ACTT5_ALTAL
ID ACTT5_ALTAL Reviewed; 578 AA.
AC C5NN18;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Acyl-CoA synthetase ACTT5 {ECO:0000303|PubMed:19271978};
DE EC=6.2.1.- {ECO:0000305|PubMed:19271978};
DE AltName: Full=ACT-toxin biosynthesis protein 5 {ECO:0000303|PubMed:19271978};
GN Name=ACTT5 {ECO:0000303|PubMed:19271978};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP PATHWAY.
RC STRAIN=SH20;
RX PubMed=19271978; DOI=10.1094/phyto-99-4-0369;
RA Miyamoto M., Ishii Y., Honda A., Masunaka A., Tsuge T., Yamamoto M.,
RA Ohtani K., Fukumoto T., Gomi K., Peever T.L., Akimitsu K.;
RT "Function of genes encoding acyl-CoA synthetase and enoyl-CoA hydratase for
RT host-selective act-toxin biosynthesis in the tangerine pathotype of
RT Alternaria alternata.";
RL Phytopathology 99:369-377(2009).
RN [2]
RP FUNCTION.
RX PubMed=18944496; DOI=10.1094/phyto.2000.90.7.762;
RA Masunaka A., Tanaka A., Tsuge T., Peever T.L., Timmer L.W., Yamamoto M.,
RA Yamamoto H., Akimitsu K.;
RT "Distribution and characterization of AKT homologs in the tangerine
RT pathotype of Alternaria alternata.";
RL Phytopathology 90:762-768(2000).
RN [3]
RP FUNCTION.
RC STRAIN=SH20;
RX PubMed=18986255; DOI=10.1094/mpmi-21-12-1591;
RA Miyamoto Y., Masunaka A., Tsuge T., Yamamoto M., Ohtani K., Fukumoto T.,
RA Gomi K., Peever T.L., Akimitsu K.;
RT "Functional analysis of a multicopy host-selective ACT-toxin biosynthesis
RT gene in the tangerine pathotype of Alternaria alternata using RNA
RT silencing.";
RL Mol. Plant Microbe Interact. 21:1591-1599(2008).
RN [4]
RP FUNCTION.
RC STRAIN=SH20;
RX PubMed=20055645; DOI=10.1094/phyto-100-2-0120;
RA Ajiro N., Miyamoto Y., Masunaka A., Tsuge T., Yamamoto M., Ohtani K.,
RA Fukumoto T., Gomi K., Peever T.L., Izumi Y., Tada Y., Akimitsu K.;
RT "Role of the host-selective ACT-toxin synthesis gene ACTTS2 encoding an
RT enoyl-reductase in pathogenicity of the tangerine pathotype of Alternaria
RT alternata.";
RL Phytopathology 100:120-126(2010).
RN [5]
RP FUNCTION.
RC STRAIN=SH20;
RX PubMed=20192828; DOI=10.1094/mpmi-23-4-0406;
RA Miyamoto Y., Masunaka A., Tsuge T., Yamamoto M., Ohtani K., Fukumoto T.,
RA Gomi K., Peever T.L., Tada Y., Ichimura K., Akimitsu K.;
RT "ACTTS3 encoding a polyketide synthase is essential for the biosynthesis of
RT ACT-toxin and pathogenicity in the tangerine pathotype of Alternaria
RT alternata.";
RL Mol. Plant Microbe Interact. 23:406-414(2010).
RN [6]
RP REVIEW ON HOST-SELECTIVE TOXINS.
RX PubMed=22846083; DOI=10.1111/j.1574-6976.2012.00350.x;
RA Tsuge T., Harimoto Y., Akimitsu K., Ohtani K., Kodama M., Akagi Y.,
RA Egusa M., Yamamoto M., Otani H.;
RT "Host-selective toxins produced by the plant pathogenic fungus Alternaria
RT alternata.";
RL FEMS Microbiol. Rev. 37:44-66(2013).
CC -!- FUNCTION: Acyl-CoA synthetase; part of the gene clusters that mediate
CC the biosynthesis of the host-selective toxins (HSTs) ACT-toxins
CC responsible for brown spot of tangerine disease by the tangerine
CC pathotype which affects tangerines and mandarins (PubMed:19271978).
CC ACT-toxins consist of three moieties, 9,10-epoxy-8-hydroxy-9-methyl-
CC decatrienoic acid (EDA), valine and a polyketide (PubMed:22846083).
CC ACT-toxin I is toxic to both citrus and pear; toxin II the 5''-deoxy
CC derivative of ACT-toxin I, is highly toxic to pear and slightly toxic
CC to citrus (PubMed:22846083). On cellular level, ACT-toxins affect
CC plasma membrane of susceptible cells and cause a sudden increase in
CC loss of K(+) after a few minutes of toxin treatment (PubMed:22846083).
CC The acyl-CoA ligase ACTT1, the hydrolase ACTT2, the enoyl-CoA
CC hydratases ACTT3 and ACTT6, and the acyl-CoA synthetase ACTT5 are all
CC involved in the biosynthesis of the AK-, AF- and ACT-toxin common 9,10-
CC epoxy-8-hydroxy-9-methyl-decatrienoic acid (EDA) structural moiety
CC (PubMed:18944496, PubMed:18986255, PubMed:19271978). The exact role of
CC each enzyme, and of additional enzymes identified within the AF-toxin
CC clusters have still to be determined (PubMed:18944496, PubMed:18986255,
CC PubMed:19271978). On the other hand, ACTTS1 to ACTTS4 are specific to
CC the tangerine pathotype (PubMed:22846083). The function of ACTTS3 is to
CC elongate the polyketide chain portion of ACT-toxin that is unique to
CC this toxin (PubMed:20192828). The enoyl-reductase ACTTS2 might
CC complement the missing enoyl-reductase (ER) domain in ACTTS3 in the
CC synthesis of the polyketide portion of ACT-toxin (PubMed:20055645). The
CC roles of the nonribosomal peptide synthetases-related proteins ACTTS1
CC and ACTTS4 have also still not been elucidated (PubMed:22846083).
CC {ECO:0000269|PubMed:18944496, ECO:0000269|PubMed:18986255,
CC ECO:0000269|PubMed:19271978, ECO:0000269|PubMed:20055645,
CC ECO:0000269|PubMed:20192828, ECO:0000303|PubMed:22846083}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:19271978}.
CC -!- DISRUPTION PHENOTYPE: Leads to drastic reduction of ACT-toxin
CC production and disease severity after inoculation on detached leaves.
CC {ECO:0000269|PubMed:19271978}.
CC -!- MISCELLANEOUS: Gene clusters encoding host-selective toxins (HSTs) are
CC localized on conditionally dispensable chromosomes (CDCs), also called
CC supernumerary chromosomes, where they are present in multiple copies
CC (PubMed:18986255). The CDCs are not essential for saprophytic growth
CC but controls host-selective pathogenicity (PubMed:18986255). Although
CC conventional disruption could not be accomplished due to the high
CC number of the copies identified in the genome, the high sequence
CC identity among these copies is likely an advantage for RNA silencing,
CC because it allows knockdown of all copies of this gene simultaneously
CC (PubMed:18986255). {ECO:0000269|PubMed:18986255}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AB444613; BAH83502.1; -; Genomic_DNA.
DR AlphaFoldDB; C5NN18; -.
DR SMR; C5NN18; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Virulence.
FT CHAIN 1..578
FT /note="Acyl-CoA synthetase ACTT5"
FT /id="PRO_0000444862"
FT REGION 472..551
FT /note="AMP-binding"
FT /evidence="ECO:0000255"
FT BINDING 211..222
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255"
SQ SEQUENCE 578 AA; 64512 MW; 1DE9D29790D23AF5 CRC64;
MLCKFQVFNP IAIELSPHIG NQLLECRGYC KSPALFLKKI CPSLKAVAKH PLIILKVYHD
ADDESRTLSR RQGLSIVRKL VAGFRKAGLK KGDCFAVTSF SDIMYSMVFL GGVAAGRVFS
GTNPAYRVAE MRHHIRTTEV KFFIVEPELL DVVIEGATRE GIPKDCIFVF NVRGQKVPYG
FRSWEWLLQH GEEDWERITD LETLKRTDVA RLTTSGTTGL PKTACQSHYN ATSFHTVIAT
KSQASITWEP RTISPLPMFH VATVPAVHAS PFRTGHPIWI MRRFKLEPFL AGIEKHQVTN
LAVIPPLVTA IINSPLSKKY SLKSVRTAVS GVAPLDAGSQ REMRKLLAPG VTFTQLWGLT
ETTGAMTLFP YPEEDDTGSV GRLIPNTDVK LVDEDGKDIT AFDVRGEICV RGPTVVRQYY
RNSKANAETW DEDGYLHTGD ILYCDSKTKL WYIVDRKKEL IKVRGFQVAP PELEAALLQA
KDDIADVAVI GLKSQPDSDA ERPRAYVVRK PGSDITEAGV KRLIDDHLAS YKQLTGGVVF
LDEIPRSPTG KILKRVLREW AGTEEKENVT TRRALIPL
