ID   ABA3_MAGOY              Reviewed;         518 AA.
AC   L7IKV1;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2013, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Alpha-ionylideneethane synthase abl3 {ECO:0000303|PubMed:28469630};
DE            EC=4.2.3.- {ECO:0000305|PubMed:28469630};
DE   AltName: Full=Abscisic acid biosynthesis protein 3 {ECO:0000303|PubMed:28469630};
DE   AltName: Full=Sesquiterpene synthase ABA3 {ECO:0000305};
GN   Name=ABA3 {ECO:0000303|PubMed:28469630};
GN   ORFNames=OOU_Y34scaffold00166g3 {ECO:0000312|EMBL:ELQ43177.1};
OS   Magnaporthe oryzae (strain Y34) (Rice blast fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=1143189;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y34;
RX   PubMed=22876203; DOI=10.1371/journal.pgen.1002869;
RA   Xue M., Yang J., Li Z., Hu S., Yao N., Dean R.A., Zhao W., Shen M.,
RA   Zhang H., Li C., Liu L., Cao L., Xu X., Xing Y., Hsiang T., Zhang Z.,
RA   Xu J.-R., Peng Y.-L.;
RT   "Comparative analysis of the genomes of two field isolates of the rice
RT   blast fungus Magnaporthe oryzae.";
RL   PLoS Genet. 8:E1002869-E1002869(2012).
RN   [2]
RP   FUNCTION.
RX   PubMed=26648962; DOI=10.3389/fpls.2015.01082;
RA   Spence C.A., Lakshmanan V., Donofrio N., Bais H.P.;
RT   "Crucial roles of abscisic acid biogenesis in virulence of rice blast
RT   fungus Magnaporthe oryzae.";
RL   Front. Plant Sci. 6:1082-1082(2015).
RN   [3]
RP   IDENTIFICATION, FUNCTION, AND PATHWAY.
RX   PubMed=28469630; DOI=10.3389/fpls.2017.00587;
RA   Lievens L., Pollier J., Goossens A., Beyaert R., Staal J.;
RT   "Abscisic acid as pathogen effector and immune regulator.";
RL   Front. Plant Sci. 8:587-587(2017).
CC   -!- FUNCTION: Alpha-ionylideneethane synthase involved in the biosynthesis
CC       of abscisic acid (ABA), a phytohormone that acts antagonistically
CC       toward salicylic acid (SA), jasmonic acid (JA) and ethylene (ETH)
CC       signaling, to impede plant defense responses (PubMed:26648962). During
CC       pathogen-host interaction, ABA plays a dual role in disease severity by
CC       increasing plant susceptibility and accelerating pathogenesis in the
CC       fungus itself (PubMed:26648962). The first step of the pathway
CC       catalyzes the reaction from farnesyl diphosphate to alpha-
CC       ionylideneethane performed by the alpha-ionylideneethane synthase ABA3
CC       via a three-step reaction mechanism involving 2 neutral intermediates,
CC       beta-farnesene and allofarnesene (By similarity). The cytochrome P450
CC       monooxygenase ABA1 might then be involved in the conversion of alpha-
CC       ionylideneethane to alpha-ionylideneacetic acid (By similarity). Alpha-
CC       ionylideneacetic acid is further converted to abscisic acid in 2 steps
CC       involving the cytochrome P450 monooxygenase ABA2 and the short-chain
CC       dehydrogenase/reductase ABA4, via the intermediates 1'-deoxy-ABA or
CC       1',4'-trans-diol-ABA, depending on the order of action of these 2
CC       enzymes (By similarity). ABA2 is responsible for the hydroxylation of
CC       carbon atom C-1' and ABA4 might be involved in the oxidation of the C-
CC       4' carbon atom (By similarity). {ECO:0000250|UniProtKB:Q14RS2,
CC       ECO:0000269|PubMed:26648962}.
CC   -!- PATHWAY: Hormone biosynthesis. {ECO:0000305|PubMed:28469630}.
CC   -!- SIMILARITY: Belongs to the alpha-ionylideneethane synthase family.
CC       {ECO:0000305}.
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DR   EMBL; JH793224; ELQ43177.1; -; Genomic_DNA.
DR   AlphaFoldDB; L7IKV1; -.
DR   Proteomes; UP000011086; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Lyase; Virulence.
FT   CHAIN           1..518
FT                   /note="Alpha-ionylideneethane synthase abl3"
FT                   /id="PRO_0000448434"
FT   REGION          294..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..340
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   518 AA;  57776 MW;  33FA595359C34C87 CRC64;
     MPPRFNDSWY YPDDIAHDLD GVEGLSEALK QEAYACAWEY TRCVIPQYTN WDRYVAFMRT
     IIIGIIAEFR GELVDVAASD SIMGCYSLSA VLDALFEGTP GRELMVREYK TFLLVTSEKT
     SKRRDSELFR RYVNGLAASP RSWFRMRDCD ALARFSLAAA LACNDMYDVF PTDEQFELLT
     EIGDTLYDAV AFYKHRSEGE TNNTFAYVPA DMRIQAFRVA REMLWALDVA YAHKPEGAIL
     VNFIRFFGGP IHMMMRRYRF VEEDLTVGKP ETAAVVAETR RNFKLWNRVD AQVAAPGQTS
     SDNSSDNRSS SISSTSSTGT DGSGAGDASS VHSSGVHSDA TSIEPEKEDQ SSVFEAPGAD
     RFRSLLARSK ELMFPELRAY LSRSGEPHCN RCLYRSSYGA QQIHRFGGVE LCRGCRAMWR
     GYVESLPERV QEAFPDVVLK APPPPSPRRA VPADGEADSA AGQRSKRLRE DLTAAGEYTT
     VAETVPAEDV PRSAPDIMED VLQAECAIDD MRSAVAVF