ACRS2_ALTAL
ID ACRS2_ALTAL Reviewed; 2513 AA.
AC R4WH05;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Highly reducing polyketide synthase ACRTS2 {ECO:0000303|PubMed:22835272};
DE Short=HR-PKS ACRTS2 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:22835272};
DE AltName: Full=ACR-toxin biosynthesis protein S2 {ECO:0000303|PubMed:22835272};
GN Name=ACRTS2 {ECO:0000303|PubMed:22835272};
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, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=HC1;
RX PubMed=22835272; DOI=10.1094/mpmi-06-12-0155-r;
RA Izumi Y., Ohtani K., Miyamoto Y., Masunaka A., Fukumoto T., Gomi K.,
RA Tada Y., Ichimura K., Peever T.L., Akimitsu K.;
RT "A polyketide synthase gene, ACRTS2, is responsible for biosynthesis of
RT host-selective ACR-toxin in the rough lemon pathotype of Alternaria
RT alternata.";
RL Mol. Plant Microbe Interact. 25:1419-1429(2012).
RN [2]
RP FUNCTION.
RC STRAIN=HC1;
RX PubMed=22779742; DOI=10.1094/phyto-02-12-0021-r;
RA Izumi Y., Kamei E., Miyamoto Y., Ohtani K., Masunaka A., Fukumoto T.,
RA Gomi K., Tada Y., Ichimura K., Peever T.L., Akimitsu K.;
RT "Role of the pathotype-specific ACRTS1 gene encoding a hydroxylase involved
RT in the biosynthesis of host-selective ACR-toxin in the rough lemon
RT pathotype of Alternaria alternata.";
RL Phytopathology 102:741-748(2012).
RN [3]
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: Highly reducing polyketide synthase; part of the gene cluster
CC that mediates the biosynthesis of the host-selective toxins (HSTs) ACR-
CC toxins responsible for brown spot of rough lemon disease by the rough
CC lemon pathotype (PubMed:22835272). ACR-toxins cause uncoupling of
CC mitochondrial oxidative-phosphorylation similar to that of classic
CC protonophore (PubMed:22846083). The structure of the major form of ACR-
CC toxin (ACR-toxin I) consists of an alpha-dihydropyrone ring in a 19-
CC carbon polyalcohol, a typical polyketide structure. Minor toxins were
CC characterized as having a pyrone ring with polyalcohol side chains
CC different in length and showing weaker toxicity (PubMed:22846083). The
CC highly reducing polyketide synthase ACRTS2 has all necessary enzymatic
CC domains for multiple cycles of condensation and beta-keto processing
CC (PubMed:22779742). The cytochrome P450 monooxygenase ACRTS1 has also
CC been shown to be essential for ACR-toxin biosynthesis, however its
CC exact role in the pathway has not been elucidated yet
CC (PubMed:22779742). {ECO:0000269|PubMed:22779742,
CC ECO:0000269|PubMed:22835272, ECO:0000303|PubMed:22846083}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:22835272}.
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; an
CC enoylreductase (ER) domain that reduces enoyl groups to alkyl group; 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:22835272}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of ACR-toxin and impairs
CC the pathogenicity (PubMed:22835272). Does not affect growth rate of
CC cultures, sporulation, and spore germination (PubMed:22835272).
CC {ECO:0000269|PubMed:22835272}.
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:22835272). The CDCs are not essential for saprophytic growth
CC but controls host-selective pathogenicity (PubMed:22835272). Although
CC conventional disruption of ACRTS2 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 ACRTS2 is likely an advantage for RNA
CC silencing, because it allows knockdown of all copies of this gene
CC simultaneously (PubMed:22835272). {ECO:0000269|PubMed:22835272}.
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DR EMBL; AB725683; BAN19720.1; -; Genomic_DNA.
DR AlphaFoldDB; R4WH05; -.
DR SMR; R4WH05; -.
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; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
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; IPR020843; PKS_ER.
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; PF08240; ADH_N; 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; SM00829; PKS_ER; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 2.
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 3: Inferred from homology;
KW Acyltransferase; Methyltransferase; Multifunctional enzyme; NADP;
KW Oxidoreductase; Phosphopantetheine; Phosphoprotein;
KW S-adenosyl-L-methionine; Transferase; Virulence.
FT CHAIN 1..2513
FT /note="Highly reducing polyketide synthase ACRTS2"
FT /id="PRO_0000444852"
FT DOMAIN 2433..2510
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:22835272"
FT REGION 7..432
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22835272"
FT REGION 547..875
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22835272"
FT REGION 942..1253
FT /note="Dehydrogenase (DH) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22835272"
FT REGION 1407..1600
FT /note="Methyltransferase (CMet) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22835272"
FT REGION 1816..2127
FT /note="Enoylreductase (ER) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22835272"
FT REGION 2152..2327
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22835272"
FT ACT_SITE 174
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 635
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 974
FT /note="For beta-hydroxyacyl dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2470
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2513 AA; 276530 MW; AB64C41B62C6456F CRC64;
MEKDTPVAII GVSYRAPGIG GKGLWDYLAE AKSAWTKVPP ERFEHFAWYK AGEKKTGVFA
NEGAHFVDNV FDFDAAFFNM RADEARCADP SHRFMLEVAL EAAENAGQSL LDLSGKKIGV
FVGAGQHEYS HRVSDDEYAI QTFTATGVAP CMAANRLSYF FDIDGPSVVL DAACASSAYA
VDMAVKAIRN GDCDGAFVGA AALNLSPSGW LVLDQSGTLS DIGRSFSYDA KASGFGRGEG
AACLLIKRLE DAIRDGDPIQ ALIRGTACSH SGRSEGITMP SRRAQEKLIW DVHNSAGLDP
SNTAVVEVFS RGHGTGTAVG DPIEAGAFTS VLARNRTAAN PIYIGSLKSN FGHLEGASGV
LAMIKAVLMV RNGVVLPTAG FERINEAIDN YEKIKVPTTP LPWPENEPRR CLVTNFGFGG
SSSAVIIDRS PYLHALDGYE DLADIKIPRL NGSSGRSESG SGQSQRLFVF SAKTRDSLTA
YLASFHEYLL KAQESHEFLK DLSYTLGQRR THHAYRASVV ANSISDLRKE IPNLKPSKIR
QRSVIFVFTG QGAQYARMAY NLRQFTVFAE TLEKAETQLN KMGASWSLTE ELNKLTDTRI
NDAEISQPAC TAVQLAMVAL LQSWGVVPNM VTGHSSGEIA AAFTAGLLTF QEAIAISYFR
GQSAVQLSAA QHEYKKGAML ALGVGSEDAL KIIDEHAQGY ATVAAINSPR SVTISGDKTA
IENVRKAADM QGLFARMLKV EVAYHSRHME QVAASYLKDI EPYFQGKAIP AENSGACRPV
FVSSVTGQII DAVDSSYWIK NLVQPVLFAD AIKEVLTHED QGKSQSIHGS SKTLVEIGPH
AALKNPVKQT AELLSSERAW NLASLNYLPS LLRGTNDVHA ILELARALFD LGASVELSGV
NGTNKHNARV LTELPSYAWD RSYYELRPRV THDKQFPGEE YHALIGRKAP SNAAQENTYR
QVFTLDEMPW IRDHVVSGVT VFPMTGYMSC AIEAARRVDS AAPAAFLITD FHVVQSLEIH
EEETVDLTTK LKPAATGEGT FSSKVWSFEV VSWSEANGWT RHCWGKIEPE IADLTLATPT
FEASLPLVTS MAGVIEHDMD NEYHNIELRG TKYGPSFRNN VKFYEGKNYT VLEHRIRDLG
DALKIPVYRG SPVSVDPPTL DSFLQGAGPF QYDGSGRRLT QMPDYISRFR ISNNITSEPN
HRLDVVMRRL DYDDKGGRMH VSVAVFGRGS DDQFTPIAEW ESFTFRTVSS ADDQSASVPD
NWSWELLPRY DLISKDTLRD RLLESVGDLG EEEDVRMSKL DAVGCYYIEK ALKDTVTLDY
SKLPTHLARF VHWGRNVLKE YEVNFESEPT SLLEDVRNLD AQGELLCLMG ENLVDILAGR
IEPLEVMLTD GRLMRHYEAD VANAHLSKII GYLTENMADL EPWQRILEIG GGTAGTTLPV
LEGLSRNRDE PGCLDYTFTD ISSGFFEMAS KKLSRWSQQI TYKRLDITQD PAMQGFTQES
YDVVVAANVL HATADMVTTM THVRSLLKPG GKLILLEATR HPPWLLPFTL LPDWWAAKDK
YRDHKQGPMM PAVVWNDLLL DSGFSGVDVV IPTNYRTDNP LMNVVCSTRI GKQDDSETIT
ICGPLVDDTE VNFAQSVARS ISKELGCPTE IKRFADIKPD DESYYILLDS KHESVFQNFN
PGKFECLKSL LLRNKGLLWV TAKGCSPDAK MIQGMVRTVR LEVEPKNLML LDNVPSTPEG
LSGILKLAAR LRDPEVSRDQ DMDFAWHDGA IHLPRMRQLK DLKEQFSVEE GVAFRRTQNL
RDNSDRGLEM TIQAAGSPDT IYFRRTDPYE VSEDEVLVRV EAAGVGHRDF EVLMGSIPWA
PPGYEGAGKV LKIGSQVSHL REGDDVFFLT PEASAFATEV KLASWLVARI PKNMTVTDAA
ACPLGYCLAT LAFRTARLTK NETVLIHSAA SSVGQACILL AQDIGARIYV TAGTEDKRDY
LHQALGIPRD HIFSSRTAEF RDSLLCKTNN RGVDVVVNSL SGELLTETWA VIAAFGRFVE
IGKKDAFLNN SLPMRPFNNN VTLSAIDLRD LYHHRPDDVR SVWNEVVNLL QRKQVRPVDS
ASVVSISHFS AALRILRSRD HIGRLVVTLG DDNSVMAETA LRPSQVSLKD DATYLVAGGT
RGIGLDLAYW MIEHGARNIV LLGRSGASGP EAQKILNKFR NTKVCVRAVA CNVGDRDELQ
NALESIKDLP AIRGVVHSAL LLSDKLFVNA SYEDWVINTT PRVAGAWNLD DLLPTDLDFF
VALSSFNGDT GHTGQAIYAG TAGFYNAFSQ YRNNRGQYTV SIGLPVVLDV GYVADHDLRG
GLLNDSLSAG VTMADIRATF NCILLGPSSP FVRNGRASTF KVYINGQPVQ DVTWNYFHPA
HSKVRLTNAN RNKVKATSGG AEISSASWTT AEDPLTGLIE ALIAKVSAMT MMEREDVLPD
APLASYSLDS LVSVELRNWI RRETTAEMTL VSITKAENLR ALAVNILAQR KAG
