ABL3_LEPMJ
ID ABL3_LEPMJ Reviewed; 426 AA.
AC E5A7E2;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 25-MAY-2022, entry version 26.
DE RecName: Full=Alpha-ionylideneethane synthase abl3 {ECO:0000303|PubMed:31034868};
DE EC=4.2.3.- {ECO:0000305|PubMed:31034868};
DE AltName: Full=Abscisic acid biosynthesis cluster protein 3 {ECO:0000303|PubMed:31034868};
DE AltName: Full=Sesquiterpene synthase abl3 {ECO:0000305};
GN Name=abl3 {ECO:0000303|PubMed:31034868}; ORFNames=LEMA_P087760.1;
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Leptosphaeria; Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8;
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
RN [2]
RP IDENTIFICATION, INDUCTION, FUNCTION, AND PATHWAY.
RX PubMed=31034868; DOI=10.1016/j.fgb.2019.04.015;
RA Darma R., Lutz A., Elliott C.E., Idnurm A.;
RT "Identification of a gene cluster for the synthesis of the plant hormone
RT abscisic acid in the plant pathogen Leptosphaeria maculans.";
RL Fungal Genet. Biol. 130:62-71(2019).
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:31034868). The first step of the pathway catalyzes the reaction
CC from farnesyl diphosphate to alpha-ionylideneethane performed by the
CC alpha-ionylideneethane synthase abl3 via a three-step reaction
CC mechanism involving 2 neutral intermediates, beta-farnesene and
CC allofarnesene (By similarity). The cytochrome P450 monooxygenase abl1
CC might then be involved in the conversion of alpha-ionylideneethane to
CC alpha-ionylideneacetic acid (By similarity). Alpha-ionylideneacetic
CC acid is further converted to abscisic acid in 2 steps involving the
CC cytochrome P450 monooxygenase abl2 and the short-chain
CC dehydrogenase/reductase abl4, via the intermediates 1'-deoxy-ABA or
CC 1',4'-trans-diol-ABA, depending on the order of action of these 2
CC enzymes (By similarity). Abl2 is responsible for the hydroxylation of
CC carbon atom C-1' and abl4 might be involved in the oxidation of the C-
CC 4' carbon atom (By similarity). {ECO:0000250|UniProtKB:Q14RS2,
CC ECO:0000269|PubMed:31034868}.
CC -!- PATHWAY: Hormone biosynthesis. {ECO:0000269|PubMed:31034868}.
CC -!- INDUCTION: Expression is induced during the early biotrophic stage of
CC development (PubMed:31034868). Expression is positively regulated by
CC the ABA cluster-specific transcription regulator abl7
CC (PubMed:31034868). {ECO:0000269|PubMed:31034868}.
CC -!- SIMILARITY: Belongs to the alpha-ionylideneethane synthase family.
CC {ECO:0000305}.
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DR EMBL; FP929136; CBX99537.1; -; Genomic_DNA.
DR RefSeq; XP_003843016.1; XM_003842968.1.
DR AlphaFoldDB; E5A7E2; -.
DR EnsemblFungi; CBX99537; CBX99537; LEMA_P087760.1.
DR GeneID; 13289267; -.
DR eggNOG; ENOG502R6U3; Eukaryota.
DR HOGENOM; CLU_707921_0_0_1; -.
DR InParanoid; E5A7E2; -.
DR OMA; EIGDTMY; -.
DR OrthoDB; 963995at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
PE 2: Evidence at transcript level;
KW Lyase; Reference proteome; Virulence.
FT CHAIN 1..426
FT /note="Alpha-ionylideneethane synthase abl3"
FT /id="PRO_0000448435"
SQ SEQUENCE 426 AA; 49237 MW; 816B5F407CC46327 CRC64;
MLLYNSFTEG LKFTKTKILL RYYASALIDV PRDDVIEDAG VSKSQAMQNI RDRWYYPPDL
ANDLQDLDMP KAMKQEIFAC AWEYTRCVIP QYTNWPRYVA FMRIIIIGIV AEFRGNLVDV
TAGDDMMGYN LSTVLDALFL GTADRENMCR EYRSFLLITA DKSSERRNGE LFRRYVNALA
HSPRQWFRMR DADALARFTI AASLACNDLD DLKFSNMEYE ILTEIGDTLY DAVAFFKHRS
EGETNSTFAY MPPDMRVEAF HQAREVLWAM DVALAPKTTL QGVINFVRFF GGPIHMMMRR
YRFVEEHLTI GQVETEKVVD QTRKNFKLWN RLDAKDAKAG DEKRYKDIVS NNSGEVMFPG
LVEFLENEDN CPDCCFRESY GAETKHQFGG VQICSACREE WGRYMKSLPD RAVKAFPELA
YVLSIP