ABA4_MAGO7
ID ABA4_MAGO7 Reviewed; 269 AA.
AC G4N1P8;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 49.
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 {ECO:0000303|PubMed:26648962}; ORFNames=MGG_07514;
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, 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; CM001233; EHA51620.1; -; Genomic_DNA.
DR RefSeq; XP_003711427.1; XM_003711379.1.
DR AlphaFoldDB; G4N1P8; -.
DR SMR; G4N1P8; -.
DR EnsemblFungi; MGG_07514T0; MGG_07514T0; MGG_07514.
DR GeneID; 2683434; -.
DR KEGG; mgr:MGG_07514; -.
DR VEuPathDB; FungiDB:MGG_07514; -.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_0_1; -.
DR InParanoid; G4N1P8; -.
DR OMA; HMFARAI; -.
DR OrthoDB; 1226147at2759; -.
DR PHI-base; PHI:5440; -.
DR Proteomes; UP000009058; Chromosome 3.
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; Reference proteome; Virulence.
FT CHAIN 1..269
FT /note="Short-chain dehydrogenase/reductase ABA4"
FT /id="PRO_0000448423"
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
