ID   ABA4_MAGOY              Reviewed;         269 AA.
AC   L7I518;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2013, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=Short-chain dehydrogenase/reductase ABA4 {ECO:0000303|PubMed:26648962};
DE            EC=1.1.1.- {ECO:0000305|PubMed:26648962};
DE   AltName: Full=Abscisic acid biosynthesis protein 4 {ECO:0000303|PubMed:26648962};
GN   Name=ABA4; ORFNames=OOU_Y34scaffold00552g20;
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, DISRUPTION PHENOTYPE, 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: Short-chain dehydrogenase/reductase involved in the
CC       biosynthesis of abscisic acid (ABA), a phytohormone that acts
CC       antagonistically toward salicylic acid (SA), jasmonic acid (JA) and
CC       ethylene (ETH) signaling, to impede plant defense responses
CC       (PubMed:26648962). During pathogen-host interaction, ABA plays a dual
CC       role in disease severity by increasing plant susceptibility and
CC       accelerating pathogenesis in the fungus itself (PubMed:26648962). The
CC       first step of the pathway catalyzes the reaction from farnesyl
CC       diphosphate to alpha-ionylideneethane performed by the alpha-
CC       ionylideneethane synthase ABA3 via a three-step reaction mechanism
CC       involving 2 neutral intermediates, beta-farnesene and allofarnesene (By
CC       similarity). The cytochrome P450 monooxygenase ABA1 might then be
CC       involved in the conversion of alpha-ionylideneethane to alpha-
CC       ionylideneacetic acid (By similarity). Alpha-ionylideneacetic acid is
CC       further converted to abscisic acid in 2 steps involving the cytochrome
CC       P450 monooxygenase ABA2 and the short-chain dehydrogenase/reductase
CC       ABA4, via the intermediates 1'-deoxy-ABA or 1',4'-trans-diol-ABA,
CC       depending on the order of action of these 2 enzymes (By similarity).
CC       ABA2 is responsible for the hydroxylation of carbon atom C-1' and ABA4
CC       might be involved in the oxidation of the C-4' carbon atom (By
CC       similarity). {ECO:0000250|UniProtKB:Q14RS1,
CC       ECO:0000269|PubMed:26648962}.
CC   -!- PATHWAY: Hormone biosynthesis. {ECO:0000269|PubMed:26648962}.
CC   -!- INDUCTION: Expression is up-regulated in spores.
CC       {ECO:0000269|PubMed:26648962}.
CC   -!- DISRUPTION PHENOTYPE: Leads to slower vegetative growth and dark
CC       pigmentation of the mycelia (PubMed:26648962). Leads also to the
CC       secretion of a very dark pigment (PubMed:26648962). Affects sporulation
CC       and appressoria formation (PubMed:26648962). Shows hyper-branching of
CC       the germ tubes, as well as unusual bulges along the hyphae with less
CC       melainized appressoria (PubMed:26648962). Significantly reduces the
CC       production of abscisic acid (ABA) (PubMed:26648962). Highly reduces
CC       virulence (PubMed:26648962). {ECO:0000269|PubMed:26648962}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; JH793052; ELQ38066.1; -; Genomic_DNA.
DR   AlphaFoldDB; L7I518; -.
DR   SMR; L7I518; -.
DR   Proteomes; UP000011086; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009688; P:abscisic acid biosynthetic process; IMP:GO_Central.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   NADP; Oxidoreductase; Virulence.
FT   CHAIN           1..269
FT                   /note="Short-chain dehydrogenase/reductase ABA4"
FT                   /id="PRO_0000448424"
FT   ACT_SITE        174
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q12634"
FT   BINDING         32..56
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q12634"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q12634"
SQ   SEQUENCE   269 AA;  28172 MW;  4C6CADCC7FF3A891 CRC64;
     MGSIENPEIM ASTMLHILPL AGKVYGITGG ASGIGLATAQ ILSRRGATVC IADVDPKAMA
     SAEVYFSGQS GAKYSITKVD ISKRSEVNAW VDGIISQFGR LDGAANVAGV IGKIHGAVPV
     SEMDDDEWDK IVAVNLTGTM YCMRAQLRNI VDGGSIVNVA SIHGLKGFAN HAAYDASKHG
     VIGLTKAAAQ ENGAREIRVN AVAPGAIYTP LMQKNWDITG RPKDAPFDDP SAFRRQGTAM
     ETGNVIAFLL GPDSTFVSGS VYSVDGAWI