ID   ABA2_MAGO7              Reviewed;         521 AA.
AC   G4N2X2;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Cytochrome P450 monooxygenase ABA2 {ECO:0000303|PubMed:26648962};
DE            EC=1.-.-.- {ECO:0000305|PubMed:26648962};
DE   AltName: Full=Abscisic acid biosynthesis protein 2 {ECO:0000303|PubMed:26648962};
GN   Name=ABA2 {ECO:0000303|PubMed:26648962}; ORFNames=MGG_07982;
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   IDENTIFICATION, INDUCTION, FUNCTION, AND PATHWAY.
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   FUNCTION.
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: Cytochrome P450 monooxygenase involved in the biosynthesis of
CC       abscisic acid (ABA), a phytohormone that acts antagonistically toward
CC       salicylic acid (SA), jasmonic acid (JA) and ethylene (ETH) signaling,
CC       to impede plant defense responses (PubMed:26648962). During pathogen-
CC       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:Q5K0D9,
CC       ECO:0000269|PubMed:26648962}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Hormone biosynthesis. {ECO:0000269|PubMed:26648962}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is induced in spores.
CC       {ECO:0000269|PubMed:26648962}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM001233; EHA53421.1; -; Genomic_DNA.
DR   RefSeq; XP_003713228.1; XM_003713180.1.
DR   AlphaFoldDB; G4N2X2; -.
DR   SMR; G4N2X2; -.
DR   STRING; 318829.MGG_07982T0; -.
DR   EnsemblFungi; MGG_07982T0; MGG_07982T0; MGG_07982.
DR   GeneID; 2683909; -.
DR   KEGG; mgr:MGG_07982; -.
DR   VEuPathDB; FungiDB:MGG_07982; -.
DR   eggNOG; KOG0157; Eukaryota.
DR   HOGENOM; CLU_001570_14_11_1; -.
DR   InParanoid; G4N2X2; -.
DR   OMA; TYTTFDI; -.
DR   OrthoDB; 1247045at2759; -.
DR   Proteomes; UP000009058; Chromosome 3.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0009688; P:abscisic acid biosynthetic process; ISS:GO_Central.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW   Virulence.
FT   CHAIN           1..521
FT                   /note="Cytochrome P450 monooxygenase ABA2"
FT                   /id="PRO_0000448417"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         458
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P04798"
FT   CARBOHYD        366
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   521 AA;  58440 MW;  A11E5D80B3E4779D CRC64;
     MYGTNLLETM GKPTAGHLGM AVTFTILVAF TIHVLRMRFF HPLRRYPGPW LNSITQIPAA
     WALLRARQPK AYRELHEKYG PIVRVAPNEL SFINVEAWDD IYGFLKSTPN FEKSPVFIGA
     VSPLNGQTGI SLANNEEHTR QRRALAAPFT NRALLQQQDI LRVHVDKLIT ALRAKARNKE
     SVNMGEWYTY TTFDIIGDIC FAEPFGCLDG GESNEWARAI INIFKAATWD QAIRRVAGTG
     TLLHKALVKI IIPAEAAQWR TIHFSNSKAK TLARLADPDR QHPDLIKHIL DSEDSRAALS
     PTEIILNMVL FISAGSETTA NTMTGWTYFM LRHPEARARA TAEVRAAFAS PRDIKWETVR
     ALPYLNATLE EALRLFSPAP SNQPRVVPAC GAVVAGCPLP SGTTVSVAPW AAVFSARNFA
     DPERFAPERW LDEGGADPRY AADRRGASQP FSTGPRGCMG KNLAYFELRL VLAHLLWHFD
     LEPTDSAAGR ECMRRWEQTD MDTYQTWMKP DLWVDLKEAQ R