PHMF_PHANO
ID PHMF_PHANO Reviewed; 338 AA.
AC Q0V6Q2;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Short-chain dehydrogenase/reductase phmF {ECO:0000303|PubMed:31815421};
DE EC=1.1.1.- {ECO:0000305|PubMed:31815421};
DE AltName: Full=Phomacin biosynthesis cluster protein F {ECO:0000303|PubMed:31815421};
GN Name=phmFA {ECO:0000303|PubMed:31815421}; ORFNames=SNOG_00312;
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: Short-chain dehydrogenase/reductase; part of the gene cluster
CC that mediates the biosynthesis of the mycotoxins phomacins, leucine-
CC derived cytochalasans with potent actin polymerization-inhibitory
CC activities and monocot-specific antigerminative activities
CC (PubMed:31815421). The first step in the pathway is catalyzed by the
CC hybrid PKS-NRPS phmA, assisted by the enoyl reductase phmE, that are
CC responsible for fusion of the leucine precursor and the polyketide
CC backbone to produce a 2-pyrrolidone intermediate (PubMed:31815421). The
CC polyketide synthase module (PKS) of phmA is responsible for the
CC synthesis of the polyketide backbone and the downstream nonribosomal
CC peptide synthetase (NRPS) amidates the carboxyl end of the polyketide
CC with the leucine precursor (PubMed:31815421). Because phmA lacks a
CC designated enoylreductase (ER) domain, the required activity is
CC provided the enoyl reductase phmE (PubMed:31815421). Reduction by the
CC hydrolyase phmG, followed by dehydration and intra-molecular Diels-
CC Alder cyclization by the Diels-Alderase phmD then yield the required
CC isoindolone-fused macrocycle (Probable). A number of oxidative steps
CC catalyzed by the tailoring cytochrome P450 monooxygenase phmB, the FAD-
CC linked oxidoreductase phmC and the short-chain dehydrogenase/reductase
CC phmF, are further required to afford the final products, phomacin D and
CC phomacin E (PubMed:31815421). {ECO:0000269|PubMed:31815421,
CC ECO:0000305|PubMed:31815421}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:31815421}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; CH445325; EAT91807.1; -; Genomic_DNA.
DR RefSeq; XP_001791002.1; XM_001790950.1.
DR AlphaFoldDB; Q0V6Q2; -.
DR SMR; Q0V6Q2; -.
DR STRING; 13684.SNOT_00312; -.
DR EnsemblFungi; SNOT_00312; SNOT_00312; SNOG_00312.
DR GeneID; 5968079; -.
DR KEGG; pno:SNOG_00312; -.
DR eggNOG; KOG1208; Eukaryota.
DR HOGENOM; CLU_010194_44_4_1; -.
DR InParanoid; Q0V6Q2; -.
DR OMA; LCKTDLG; -.
DR OrthoDB; 1076292at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW NAD; NADP; Oxidoreductase; Reference proteome; Virulence.
FT CHAIN 1..338
FT /note="Short-chain dehydrogenase/reductase phmF"
FT /id="PRO_0000449453"
FT ACT_SITE 211
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 38..46
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 65..66
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 95..97
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 238..240
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
SQ SEQUENCE 338 AA; 36227 MW; 315E6689FCED53D7 CRC64;
MAEAFTTVPA KSSPARFRYT KANPVKDPTT SFAGKTILIT GPNAGLGFEA ATKFARLGAS
KLIFGVRSLE RGQEAKTKIE QLTKCKRDAI QLVQLDMGSY ASIEKFAKSV TDEFPVIHAA
VLNAGVAPPS YKLSQEGWEM SLQVNVISTA YLAILLLPKL RESGRAIGEP AYLEFVSSTG
HGDVTTESVR DGKSILKKVN DPANFKFTAQ YQITKLLEIW AMEHIAAKTS PKEVIVNSAC
PGLCKSSIGR DFGIVLRGLD AVFKGIFAQT AEAGSRILVS AVTAGTDSHG GFWALDAVSV
PGELVTSDEG KALSKQFWAE VLDVLRKQNA DVEAILNG
