PHMC_PHANO
ID PHMC_PHANO Reviewed; 439 AA.
AC Q0V6Q5;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=FAD-linked oxidoreductase phmC {ECO:0000303|PubMed:31815421};
DE EC=1.-.-.- {ECO:0000305|PubMed:31815421};
DE AltName: Full=Phomacin biosynthesis cluster protein C {ECO:0000303|PubMed:31815421};
DE Flags: Precursor;
GN Name=phmC {ECO:0000303|PubMed:31815421}; ORFNames=SNOG_00309;
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: FAD-linked oxidoreductase; part of the gene cluster that
CC mediates 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:31815421}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; CH445325; EAT91804.2; -; Genomic_DNA.
DR RefSeq; XP_001790999.1; XM_001790947.1.
DR AlphaFoldDB; Q0V6Q5; -.
DR SMR; Q0V6Q5; -.
DR STRING; 321614.Q0V6Q5; -.
DR GeneID; 5967850; -.
DR KEGG; pno:SNOG_00309; -.
DR InParanoid; Q0V6Q5; -.
DR OrthoDB; 317492at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW Signal; Virulence.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..439
FT /note="FAD-linked oxidoreductase phmC"
FT /evidence="ECO:0000255"
FT /id="PRO_5004178710"
FT DOMAIN 89..272
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 439 AA; 46554 MW; A5B5C7D4C7658E9E CRC64;
MLSSILLTIF CAFLSSTGAA NVADWNSLNK TLKGQLKGAT PLASPCFSQV NAYEETQSED
CATAIGQQCL LDSSDPSSIK AYANVSCNQG SVPSYYIQVK SAEEVKKAFA FAARTQTAIS
IKNSGHDYNG RSSGAGSLSL WTRKLQELKY EPSFVPQQCG RQAGVAAITT GAGINFDQVY
TFAHEKGVTY LGGSGPTVGA SGGWVMTGGH GVLSRVYGLG VDRVLEFEVV TTDGVTRIAN
ACQNQDLFWA LRGGGGGTFG VILSTTTRVE PKLSIAVAFI ALPANTSQQV LAEWTSLAIN
STIKWAADGW GGFQGSGITL LGTPLLSLAQ AESSMAELAQ FAKRNGGSVA VELLSDFYDM
YTKYYITNVQ AGGSALFSHN WMIPSRAYAN AQGRKQLQDH MDWMSSVGLN PGFLATTPYV
YSGVAKQCGT FDAFGWMGL
