RAP1_MAGO7
ID RAP1_MAGO7 Reviewed; 359 AA.
AC G4MVZ3;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Trans-enoyl reductase RAP1 {ECO:0000303|PubMed:18433432};
DE EC=1.-.-.- {ECO:0000269|PubMed:29142718};
DE AltName: Full=ACE1 cytochalasan biosynthesis cluster protein RAP1 {ECO:0000303|PubMed:29142718};
GN Name=RAP1 {ECO:0000303|PubMed:18433432}; ORFNames=MGG_08391;
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, CATALYTIC ACTIVITY, AND PATHWAY.
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: Trans-enoyl reductase; part of the gene cluster that mediates
CC the 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, PubMed:29142718). The
CC first step in the pathway is catalyzed by the hybrid PKS-NRPS ACE1,
CC assisted by the enoyl reductase RAP1, that are responsible for fusion
CC of the tyrosine precursor and the polyketide backbone
CC (PubMed:29142718). The polyketide synthase module (PKS) of ACE1 is
CC responsible for the synthesis of the polyketide backbone and the
CC downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl
CC end of the polyketide with the tyrosine precursor (PubMed:29142718).
CC Because ACE1 lacks a designated enoylreductase (ER) domain, the
CC required activity is provided the enoyl reductase RAP1
CC (PubMed:29142718). Reduction by the hydrolyase ORFZ, followed by
CC dehydration and intra-molecular Diels-Alder cyclization by the Diels-
CC Alderase ORF3 then yield the required isoindolone-fused macrocycle
CC (Probable). A number of oxidative steps catalyzed by the tailoring
CC enymes identified within the cluster, including cytochrome P450
CC monooxygenases CYP1 to CYP4, the FAD-linked oxidoreductase OXR2 and the
CC short-chain dehydrogenase/reductase OXR1, are further required to
CC 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:0000269|PubMed:29142718}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9Y7D0}.
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 zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; CM001232; EHA55861.1; -; Genomic_DNA.
DR RefSeq; XP_003715668.1; XM_003715620.1.
DR AlphaFoldDB; G4MVZ3; -.
DR SMR; G4MVZ3; -.
DR STRING; 318829.MGG_08391T0; -.
DR EnsemblFungi; MGG_08391T0; MGG_08391T0; MGG_08391.
DR GeneID; 2678520; -.
DR KEGG; mgr:MGG_08391; -.
DR VEuPathDB; FungiDB:MGG_08391; -.
DR eggNOG; KOG1198; Eukaryota.
DR HOGENOM; CLU_026673_16_1_1; -.
DR InParanoid; G4MVZ3; -.
DR OMA; CAQDIRA; -.
DR OrthoDB; 727365at2759; -.
DR Proteomes; UP000009058; Chromosome 2.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW NADP; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..359
FT /note="Trans-enoyl reductase RAP1"
FT /id="PRO_0000449429"
FT BINDING 49..52
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 137..144
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 195..198
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 213
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 260..261
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 281..285
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 350..351
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
SQ SEQUENCE 359 AA; 39260 MW; 795B00B5A564966F CRC64;
MAPFIPSSHT AIIQHDDAGG VKITPGLPLP VLEPGQVLVK TAAVALNPCD FKMPQRFSQA
GTYNGCDYAG TVVQLTEEVE KNGLLKVGDR IFAACVGNNP HDKDSGSFAE YLKGTAKFCW
KIPDWMSFEE AAGLSGTCIA TACMSLFQSL KLPGTFEEPA TKPLDVLIWG GASSVGTTMI
QMVKLLGHRA ITTCSPKNFE LVKSYGADAV FDYRSPTCAA DIKKLTRNSL KYVVDPFSDL
RTMALADEAM GRSGGKYVAL ESYQDTHDKK SKLIERELIM GQMILGRAIK LPGDYGKPEN
PEMGRWGVEC YKSVQRLVDD RKLRPHPLRI LDGGLEAILD GLEMLKRREV AAEKIVVRL
