ACTS1_ALTAL
ID ACTS1_ALTAL Reviewed; 405 AA.
AC A0A125SUR4;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=Nonribosomal peptide synthetase ACTTS1 {ECO:0000305};
DE Short=NRPS ACTTS1 {ECO:0000305};
DE EC=6.3.2.- {ECO:0000305};
DE AltName: Full=ACT-toxin biosynthesis protein S1 {ECO:0000303|Ref.1};
GN Name=ACTTS1 {ECO:0000303|Ref.1};
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].
RC STRAIN=Tangerine pathotype;
RA Katsumoto M., Ogawa M., Miyamoto Y., Ishimoto T., Masunaka A., Ohtani K.,
RA Mochizuki S., Tsuge T., Yamamoto M., Gomi K., Ichimura K., Peever T.L.,
RA Akimitsu K.;
RT "A non-ribosomal peptide synthetase gene ACTTS4 required for biosynthesis
RT of ACT-toxin in the tangerine pathotype of Alternaria alternata.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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=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 [5]
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 [6]
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 [7]
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: Nonribosomal peptide synthetase; part of the gene clusters
CC that mediate the biosynthesis of the host-selective toxins (HSTs) ACT-
CC toxins 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:0000305}.
CC -!- DOMAIN: NRP synthetases are composed of discrete domains (adenylation
CC (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation
CC (C) domains) which when grouped together are referred to as a single
CC module (By similarity). Each module is responsible for the recognition
CC (via the A domain) and incorporation of a single amino acid into the
CC growing peptide product. Thus, an NRP synthetase is generally composed
CC of one or more modules and can terminate in a thioesterase domain (TE)
CC that releases the newly synthesized peptide from the enzyme.
CC Occasionally, methyltransferase domains (responsible for amino acid
CC methylation) are present within the NRP synthetase (By similarity). The
CC provided sequence of ACTTS1 contains only 1 condensation (C) domain
CC (Probable). {ECO:0000250|UniProtKB:A0A144KPJ6, ECO:0000305}.
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 of ACTT2 could not be accomplished due to the
CC high number of the copies identified in the genome, the high sequence
CC identity among these copies of ACTT2 is likely an advantage for RNA
CC silencing, because it allows knockdown of all copies of this gene
CC simultaneously (PubMed:18986255). {ECO:0000269|PubMed:18986255}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR EMBL; LC026100; BAU45384.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A125SUR4; -.
DR SMR; A0A125SUR4; -.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.559.10; -; 1.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR Pfam; PF00668; Condensation; 1.
PE 3: Inferred from homology;
KW Ligase; Virulence.
FT CHAIN 1..405
FT /note="Nonribosomal peptide synthetase ACTTS1"
FT /id="PRO_0000444814"
FT REGION 39..383
FT /note="Condensation 1"
FT /evidence="ECO:0000255"
SQ SEQUENCE 405 AA; 46075 MW; FBBE0AD749500905 CRC64;
MSSDSEKGRF SLLGLSEPEL SAFIIHKASQ ANVEVSVIED VYPCSPMQEN IQMSKSRSHD
AQYRMVAINH ITLPRAGDSI DIHRLRHAWQ QVADRHSILR TIFAESFDHG RFCDQIVLEH
PDINFHEVSD VNQTPDGISF RQDSPAYLLT IMPLELDERG VVCRIEIDHT IIDGWSYGIM
LRDWARAYAG KLREEGPAPQ YSDYIAFLQT ENHEAHLQYW LNALTGVQPC LVPGTMGLHV
KRTQSSRSVP VLNIRSPILQ AFCRKLKVTV FNVVQAAWTM VLRKYTGMDD VCFGYVAACR
DLPIGNAEEI VGPLINMLVC RTRLDSLQST SELVQAMQRQ MIENGRHQTT SLGAIHHALK
MRGLRLFNTA VNFRSFRRDK FQEHGIAIEV FEDRRNMEVS KISLA
