ID   ORFZB_MAGO7             Reviewed;         424 AA.
AC   G4MVZ4;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Hydrolase ORFZ {ECO:0000303|PubMed:18433432};
DE            EC=3.7.1.- {ECO:0000305|PubMed:18433432};
DE   AltName: Full=ACE1 cytochalasan biosynthesis cluster protein ORFZ {ECO:0000303|PubMed:29142718};
GN   Name=ORFZ {ECO:0000303|PubMed:18433432}; ORFNames=MGG_08390;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
RN   [2]
RP   FUNCTION, INDUCTION, AND PATHWAY.
RX   PubMed=18433432; DOI=10.1111/j.1469-8137.2008.02459.x;
RA   Collemare J., Pianfetti M., Houlle A.E., Morin D., Camborde L., Gagey M.J.,
RA   Barbisan C., Fudal I., Lebrun M.H., Boehnert H.U.;
RT   "Magnaporthe grisea avirulence gene ACE1 belongs to an infection-specific
RT   gene cluster involved in secondary metabolism.";
RL   New Phytol. 179:196-208(2008).
RN   [3]
RP   FUNCTION.
RX   PubMed=29142718; DOI=10.1039/c4sc03707c;
RA   Song Z., Bakeer W., Marshall J.W., Yakasai A.A., Khalid R.M., Collemare J.,
RA   Skellam E., Tharreau D., Lebrun M.H., Lazarus C.M., Bailey A.M.,
RA   Simpson T.J., Cox R.J.;
RT   "Heterologous expression of the avirulence gene ACE1 from the fungal rice
RT   pathogen Magnaporthe oryzae.";
RL   Chem. Sci. 6:4837-4845(2015).
RN   [4]
RP   FUNCTION.
RX   PubMed=31644300; DOI=10.1021/acs.orglett.9b03372;
RA   Wang C., Becker K., Pfuetze S., Kuhnert E., Stadler M., Cox R.J.,
RA   Skellam E.;
RT   "Investigating the function of cryptic cytochalasan cytochrome P450
RT   monooxygenases using combinatorial biosynthesis.";
RL   Org. Lett. 21:8756-8760(2019).
CC   -!- FUNCTION: Hydrolyase; part of the gene cluster that mediates the
CC       biosynthesis of a tyrosine-derived cytochalasan acting as a fungal
CC       signal recognized by resistant rice plants and leads to avirulence in
CC       Pi33 resistant rice cultivars (PubMed:18433432). The first step in the
CC       pathway is catalyzed by the hybrid PKS-NRPS ACE1, assisted by the enoyl
CC       reductase RAP1, that are responsible for fusion of the tyrosine
CC       precursor and the polyketide backbone (PubMed:29142718). The polyketide
CC       synthase module (PKS) of ACE1 is responsible for the synthesis of the
CC       polyketide backbone and the downstream nonribosomal peptide synthetase
CC       (NRPS) amidates the carboxyl end of the polyketide with the tyrosine
CC       precursor (PubMed:29142718). Because ACE1 lacks a designated
CC       enoylreductase (ER) domain, the required activity is provided the enoyl
CC       reductase RAP1 (PubMed:29142718). Reduction by the hydrolyase ORFZ,
CC       followed by dehydration and intra-molecular Diels-Alder cyclization by
CC       the Diels-Alderase ORF3 then yield the required isoindolone-fused
CC       macrocycle (Probable). A number of oxidative steps catalyzed by the
CC       tailoring enymes identified within the cluster, including cytochrome
CC       P450 monooxygenases CYP1 to CYP4, the FAD-linked oxidoreductase OXR2
CC       and the short-chain dehydrogenase/reductase OXR1, are further required
CC       to afford the final cytochalasans that confer avirulence and which have
CC       still to be identified (Probable). The monooxygenase CYP1 has been
CC       shown to be a site-selective C-18 hydroxylase whereas the function of
CC       CYP3 is the site-selective epoxidation of the C-6/C-7 olefin that is
CC       present in some intermediate compounds (PubMed:31644300). Finally, SYN2
CC       and RAP2 are not required for avirulence in Pi33 resistant rice
CC       cultivars (PubMed:18433432). {ECO:0000269|PubMed:18433432,
CC       ECO:0000269|PubMed:29142718, ECO:0000269|PubMed:31644300,
CC       ECO:0000305|PubMed:18433432, ECO:0000305|PubMed:29142718}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:18433432}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q93NG6}.
CC   -!- INDUCTION: Expressed exclusively during fungal penetration of host
CC       leaves, the time point at which plant defense reactions are triggered.
CC       {ECO:0000269|PubMed:18433432}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. FUS2 hydrolase
CC       family. {ECO:0000305}.
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DR   EMBL; CM001232; EHA55862.1; -; Genomic_DNA.
DR   RefSeq; XP_003715669.1; XM_003715621.1.
DR   AlphaFoldDB; G4MVZ4; -.
DR   SMR; G4MVZ4; -.
DR   STRING; 318829.MGG_08390T0; -.
DR   ESTHER; mago7-ORFZB; Duf_1100-S.
DR   EnsemblFungi; MGG_08390T0; MGG_08390T0; MGG_08390.
DR   GeneID; 2678521; -.
DR   KEGG; mgr:MGG_08390; -.
DR   VEuPathDB; FungiDB:MGG_08390; -.
DR   eggNOG; ENOG502QPTG; Eukaryota.
DR   HOGENOM; CLU_034451_0_0_1; -.
DR   InParanoid; G4MVZ4; -.
DR   OMA; MQEMKRY; -.
DR   OrthoDB; 1133794at2759; -.
DR   Proteomes; UP000009058; Chromosome 2.
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   2: Evidence at transcript level;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..424
FT                   /note="Hydrolase ORFZ"
FT                   /id="PRO_0000449473"
FT   ACT_SITE        243
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q4WZB3"
SQ   SEQUENCE   424 AA;  46951 MW;  7C1FD0439BE3655E CRC64;
     MHHFFKGQFF DFETCRILGT AVYGGADVAE VLEAVGQIRD GDPVSWGRAW AIQAERALVL
     AEEACKSGDR TAARDAYLRG SNYTRASGYM LTGEGPNRPD PRSREIVERV QAIFRKAAAL
     FDHPVQFLKI PFEGGLKLPC TLYLPPPDRR LPGKIPILIS GGGADALQEE LYYMHPSAGP
     DLGYAVLTFE GPGQGVMLRK HDAKMRPDWE AVAGAVIDFL EELARSQPDL DLDTSRIAFS
     GCSLGGYFAL RAAADPRVKA CVSLDPLYSF WDFAMEHVSP TFINAWEAGW LKDGAVDAVV
     RMMMAMSFQM RWELSIAGTF FGQTSPARIM KEMKKFSLAG GQLRRVQCPV LVSGASHSLY
     LEGNHHTMRI YNELVNHTKG DKQLWLTATP GQGSLQAKMG ALRLANQKTF KFLDEHFGIE
     RPQL