ID   ABA2_MAGOY              Reviewed;         418 AA.
AC   L7HT17;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2013, sequence version 1.
DT   03-AUG-2022, entry version 26.
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=OOU_Y34scaffold00799g15;
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   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   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; JH793116; ELQ34093.1; -; Genomic_DNA.
DR   AlphaFoldDB; L7HT17; -.
DR   SMR; L7HT17; -.
DR   Proteomes; UP000011086; Unassembled WGS sequence.
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   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase; Virulence.
FT   CHAIN           1..418
FT                   /note="Cytochrome P450 monooxygenase ABA2"
FT                   /id="PRO_0000448418"
FT   BINDING         355
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"
SQ   SEQUENCE   418 AA;  46664 MW;  A14AA627A392B085 CRC64;
     MYGTNLLETM GKPTAGHLGM AVTFTPKAYR ELHEKYAAPF TNRALLQQQD ILRVHVDKLI
     TALRAKARNK ESVNMGEWSP HTQPDTYTTF DIIGDICFAE PFGCLDGGES NEWARAIINI
     FKAATWDQAI RRVAGTGTLL HKALVKIIIP AEAAQWRTIH FSNSKAKTLA RLADPDRQHP
     DLIKHILDSE DSRAALSPTE IILNMVLFIS AGSETTANTM TGWTYFMLRH PEARARATAE
     VRAAFASPRD IKWETVRALP YLNATLEEAL RLFSPAPSNQ PRVVPACGAV VAGCPLPSGT
     TVSVAPWAAV FSARNFADPE RFAPERWLDE GGADPRYAAD RRGASQPFST GPRGCMGKNL
     AYFELRLVLA HLLWHFDLEP TDSAAGRECM RRWEQTDMDT YQTWMKPDLW VDLKEAQR