ABA3_BOTFB
ID ABA3_BOTFB Reviewed; 440 AA.
AC A0A384JQC9;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 1.
DT 25-MAY-2022, entry version 10.
DE RecName: Full=Alpha-ionylideneethane synthase aba3 {ECO:0000303|PubMed:16820452};
DE EC=4.2.3.- {ECO:0000269|PubMed:30226766};
DE AltName: Full=Abscisic acid biosynthesis cluster protein 3 {ECO:0000303|PubMed:16820452};
DE AltName: Full=Sesquiterpene synthase aba3 {ECO:0000303|PubMed:30226766};
GN Name=aba3 {ECO:0000303|PubMed:16820452}; ORFNames=BCIN_08g03880;
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, CATALYTIC ACTIVITY, AND PATHWAY.
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: Alpha-ionylideneethane synthase; 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: Expression is enhanced at 60 and 90 min after the addition
CC of the ABA precursor mevalonic acid (MVA) to the medium, but declined
CC after 120 min. {ECO:0000269|PubMed:16820452}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of abscisic acid (ABA).
CC {ECO:0000269|PubMed:16820452}.
CC -!- SIMILARITY: Belongs to the alpha-ionylideneethane synthase family.
CC {ECO:0000305}.
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DR EMBL; CP009812; ATZ52743.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A384JQC9; -.
DR VEuPathDB; FungiDB:Bcin08g03880; -.
DR Proteomes; UP000001798; Chromosome bcin08.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0009688; P:abscisic acid biosynthetic process; IDA:GO_Central.
PE 1: Evidence at protein level;
KW Lyase; Reference proteome; Virulence.
FT CHAIN 1..440
FT /note="Alpha-ionylideneethane synthase aba3"
FT /id="PRO_0000448433"
SQ SEQUENCE 440 AA; 50777 MW; 281251A059F3C380 CRC64;
MQQVITQTLV DDRFIQISDS KKSEGLATDS TKRQSQEQPI HDKDPIKAAT AAMAATPLVK
EHQDTWYYPP DIANDLQSIN LPAELKGEIF ACAWEYTRCV IPNYTNWNRY VAFMRIIIMG
IIAEFRGEMV DVTASNNLLG YDLDATLAAL FEGTPGHKEM AREYKTFLLI TADKASERRD
GELFRRYVNA LAQSPRHWFR MRDCDALARF TIASALACND LDDIWFTEDQ FEILTEIGDT
LYDAVAFYKH RAEGETNSTF AYMPEDLRIK AYSECREILW ALDAAWARNP KLANVINFVR
FFGGPIHMMM RRYRFVEENL TIGKSETDKV VDQTRKNFKL WNRVDANKRS VLNTQRYKAL
IARSEELMFP GLAEFLEMGG DGICDKCKYR ESYGAELSHQ FGGVELCSEC RLSWRKYLEC
FVERATKVFP ELKTHFEVPV
