; MK376933; AZZ09612.1; -; Genomic_DNA.
DR   SMR; A0A3Q9U4Z5; -.
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; IPR013154; ADH_N.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   Pfam; PF08240; ADH_N; 1.
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..358
FT                   /note="Trans-enoyl reductase pvhC"
FT                   /id="PRO_0000453337"
FT   BINDING         48..51
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         134..141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         169..172
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         192..195
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         210
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         257..258
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         278..282
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         347..348
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
SQ   SEQUENCE   358 AA;  38438 MW;  915F332F1B336453 CRC64;
     MPSRTQNIQS AWIGTTDGGS RLAHDAPIPA IARERVLIKT KAVSVSPVDS KLVGPYVTPN
     AVAGFDFSGI VEELGPEATK CGLKVGDRVC SAVVGMNPAD PTIGAFAEYT AAVEWILLKL
     PPSITFEQGA TLGISFLTSG LALFRSLGIP GRPLEPAPKP LCILVYGGSS SCGTASLQLL
     REAGHIPITT CSPHNFELVK SYGAVDAFDY NDPDTMDKIK KYTKNGLRYA LDCISTTSSM
     QFCYKVIGRA GGKYTSLEPF SAAVAQTRKV VSPDWVMGPS LLGQEVAWPE PHYRKQDDDL
     AQFGAEWTAT LNQLLKKELI KPHPMQIRDG GLENIQQGLE DLRAKKVSGA KIVYPLGS