ID   PHMG_PHANO              Reviewed;         442 AA.
AC   Q0V6Q1;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Hydrolase phmG {ECO:0000303|PubMed:31815421};
DE            EC=3.7.1.- {ECO:0000305|PubMed:31815421};
DE   AltName: Full=Phomacin biosynthesis cluster protein G {ECO:0000303|PubMed:31815421};
GN   Name=phmG {ECO:0000303|PubMed:31815421}; ORFNames=SNOG_00313;
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: Hydrolyase; 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   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q93NG6}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. FUS2 hydrolase
CC       family. {ECO:0000305}.
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DR   EMBL; CH445325; EAT91808.1; -; Genomic_DNA.
DR   RefSeq; XP_001791003.1; XM_001790951.1.
DR   AlphaFoldDB; Q0V6Q1; -.
DR   SMR; Q0V6Q1; -.
DR   ESTHER; phano-phmG; Duf_1100-S.
DR   GeneID; 5968092; -.
DR   KEGG; pno:SNOG_00313; -.
DR   InParanoid; Q0V6Q1; -.
DR   OMA; MQEMKRY; -.
DR   OrthoDB; 1133794at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   Pfam; PF12697; Abhydrolase_6; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome; Virulence.
FT   CHAIN           1..442
FT                   /note="Hydrolase phmG"
FT                   /id="PRO_0000449474"
FT   ACT_SITE        259
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q4WZB3"
SQ   SEQUENCE   442 AA;  49353 MW;  B265CB2EC2D1C29C CRC64;
     MTNSSPPFST IHQFFPGNTF LNFESVRILS TAPYGGCDAA EFLTAIAAIN PKDPQTWADA
     WSHMAHLAET MAEEALSRGD VVAARDGFLR ASSYTRASGY LYINGPTLDE HHPLAFEISK
     KVQSLFRRAL PFLDCDVHVV EIPYVVDSPE RKEVMLPGYL YLPNAQHRLP DGKIPVLLNT
     GGADSVQEEL YYIHPQGGHT RGYAVLTFEG PGQGIVLREH GLHMRPDWEV TGWKGYSSTL
     KREVGVELDL DRIAVAGASM GGYYALRAAK DSRIKACVAI DPFYDMWDFG TKHISGLFMS
     AWTGGWIGDD WVDRIIRLGM RTNFQLRWEV GVTAAFWGIA SPAKILKEMS KYSLKGGYLE
     KVQCPVLVTG AGKSLYFDTE EHTMKVFDDL GHLEERWRRV WMPNRPEEGG LQAKIGAFGL
     ANMKAYGFLD EVFGIRRVTV ES