PHME_PHANO
ID PHME_PHANO Reviewed; 349 AA.
AC Q0V6Q3;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Trans-enoyl reductase phmE {ECO:0000303|PubMed:31815421};
DE EC=1.-.-.- {ECO:0000305|PubMed:31815421};
DE AltName: Full=Phomacin biosynthesis cluster protein E {ECO:0000303|PubMed:31815421};
GN Name=phmE {ECO:0000303|PubMed:31815421}; ORFNames=SNOG_00311;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
RN [2]
RP FUNCTION, AND PATHWAY.
RX PubMed=31815421; DOI=10.1021/acschembio.9b00791;
RA Li H., Wei H., Hu J., Lacey E., Sobolev A.N., Stubbs K.A., Solomon P.S.,
RA Chooi Y.H.;
RT "Genomics-driven discovery of phytotoxic cytochalasans involved in the
RT virulence of the wheat pathogen Parastagonospora nodorum.";
RL ACS Chem. Biol. 15:226-233(2020).
CC -!- FUNCTION: Trans-enoyl reductase; part of the gene cluster that mediates
CC the biosynthesis of the mycotoxins phomacins, leucine-derived
CC cytochalasans with potent actin polymerization-inhibitory activities
CC and monocot-specific antigerminative activities (PubMed:31815421). The
CC first step in the pathway is catalyzed by the hybrid PKS-NRPS phmA,
CC assisted by the enoyl reductase phmE, that are responsible for fusion
CC of the leucine precursor and the polyketide backbone to produce a 2-
CC pyrrolidone intermediate (PubMed:31815421). The polyketide synthase
CC module (PKS) of phmA is responsible for the synthesis of the polyketide
CC backbone and the downstream nonribosomal peptide synthetase (NRPS)
CC amidates the carboxyl end of the polyketide with the leucine precursor
CC (PubMed:31815421). Because phmA lacks a designated enoylreductase (ER)
CC domain, the required activity is provided the enoyl reductase phmE
CC (PubMed:31815421). Reduction by the hydrolyase phmG, followed by
CC dehydration and intra-molecular Diels-Alder cyclization by the Diels-
CC Alderase phmD then yield the required isoindolone-fused macrocycle
CC (Probable). A number of oxidative steps catalyzed by the tailoring
CC cytochrome P450 monooxygenase phmB, the FAD-linked oxidoreductase phmC
CC and the short-chain dehydrogenase/reductase phmF, are further required
CC to afford the final products, phomacin D and phomacin E
CC (PubMed:31815421). {ECO:0000269|PubMed:31815421,
CC ECO:0000305|PubMed:31815421}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:31815421}.
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; CH445325; EAT91806.2; -; Genomic_DNA.
DR RefSeq; XP_001791001.1; XM_001790949.1.
DR AlphaFoldDB; Q0V6Q3; -.
DR SMR; Q0V6Q3; -.
DR GeneID; 5967965; -.
DR KEGG; pno:SNOG_00311; -.
DR InParanoid; Q0V6Q3; -.
DR OrthoDB; 727365at2759; -.
DR Proteomes; UP000001055; 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; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW NADP; Nucleotide-binding; Oxidoreductase; Reference proteome; Virulence.
FT CHAIN 1..349
FT /note="Trans-enoyl reductase phmE"
FT /id="PRO_0000449431"
FT BINDING 55..58
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 143..150
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 182..185
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 200
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 247..248
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 267..271
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 336..337
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
SQ SEQUENCE 349 AA; 37623 MW; AA3F4D034049449F CRC64;
MSRVRYNNSV ALPATQTVIK QNEDGLLTIQ KDFPLPEIRS DRLLVRVEYV AINPCDWKMS
ERFPAPGAVD GCDFAGTVVA LGSDVSKTGR FQVGEKVCGG VHGSNPIDPT TGSFAEYLSA
DAEFTFKVPG YMGLKEAAAV GGTGIGTMGL ALSKSLGLPG SPTRPVGETD SKYVLVPIAV
CSPKNYDLVK SYGAVKAFDY HSPTCAQDIR AYTKNRLAHI IDPIVEAKTM QLCYAAMGRA
GGKYCALEAY ADELCTRKVV KPELVMGMAI LGRKVALNHG YGSEADAGKR AFGIEWYREM
QDLLDAGRLM THPVRVVPGR FDGIMKGLQM LKTKQVSGEK LIVQLGSNN
