ABA3_BOTFU
ID ABA3_BOTFU Reviewed; 417 AA.
AC Q14RS2;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 19.
DE RecName: Full=Alpha-ionylideneethane synthase aba3 {ECO:0000303|PubMed:30226766};
DE EC=4.2.3.- {ECO:0000269|PubMed:30226766};
DE AltName: Full=Abscisic acid biosynthesis cluster protein 3 {ECO:0000303|PubMed:30226766};
DE AltName: Full=Sesquiterpene synthase aba3 {ECO:0000303|PubMed:30226766};
GN Name=aba3 {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, 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:30226766}.
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; AM237449; CAJ87067.1; -; Genomic_DNA.
DR AlphaFoldDB; Q14RS2; -.
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; Virulence.
FT CHAIN 1..417
FT /note="Alpha-ionylideneethane synthase aba3"
FT /id="PRO_0000448432"
SQ SEQUENCE 417 AA; 47913 MW; 2B624DC7563C544C CRC64;
MQQVITQTLV DDRFIQISDS KKSEGLATDS TKRQSQEQPI HDKDPIKAAT AAMATTPLVK
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 ESTVQNCHTS LVVLNYAANA DYRGEST