ACTS3_ALTAL
ID ACTS3_ALTAL Reviewed; 2457 AA.
AC D9N1A1;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Highly reducing polyketide synthase ACTTS3 {ECO:0000303|PubMed:20192828};
DE Short=HR-PKS ACTTS3 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000305|PubMed:20192828};
DE AltName: Full=ACT-toxin biosynthesis protein S3 {ECO:0000303|PubMed:20192828};
GN Name=ACTTS3 {ECO:0000303|PubMed:20192828};
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, DOMAIN, DISRUPTION PHENOTYPE,
RP AND PATHWAY.
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 [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 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).
RN [7]
RP INDUCTION.
RX PubMed=29616013; DOI=10.3389/fmicb.2018.00508;
RA Wang M., Yang X., Ruan R., Fu H., Li H.;
RT "Csn5 is required for the conidiogenesis and pathogenesis of the Alternaria
RT alternata tangerine pathotype.";
RL Front. Microbiol. 9:508-508(2018).
CC -!- FUNCTION: Highly reducing polyketide synthase; part of the gene
CC clusters that mediate the biosynthesis of the host-selective toxins
CC (HSTs) ACT-toxins responsible for brown spot of tangerine disease by
CC the tangerine pathotype which affects tangerines and mandarins
CC (PubMed:19271978). ACT-toxins consist of three moieties, 9,10-epoxy-8-
CC hydroxy-9-methyl-decatrienoic acid (EDA), valine and a polyketide
CC (PubMed:22846083). ACT-toxin I is toxic to both citrus and pear; toxin
CC II the 5''-deoxy derivative of ACT-toxin I, is highly toxic to pear and
CC slightly toxic to citrus (PubMed:22846083). On cellular level, ACT-
CC toxins affect plasma membrane of susceptible cells and cause a sudden
CC increase in loss of K(+) after a few minutes of toxin treatment
CC (PubMed:22846083). The acyl-CoA ligase ACTT1, the hydrolase ACTT2, the
CC enoyl-CoA hydratases ACTT3 and ACTT6, and the acyl-CoA synthetase ACTT5
CC are all involved in the biosynthesis of the AK-, AF- and ACT-toxin
CC common 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid (EDA) structural
CC moiety (PubMed:18944496, PubMed:18986255, PubMed:19271978). The exact
CC role of each enzyme, and of additional enzymes identified within the
CC AF-toxin clusters have still to be determined (PubMed:18944496,
CC PubMed:18986255, PubMed:19271978). On the other hand, ACTTS1 to ACTTS4
CC are specific to the tangerine pathotype (PubMed:22846083). The function
CC of ACTTS3 is to elongate the polyketide chain portion of ACT-toxin that
CC is unique to this toxin (PubMed:20192828). The enoyl-reductase ACTTS2
CC might complement the missing enoyl-reductase (ER) domain in ACTTS3 in
CC the synthesis of the polyketide portion of ACT-toxin (PubMed:20055645).
CC The roles of the nonribosomal peptide synthetases-related proteins
CC ACTTS1 and ACTTS4 have also still not been elucidated
CC (PubMed:22846083). {ECO:0000269|PubMed:18944496,
CC ECO:0000269|PubMed:18986255, ECO:0000269|PubMed:19271978,
CC ECO:0000269|PubMed:20055645, ECO:0000269|PubMed:20192828,
CC ECO:0000303|PubMed:22846083}.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000250|UniProtKB:Q9Y8A5};
CC Note=Binds 1 phosphopantetheine covalently.
CC {ECO:0000250|UniProtKB:Q9Y8A5};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:20192828}.
CC -!- INDUCTION: Expression is positively regulated by CSN5 during infection.
CC {ECO:0000269|PubMed:29616013}.
CC -!- DOMAIN: Multidomain protein; including a ketosynthase (KS) that
CC catalyzes repeated decarboxylative condensation to elongate the
CC polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects
CC and transfers the extender unit malonyl-CoA; a dehydratase (DH) domain
CC that reduces hydroxyl groups to enoyl groups; a methyltransferase
CC (CMeT) domain responsible for the incorporation of methyl groups; a
CC ketoreductase (KR) domain that catalyzes beta-ketoreduction steps; and
CC an acyl-carrier protein (ACP) that serves as the tether of the growing
CC and completed polyketide via its phosphopantetheinyl arm.
CC {ECO:0000305|PubMed:20192828}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of ACT-toxin and leads
CC to the loss of pathogenicity (PubMed:20192828). Does not affect growth
CC rate of cultures, sporulation, and spore germination (PubMed:20192828).
CC {ECO:0000269|PubMed:20192828}.
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}.
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DR EMBL; AB516321; BAJ14522.1; -; Genomic_DNA.
DR AlphaFoldDB; D9N1A1; -.
DR SMR; D9N1A1; -.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Methyltransferase; Multifunctional enzyme; NADP;
KW Oxidoreductase; Phosphopantetheine; Phosphoprotein;
KW S-adenosyl-L-methionine; Transferase; Virulence.
FT CHAIN 1..2457
FT /note="Highly reducing polyketide synthase ACTTS3"
FT /id="PRO_0000444855"
FT DOMAIN 2374..2451
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 4..513
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 545..856
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 938..1244
FT /note="Dehydrogenase (DH) domain"
FT /evidence="ECO:0000255"
FT REGION 1399..1587
FT /note="Methyltransferase (CMet) domain"
FT /evidence="ECO:0000255"
FT REGION 2085..2281
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255"
FT ACT_SITE 179
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 641
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 970
FT /note="For beta-hydroxyacyl dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2411
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2457 AA; 271083 MW; 43CF5D9695EFE055 CRC64;
MTPLREPIAV IGSACRFPGG ANSPHKLWEL LRDPRDILRE FPDDRLVLSK FYNGNANHHG
STNVRNRSYL LSEDIRAFDA PFFHINPREA DGMDPAQRIL LEAVYEALEA AGYTMEQMQG
THTSVFVGVM NSDWWDLQMR DTETIATHAA TGTARSIVSN RISYVFDLKG VSMTIDTACS
SSLVALHQAV QSLRSGESTA AIVGGANILL DPAMYIAEST LQMLSPESRS RMWDKSANGY
ARGEGCAAVF LKPLTRAIAD GDHIECVIRE TGVSSDGRTQ GITMPSAAAQ AALIKSTYRS
AGLDPLADRC QYFECHGTGT PAGDPIEAQA IAEAFFSHSG EDAEIYVGSI KTVIGHLEGC
AGLAGLLKAS LAIQNRTIPA NMLFNDLNPL IGPYYRNLKI LQAAKPWPQD IHGPRRASVN
SFGFGGTNAH VILESYEPEM QGTHVLQERS FHGPLTFSAC SKSSLLATIS NFTSYIKTNP
AVDLQNLAWV LQRKRTEFPV KQHFSGSTHA RLIESMEAYL QNAGSSGLHN TTIDTKLLYP
SEIPRVLGIF TGQGAQWATM GKEFIQNSYL FRESIDRSEA ALVALPDPPS WSLISELFAT
VETSRLNEAE LSQPLCTAIQ IAIVDLMFAA GVKLDAVVGH SSGEIAAAYA SGIISAADAM
AIAYYRGFHA KRSHGTGGKR GGMVAAELSY EAALQFCEKV EWAGRLVLAA SNSPSSITLS
GDLDAVQEAH AYFEKENIFS RLLRVDTAYH SHHMIPCAEP YLTSLKACNI QVSQARSDCI
WISSVSGDVQ SSSEEQGALT GEYWVDNMVK PVLFSQAVQC SIWNSGPFES IVEIGPHFAL
KGPTTQVMEA VLESSPPYLS FMRRGHGIET FSDGLGRLWS KLGPSSVDLT GYWKACSSSH
IKFQMLKGLP AYAWDHDKVY WKEGRISRNH RLRKDVPHEL LGRRTADDSD YELRWRNVLR
LTEIPWIRGH KFQGQVLFPA AGYVTMALEA SKALVGDRHV RLFELRDICI RKALVLEEDQ
SSLETVFSVK RLNADFGIHD ENMDLLEAEF SCYVCADETV GTLEKTVSGR IIIHLGSGVD
VKLPPAAHFC TDLSPVDLDR FYSTVEELGL SYQGLFKGLD HAERMLNHSH ALAVWENHSM
GAGSMVHPAL LDVMFQAIFV ASISPAAPST LWTPYLPVSI DRIIVDPDHI PVYSHPEVRA
HIQAYVTKSS ASSIVGDIHL LDSNGIHNGI QVEGLSLKSV AEPTEENDRS IFSQTVWDTD
IASGTDFLRD RKEDAQESKL IHAIERVALF HFRSLVEAIT VEKAKTLAWH HQLFLKAVKA
NIETIRTGGN PVVRQEWLCD TRETIEDLRA QHPGQIDLNL MHAVSEKLIS IVCGETQILE
VMLQDDMLND FYMRGRGFET MNNCIARAVQ QIAHKHPRAK YLEIGAGTGG TTHRILDTIE
SAYTSYEYTD ISSAFFEKAS HKFDKHASKM VFKVLDIEKD VVDQGFENGA YDVVIAANVL
HATRTLSGTM GHIRSLLKPG GYLIFMEVTG DQLRLLFLFG ALPGWWLGAG EGRSLGPGVS
TIAWDNILRN TGFSGVDDVF YDFPDRSRHT CSVMISQAVD DQLRLLRDPL AATGMPISEQ
VLIIGGDTSS VSQLAYDTKR LISPWASCVA INNIDGLDSR RLPSRFSVIC LTELDKPLFS
EIMSEQRLSN LQNLFATANV VFWITSGCNE GTPVANMMVG IGRALATELP HLTLQFLDVK
TVERLKPSIV AQSFFRLVLA KPLVMAEKSM LWTTEPELVF DGDDILIPRV LPDKEMNNRF
NAARRPISEN LWKESTCIEL SNADNSSAPA LFEIKNTIRP GETTIDVKYS VCLGKRCTFV
LGVVSGTSDT VLAISDTNAS SVRISKEHVF FLPHDFSGNS ATLLLDTANH VLAAKLLRCI
SPNSIALIYE PGVRLAAAIR HHAHENTVDV FPATSNREKC GEGWAFIHPH ATERDIRTII
PRNTGCFINL SFKPPGALSR ALLQQTIIHG PDCLSQIVSS ADGFLLEAAF NWATTGLLSL
DSVETVSVQS YVGTTRPSRD FPLVFDWTAP RLPVTVKPLE PKGLFLPDKT YLMIGMTGDL
GRSLCRWMAE HGARYVVLTS RNAEVDSAWI ESMAAIGATV KVYKMDVSNR KSVLGVYTTI
KNSLPTIAGV CNAAMVLEDR LFANMTVGAL SKVFEPKVEG SKVLDEIFHE LNLDFFILFS
SLTSILGNGG QSNYHAANLF MTSMCAQRRA RGLAASVMHI GMVADIGYVA RSDRHIENHL
RKLQYHPMSE TDMHYLFAEA VMSSRADHPG NWNIVSGIET FVDAPGVKLR PPHYHNPRFA
HYVREENARK EDLRTDKTEK SVKELLEDAI SEEDVTTVFQ QAFLIKLERL TQLESHRIDA
NKSLLNLGVD SLSAVEIRNW FLQTVGVDIP VLKLLRGDTV SEISIDATKK YLAQRTS
