AFT91_ALTAL
ID AFT91_ALTAL Reviewed; 3005 AA.
AC Q50LG3;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Highly reducing polyketide synthase AFT9-1 {ECO:0000303|Ref.1};
DE Short=HR-PKS AFT9-1 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000305|Ref.1};
DE AltName: Full=AF-toxin biosynthesis protein 9-1 {ECO:0000303|Ref.1};
GN Name=AFT9-1 {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], FUNCTION, AND PATHWAY.
RC STRAIN=NAF8;
RX DOI=10.1007/s10327-004-0170-3;
RA Ruswandi S., Kitani K., Akimitsu K., Tsuge T., Shiraishi T., Yamamoto M.;
RT "Structural analysis of cosmid clone pcAFT-2 carrying AFT10-1 encoding an
RT acyl-CoA dehydrogenase involved in AF-toxin production in the strawberry
RT pathotype of Alternaria alternata.";
RL J. Gen. Plant Pathol. 71:107-116(2005).
RN [2]
RP FUNCTION.
RC STRAIN=NAF8;
RX PubMed=12019223; DOI=10.1093/genetics/161.1.59;
RA Hatta R., Ito K., Hosaki Y., Tanaka T., Tanaka A., Yamamoto M.,
RA Akimitsu K., Tsuge T.;
RT "A conditionally dispensable chromosome controls host-specific
RT pathogenicity in the fungal plant pathogen Alternaria alternata.";
RL Genetics 161:59-70(2002).
RN [3]
RP FUNCTION.
RC STRAIN=NAF8;
RX PubMed=15066029; DOI=10.1111/j.1365-2958.2004.04004.x;
RA Ito K., Tanaka T., Hatta R., Yamamoto M., Akimitsu K., Tsuge T.;
RT "Dissection of the host range of the fungal plant pathogen Alternaria
RT alternata by modification of secondary metabolism.";
RL Mol. Microbiol. 52:399-411(2004).
RN [4]
RP FUNCTION.
RC STRAIN=NAF8;
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 [5]
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
CC clusters that mediate the biosynthesis of the host-selective toxins
CC (HSTs) AF-toxins responsible for Alternaria black spot of strawberry
CC disease by the strawberry pathotype (Ref.1). AF-toxin I and III are
CC valine derivatives of 2,3-dyhydroxy-isovaleric acid and 2-hydroxy-
CC isovaleric acid respectively, while AF II is an isoleucine derivative
CC of 2-hydroxy-valeric acid (PubMed:15066029, Ref.1, PubMed:22846083).
CC These derivatives are bound to a 9,10-epoxy-8-hydroxy-9-methyl-
CC decatrienoic acid (EDA) moiety (PubMed:15066029, Ref.1,
CC PubMed:22846083). On cellular level, AF-toxins affect plasma membrane
CC of susceptible cells and cause a sudden increase in loss of K(+) after
CC a few minutes of toxin treatment (PubMed:22846083). The aldo-keto
CC reductase AFTS1 catalyzes the conversion of 2-keto-isovaleric acid (2-
CC KIV) to 2-hydroxy-isovaleric acid (2-HIV) by reduction of its ketone to
CC an alcohol (PubMed:15066029). The acyl-CoA ligase AFT1, the hydrolase
CC AFT2 and the enoyl-CoA hydratases AFT3 and AFT6, but also the
CC polyketide synthase AFT9, the acyl-CoA dehydrogenase AFT10, the
CC cytochrome P450 monooxygenase AFT11 and the oxidoreductase AFT12 are
CC all involved in the biosynthesis of the AK-, AF- and ACT-toxin common
CC EDA structural moiety (PubMed:12019223, Ref.1, PubMed:18986255). The
CC exact function of each enzyme, and of additional enzymes identified
CC within the AF-toxin clusters have still to be determined
CC (PubMed:12019223, Ref.1, PubMed:18986255).
CC {ECO:0000269|PubMed:12019223, ECO:0000269|PubMed:15066029,
CC ECO:0000269|PubMed:18986255, ECO:0000269|Ref.1,
CC ECO:0000303|PubMed:22846083}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|Ref.1}.
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:12019223). The CDCs are not essential for saprophytic growth
CC but controls host-selective pathogenicity (PubMed:12019223).
CC {ECO:0000269|PubMed:12019223}.
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DR EMBL; AB179766; BAD97694.1; -; Genomic_DNA.
DR SMR; Q50LG3; -.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 3.30.559.70; -; 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; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR039551; Cho/carn_acyl_trans.
DR InterPro; IPR042231; Cho/carn_acyl_trans_2.
DR InterPro; IPR011032; GroES-like_sf.
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; PF00755; Carn_acyltransf; 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; 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; PS50075; CARRIER; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Methyltransferase; Multifunctional enzyme; NADP;
KW Oxidoreductase; Phosphopantetheine; Phosphoprotein; Transferase; Virulence.
FT CHAIN 1..3005
FT /note="Highly reducing polyketide synthase AFT9-1"
FT /id="PRO_0000444853"
FT DOMAIN 2293..2375
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 1..340
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 437..751
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 821..1114
FT /note="Dehydrogenase (DH) domain"
FT /evidence="ECO:0000255"
FT REGION 1259..1445
FT /note="Methyltransferase (CMet) domain"
FT /evidence="ECO:0000255"
FT REGION 1683..1985
FT /note="Enoyl reductase (ER) (ER) domain"
FT /evidence="ECO:0000255"
FT REGION 2008..2191
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255"
FT ACT_SITE 87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2335
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 3005 AA; 330824 MW; 778AE477D7565744 CRC64;
MDPQQRLLLE TTYEALENAG IPQANTNGSN TSVHVAMFTR DYDRNVYKDT VGIPKYQVTG
TGEAIMSNRI SHIFNLHGPS MTIDTGCSGA MTAVSQACMS LRSGDCDIAL AGAVNLIMSP
DHHISMSNLH MLNAEGKSYA FDSRGAGYGR GEGVATIVMK RLDDAVRCHD PIRAVILDAV
INQDGYTAGI TLPSSEAQAQ LERKALNRVG LKPQEVAYIE AHGTGTAAGD AAELDALSSV
FCVDRDLPLY VGSVKSNIGH LEAASGMAAL IKATLMLENE AIPPSINFSR PKENLRIDER
NIKIPTALQP WPKGASARIC VNSFGYGGTN AHAILERAPE RPTVMGPKNT PYLFLLSAKS
RASLSRTVKN IKEWISSQHD TLSLRDLSYT LNQRRSMMSW RFGGVATTHQ ELLDVLTQEL
KSSSAVRTPT RANINFVFTG QGAQWPGMGR ELLVVRAFKD SLNQSRNVLH QLGASWDLFD
ELVRDKESSR LKEPQLSQPV TTAIQIALVE TFRSFGISPG AVVGHSSGEI AAAYTAGYLS
HDTAIKIAYY RGFSAEIAKA KGMENGAMLA TDLGEATARE YVAKLVKGKA TVACQNSPNS
STLSGDTTAV SELEEMLSKD SVFNRRLQVD AAYHSHHMEA AAEEYEKSLG DVCVEQPLTK
VRFFSSVVGR EVWEGFDSTY WTTNLTSTVR YCDALQALCR TQFAQPQGEQ SHQLFVEIGP
HNALAGPTRQ SISDLDKQST YSYMSALVRG SGGVGTILGV LSELIKHGHH VDLAALRTLD
PTCQEANVLH DLPSYAWDHS KRFWNESRLS REYRLRKHPY HDLLGLKMTD HTPLRPSWRY
LVGVEGLPWL KDHIVDGTII FPGSGYLCMV MEAAETSFTK ALIIPESPSR VELQLNFCPV
GPTNGNAFHF VITAVSAAGI WAEHCKGSVE VKYAAANRPR KALDIPVTFD QISEGLDVES
EAIEKISSQE LYDELSAVGN TYGPMFRGIN KAIIQADRSA SFISIPDVTR MMPAQYMRPH
FIHPTTLDIL LHSSLPLVNR QVGQASIMPV RIDELALSTL IQNESGSSLA AITTLTSADL
RGGDADILVF SDSGDATDRP VMSVSGLELR RLAPTGQPAT SGTARDICYE MKWDADVEFI
SAEFLRPQKL PPSVKQKWDV IDRATDIYIQ RCLQHLGKRA LDASGDHHKL LVKWMNSTVA
KTQTCEDPTE AKILEMSSSQ GVEGEFLARL GPALPEIITG KVNPLQLMLE DGLLYRVYAD
DSSKRCYDLM AGYLNSKSFK QSGFAVLEIG AGTGGATLPF LQSLDHNGNR PVVFDFTDIS
AGLFESAKER LQDWSDVVNF RTLDIEKNPK DQGFTEGFYD IILACNVLHA TSSVDSTLSK
VRQLLKPEGV LLLLEVTKPR HYHNVTFGTL PGWWKGVNDS RAAGPLLSPE GWSTRMRKAS
LNMQLAVYDD NETPISSLIV AKPIQEVTKK KQVQIVLDSS VPIWLRKFAD QVLSRLAAEE
FGVSLTSWDE MTVNPHDSSI WLVIDNGEHP VLSHVTPIQL QSVTEMLKAP SHVLWISVVH
DPQFSENPFK HLITGISRTA HAENDRLKMI TVDVQQSICQ EEGKEEGNRF MSFLMGVVIS
LSKADLLTIE REYVYKNGQV NIPRVLPSPD IQGWMPGNVT GLPEMKPFHD SQKAWILDIE
RSEFMKMPVF TENDAFRESL DENEIEIDVE AIGVPELLIR HSINGFAGRV IAIRSKVDGI
KVKDNIVAFA ASSYPNRLRV HQSQARVVPQ GVSSRIAAAL LIPLMAVSHA LVNIASTNSP
IVLIHGATGT IAQSSVAIAK ALGSVIIQTV SGDVESPALD DVVSTFADHV VPDQGYSSKH
QLQKVLRQRK VDVILSFSKN RVSKEVAGTL KPFGHCIHIE NGPKPSLQIE QSQYLSNATI
SRFRMDAVVR AQPEAVAFAF STVIDALGSS KMDSKAVNVV SRPVGELDRL FKQEYQHHRN
ESTVLHVDDC LVRVWSSEKR SLSLDSDATY VVSGGRGDLG KRFIRLMCAA GARHFVTLSR
GVSSSHTQLT SLQTELQENV RNDCVLQDIQ CNIADLNEVQ NALAIIKTQG LPPVRGIIQA
AVALEDSTMN SITSDSFNRV LGAKAHGTMN LRNTFAPEGL AFFISLSSAV TVIGTSGQSS
YNAENSVQDA LAQFSNRDGC HYMSLNVGTI EGADATADNQ TRVQALRRQG LISITPDELL
GFFRYSVTSE ARKGHRCRQA IIGFTPESLS LTTAANGTVH SPMFTHVRER GDRKTSEKRS
GAKKTFKATI QETRDFEKIS QLMALWIGEK VANLVAADAS EVDLGSSIAD FYVDSLIIIE
LRNWINRELQ ASIFIPETME SQNLLSLGAK VASRSALVPS SISSKVSNSN DEALSIDSTA
SLSLAPSSQP PEMLETPYAQ LQHLPAADLH TALDMLIESR KGFCTQAELE ETLRASAEWR
GVEKADRDAI VSKFTGSNLR LESYEKALHL ERREPLQDHA VFYLGHITDQ VPDHTQAERA
AIIVHSTLSF KHQLEMGVLE QNSLNGSPLC MSTLQWLFHA TQEPRHELDV MKKYRASGNV
AIMRRGHIFV ATVHDDDGLA ALVALFEDVI QHSEDAIPAL SILTSHRRDD WAQLKGSLES
ITGNAAKLEA IQSAAFVICL DEGAPTNPGE RATSQLLNDR HLSNRWLDKT LQFSVAANGV
SSLIGLNSTL DGLSVKQLHE AITEQILAST RGHMDILHQD HERRPAKRLS VFRELGFEIP
PPITTAIEEK RLRNLAHYPS VAAFSQHYAD LNRTFLGTRR LRSKGTVLMA IVFAIRLFYG
RFEPVWETVT LAKYARGRTD WLQIVTPDVM EWIESAIQRN SGGKSTICGR DMLVQLQAST
TKHTQNVRQV ADSRGFVEPL YAFQAFIESE GRKLPRLFKS EAWKHSDRNA TPKLVKTDCL
GSGGWLRMQE AGFLMPHPNS LFIHYEVHHT DPLVLVQGRD RDVAKFSGCL NEAVKAMRTI
IEQSS
