ID   ABA4_BOTFU              Reviewed;         258 AA.
AC   Q14RS1;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Short-chain dehydrogenase/reductase aba4 {ECO:0000303|PubMed:16820452};
DE            EC=1.1.1.- {ECO:0000305|PubMed:16820452};
DE   AltName: Full=Abscisic acid biosynthesis cluster protein 4 {ECO:0000303|PubMed:16820452};
GN   Name=aba4 {ECO:0000303|PubMed:16820452};
OS   Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=40559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, FUNCTION, DISRUPTION
RP   PHENOTYPE, AND PATHWAY.
RC   STRAIN=SAS56;
RX   PubMed=16820452; DOI=10.1128/aem.02919-05;
RA   Siewers V., Kokkelink L., Smedsgaard J., Tudzynski P.;
RT   "Identification of an abscisic acid gene cluster in the grey mold Botrytis
RT   cinerea.";
RL   Appl. Environ. Microbiol. 72:4619-4626(2006).
RN   [2]
RP   FUNCTION.
RX   PubMed=15240257; DOI=10.1128/aem.70.7.3868-3876.2004;
RA   Siewers V., Smedsgaard J., Tudzynski P.;
RT   "The P450 monooxygenase BcABA1 is essential for abscisic acid biosynthesis
RT   in Botrytis cinerea.";
RL   Appl. Environ. Microbiol. 70:3868-3876(2004).
RN   [3]
RP   FUNCTION.
RX   PubMed=30226766; DOI=10.1021/jacs.8b08925;
RA   Takino J., Kozaki T., Sato Y., Liu C., Ozaki T., Minami A., Oikawa H.;
RT   "Unveiling biosynthesis of the phytohormone abscisic acid in fungi:
RT   unprecedented mechanism of core scaffold formation catalyzed by an unusual
RT   sesquiterpene synthase.";
RL   J. Am. Chem. Soc. 140:12392-12395(2018).
CC   -!- FUNCTION: Short-chain dehydrogenase/reductase; part of the gene cluster
CC       that mediates the biosynthesis of abscisic acid (ABA), a phytohormone
CC       that acts antagonistically toward salicylic acid (SA), jasmonic acid
CC       (JA) and ethylene (ETH) signaling, to impede plant defense responses
CC       (PubMed:15240257, PubMed:16820452). 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 (PubMed:30226766). The cytochrome P450
CC       monooxygenase aba1 might then be involved in the conversion of alpha-
CC       ionylideneethane to alpha-ionylideneacetic acid (Probable). 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 (Probable). Aba2 is responsible for the hydroxylation of carbon
CC       atom C-1' and aba4 might be involved in the oxidation of the C-4'
CC       carbon atom (PubMed:16820452). {ECO:0000269|PubMed:15240257,
CC       ECO:0000269|PubMed:16820452, ECO:0000269|PubMed:30226766,
CC       ECO:0000305|PubMed:16820452}.
CC   -!- PATHWAY: Hormone biosynthesis. {ECO:0000269|PubMed:16820452}.
CC   -!- INDUCTION: Constitutively expressed at a low level.
CC       {ECO:0000269|PubMed:16820452}.
CC   -!- DISRUPTION PHENOTYPE: Reduces the production of abscisic acid (ABA) and
CC       accumulates a compound that corresponds probably to 1',4'-trans-diol-
CC       ABA. {ECO:0000269|PubMed:16820452}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AM237450; CAJ87068.1; -; Genomic_DNA.
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; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   2: Evidence at transcript level;
KW   NADP; Oxidoreductase; Virulence.
FT   CHAIN           1..258
FT                   /note="Short-chain dehydrogenase/reductase aba4"
FT                   /id="PRO_0000448421"
FT   ACT_SITE        160
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q12634"
FT   BINDING         18..42
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q12634"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q12634"
SQ   SEQUENCE   258 AA;  27106 MW;  49CCC374D382478F CRC64;
     MSSQPFTNKV IALTGSASGI GLETAKLLAS RGARLSLADI QEDKLKELQA XXESEYHVDV
     ITTKVDVRKF GEVEAWINKT IDNFGKLDGS ANLAGVAPES IGLKGIVEQD LDEWEFVLGV
     NLTGTMNSLK AQLKVMANNG SIVNASSIRG LTGAAKNASY SSAKHGIIGL TRTAAKEVGG
     KGIRVNAICP GRISTPMLKT AENSIGLHLQ PGSANYPPIA LGRDGEAKEV AQLVAFLLSD
     ESTYISGADI SIDGGWRC