ID   ABL6_LEPMJ              Reviewed;         495 AA.
AC   E5A7D7;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Acyltransferase abl6 {ECO:0000303|PubMed:31034868};
DE            EC=2.3.1.- {ECO:0000305|PubMed:31034868};
DE   AltName: Full=Abscisic acid biosynthesis cluster protein 6 {ECO:0000303|PubMed:31034868};
GN   Name=abl6 {ECO:0000303|PubMed:31034868}; ORFNames=LEMA_P087710.1;
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, AND FUNCTION.
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: Acyltransferase; part of the gene cluster that mediates the
CC       biosynthesis of abscisic acid (ABA), a phytohormone that acts
CC       antagonistically toward salicylic acid (SA), jasmonic acid (JA) and
CC       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). The acyltransferase abl6 seems not
CC       essential for the biosynthesis of ABA, but it may acetylate ABA as part
CC       of the synthesis of another ABA-related molecule (PubMed:31034868).
CC       {ECO:0000250|UniProtKB:Q6H9H9, 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 plant acyltransferase family. {ECO:0000305}.
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DR   EMBL; FP929136; CBX99532.1; -; Genomic_DNA.
DR   RefSeq; XP_003843011.1; XM_003842963.1.
DR   AlphaFoldDB; E5A7D7; -.
DR   SMR; E5A7D7; -.
DR   EnsemblFungi; CBX99532; CBX99532; LEMA_P087710.1.
DR   GeneID; 13289263; -.
DR   eggNOG; ENOG502RA8D; Eukaryota.
DR   HOGENOM; CLU_560366_0_0_1; -.
DR   InParanoid; E5A7D7; -.
DR   OMA; RTIVKWG; -.
DR   OrthoDB; 1130893at2759; -.
DR   Proteomes; UP000002668; Genome.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; -; 2.
DR   InterPro; IPR023213; CAT-like_dom_sf.
PE   2: Evidence at transcript level;
KW   Reference proteome; Transferase.
FT   CHAIN           1..495
FT                   /note="Acyltransferase abl6"
FT                   /id="PRO_0000448426"
FT   ACT_SITE        171
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8W1W9"
SQ   SEQUENCE   495 AA;  55027 MW;  1A0B4F9CF8E5EFB7 CRC64;
     MKVEVMSSHR VHPEHKKASE ETAILPVIDS WYCYWRTLAA IYLFDAYSGP ELYTDLRQSL
     SKTLDDFPQL AGTLDNCNIQ VEDKSGRSVR RTRVTWGGNT LGGEFIEAKT NARVRSLLPP
     SIQNISSFAW DRSDRTLRPL FPATLPETSG IRVQVTSFKC GGFGIALDMD HALADAHTVG
     LFIGHWSAIH TRMFTSTTTF PSQISLPNVM FNPQFVEKKV HETDNTYGSK MVMLDRAREL
     PTRRPDLRDK SSQRTMQGNM FKPPPKPSAG VPYLLHFSAS EYERITRGIQ QATASPQITD
     QVAFVSFLWA ALNKARARCS VGQAVDLHLP TSFRWTLGLP EGLIGSPLVA VMMDGGPDGE
     VCYTDPVVLA TIITKTLERY TEDALLAIVY DASLRDSPAS MLRGFERRER MEFTSGVGFG
     SDKLSFGCHS PVFVGPIILP VDNLFIMAEG MRTSEAHSSK WYKHGANIFV SLPQDVFRAL
     LADPALINVE LLGDI