ABA4_BOTFB
ID ABA4_BOTFB Reviewed; 258 AA.
AC A0A384JQF5;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 1.
DT 03-AUG-2022, entry version 14.
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}; ORFNames=BCIN_08g03830;
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
RX PubMed=23104368; DOI=10.1128/ec.00164-12;
RA Staats M., van Kan J.A.L.;
RT "Genome update of Botrytis cinerea strains B05.10 and T4.";
RL Eukaryot. Cell 11:1413-1414(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
RX PubMed=26913498; DOI=10.1111/mpp.12384;
RA van Kan J.A.L., Stassen J.H.M., Mosbach A., van der Lee T.A.J., Faino L.,
RA Farmer A.D., Papasotiriou D.G., Zhou S., Seidl M.F., Cottam E., Edel D.,
RA Hahn M., Schwartz D.C., Dietrich R.A., Widdison S., Scalliet G.;
RT "A gapless genome sequence of the fungus Botrytis cinerea.";
RL Mol. Plant Pathol. 18:75-89(2017).
RN [4]
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 [5]
RP INDUCTION, FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
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 [6]
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}.
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; CP009812; ATZ52740.1; -; Genomic_DNA.
DR RefSeq; XP_001553969.1; XM_001553919.1.
DR AlphaFoldDB; A0A384JQF5; -.
DR SMR; A0A384JQF5; -.
DR GeneID; 5434516; -.
DR KEGG; bfu:BCIN_08g03830; -.
DR VEuPathDB; FungiDB:Bcin08g03830; -.
DR Proteomes; UP000001798; Chromosome bcin08.
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; Reference proteome; Virulence.
FT CHAIN 1..258
FT /note="Short-chain dehydrogenase/reductase aba4"
FT /id="PRO_0000448422"
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; 27151 MW; 42886C32FE2475A1 CRC64;
MSSQPFTNKV IALTGSASGI GLETAKLLAS RGARLSLADI QEDKLKELQA QLESEYYVDV
ITTKVDVRKF GEVEAWINKT IDNFGKLDGS ANLAGVAPES IGLKGIVEQD LDEWEFVLGV
NLTGTMNSLK AQLKVMANNG SIVNASSIRG LTGAAKNASY SSAKHGIIGL TRTAAKEVGG
KGIRVNAICP GRISTPMLKT AENSIGLHLQ PGSANYPPIA LGRDGEAKEV AQLVAFLLSD
ESTYISGADI SIDGGWRC
