PHMD_PHANO
ID PHMD_PHANO Reviewed; 358 AA.
AC Q0V6Q4;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Diels-Alderase phmD {ECO:0000303|PubMed:31815421};
DE EC=5.5.1.- {ECO:0000305|PubMed:31815421};
DE AltName: Full=Phomacin biosynthesis cluster protein D {ECO:0000303|PubMed:31815421};
GN Name=phmD {ECO:0000303|PubMed:31815421}; ORFNames=SNOG_00310;
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: Diels-Alderase; part of the gene cluster that mediates the
CC biosynthesis of the mycotoxins phomacins, leucine-derived cytochalasans
CC with potent actin polymerization-inhibitory activities and monocot-
CC specific antigerminative activities (PubMed:31815421). The first step
CC in the pathway is catalyzed by the hybrid PKS-NRPS phmA, assisted by
CC the enoyl reductase phmE, that are responsible for fusion of the
CC 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:0000305|PubMed:31815421}.
CC -!- SIMILARITY: Belongs to the Diels-Alderase family. {ECO:0000305}.
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DR EMBL; CH445325; EAT91805.1; -; Genomic_DNA.
DR RefSeq; XP_001791000.1; XM_001790948.1.
DR AlphaFoldDB; Q0V6Q4; -.
DR SMR; Q0V6Q4; -.
DR GeneID; 5968076; -.
DR KEGG; pno:SNOG_00310; -.
DR InParanoid; Q0V6Q4; -.
DR OMA; GGHERFW; -.
DR OrthoDB; 1068172at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Isomerase; Reference proteome; Virulence.
FT CHAIN 1..358
FT /note="Diels-Alderase phmD"
FT /id="PRO_0000449456"
SQ SEQUENCE 358 AA; 40147 MW; F3B00545CF7EB4F3 CRC64;
MSKSKDPIFF STGGLDNFIS PKMRPLNGTA GEQWEFDGVS DDAKLAFVFG FYRDPNYAIL
GSGNLRVSVE MAWPNGSRFA QVDYPTDNII EECDWGTRGI WRSNDFNYTF EITADMKRAR
VGMHTPQVTG IVSMTSTSQP RYPDGRTYPS ENSTSEALPY FHFVEPIPVA RAHVDMTILG
EKFAWDGLGG MERLWGAFSW FTCLQGMNVI RILAGPYSLS MLSFTSNIKK GREYPSIALF
DNGEPVFSSQ NTEESDVNDY FSFTKTYDGK VTGTLRDKVT GYELELVSPG RQLHWTFLID
HANLAFEYIL GRGTGGSGFS AWVNGGRMGR EQFKGIALTE ALTFPKKSPL FRPQYSED