ALT1_ALTAL
ID ALT1_ALTAL Reviewed; 2624 AA.
AC A0A3G9H990;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Highly reducing polyketide synthase ALT1 {ECO:0000303|PubMed:18435561};
DE Short=HR-PKS FUM1 {ECO:0000303|PubMed:18435561};
DE EC=2.3.1.- {ECO:0000269|PubMed:18435561};
DE AltName: Full=AAL-toxin biosynthesis cluster protein 1 {ECO:0000303|PubMed:18435561};
GN Name=ALT1 {ECO:0000303|PubMed:18435561};
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=As-27;
RA Akagi Y., Akamatsu H., Takao K., Tsuge T., Kodama M.;
RT "AAL-toxin biosynthetic genes cluster in the tomato pathotype of Alternaria
RT alternata.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND PATHWAY.
RX PubMed=18435561; DOI=10.1021/np8000514;
RA Zhu X., Vogeler C., Du L.;
RT "Functional complementation of fumonisin biosynthesis in FUM1-disrupted
RT fusarium verticillioides by the AAL-toxin polyketide synthase gene ALT1
RT from Alternaria alternata f. sp. Lycopersici.";
RL J. Nat. Prod. 71:957-960(2008).
RN [3]
RP FUNCTION.
RX PubMed=19749175; DOI=10.1128/ec.00135-09;
RA Akagi Y., Akamatsu H., Otani H., Kodama M.;
RT "Horizontal chromosome transfer, a mechanism for the evolution and
RT differentiation of a plant-pathogenic fungus.";
RL Eukaryot. Cell 8:1732-1738(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND PATHWAY.
RX PubMed=19449880; DOI=10.1021/np900193j;
RA Li Y., Shen Y., Zhu X., Du L.;
RT "Introduction of the AAL-toxin polyketide synthase gene ALT1 into FUM1-
RT disrupted Fusarium verticillioides produces metabolites with the fumonisin
RT methylation pattern.";
RL J. Nat. Prod. 72:1328-1330(2009).
RN [5]
RP FUNCTION.
RX DOI=10.4172/2157-7471.S2-001;
RA Kheder A.A., Akagi Y., Tsuge T., Kodama M.;
RT "Functional analysis of the ceramide synthase gene ALT7, a homolog of the
RT disease resistance gene Asc1, in the plant pathogen Alternaria alternata.";
RL J. Plant Pathol. Microbiol. 2:0-0(2012).
CC -!- FUNCTION: Highly reducing polyketide synthase; part of the gene cluster
CC that mediates the biosynthesis of the host-selective toxins (HSTs) AAL-
CC toxins, sphinganine-analog mycotoxins responsible for Alternaria stem
CC canker on tomato by the tomato pathotype (PubMed:18435561,
CC PubMed:19749175, PubMed:19449880). The biosynthesis starts with the
CC polyketide synthase ALT1-catalyzed C-16 carbon chain assembly from one
CC starter acetyl-CoA unit with malonyl-CoA extender units
CC (PubMed:18435561, PubMed:19449880). ALT1 also selectively transfers
CC methyl groups at the first and the third cycle of chain elongation for
CC AAL toxin (PubMed:19449880). The C-16 polyketide chain is released from
CC the enzyme by a nucleophilic attack of a carbanion, which is derived
CC from R-carbon of glycin by decarboxylation, on the carbonyl carbon of
CC polyketide acyl chain (Probable). This step is probably catalyzed by a
CC pyridoxal 5'-phosphate-dependent aminoacyl transferase ALT4 (Probable).
CC The respective functions of the other enzymes encoded by the cluster
CC have still to be elucidated (Probable). The sphingosine N-
CC acyltransferase-like protein ALT7 seems not to act as a
CC resistance/self-tolerance factor against the toxin in the toxin
CC biosynthetic gene cluster, contrary to what is expected (Ref.5).
CC {ECO:0000269|PubMed:18435561, ECO:0000269|PubMed:19449880,
CC ECO:0000269|PubMed:19749175, ECO:0000269|Ref.5,
CC ECO:0000305|PubMed:19449880}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:18435561,
CC ECO:0000269|PubMed:19449880}.
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:18435561}.
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 The CDCs are not essential for saprophytic growth but controls host-
CC selective pathogenicity. {ECO:0000269|PubMed:19749175}.
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DR EMBL; AB969680; BBG74267.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G9H990; -.
DR SMR; A0A3G9H990; -.
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; IPR006162; Ppantetheine_attach_site.
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.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Methyltransferase; Multifunctional enzyme; NADP;
KW Oxidoreductase; Phosphopantetheine; Phosphoprotein; Transferase.
FT CHAIN 1..2624
FT /note="Highly reducing polyketide synthase ALT1"
FT /id="PRO_0000449847"
FT DOMAIN 2522..2600
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:18435561"
FT REGION 31..452
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18435561"
FT REGION 289..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..945
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18435561"
FT REGION 1009..1301
FT /note="Dehydrogenase (DH) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18435561"
FT REGION 1493..1599
FT /note="Methyltransferase (CMet) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18435561"
FT REGION 1895..2205
FT /note="Enoyl reductase (ER) (ER) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18435561"
FT REGION 2230..2509
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18435561"
FT ACT_SITE 200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2559
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2624 AA; 284432 MW; F99B76169A32ACB7 CRC64;
MAIVTAFEDE PINGNGMLNA PSISPDPVLP LAIVGMGMRL PGAIHTPEHL WQTLVNKRST
RCEIPDTRFS TNGFHSPSAK PGSIAMRHGH FLADSDSLHH LDPSFFSMGM NEAVDIDPQQ
RLLLEVVYEC MESSGQVNWQ GSKIGCWVGV WGEDWLDLHA KDTFDSGMFR IAGGHDFAIS
NRISYEYNLK GPSYTIKAGC SSSLIALHEA VRALRAGDCD GAIVAGTNLI FSPTMSIGMT
EQGVLSPDAS CKSFDANANG YARGEAINAI YLKRLDVALQ NGDSVRAVVR GTSSNSDGKT
PGMSMPSSES HISLIRQAYR EAGLDPAQTP FVEAHGTGTP VGDPLEAIAI ARVFGGRDRT
LYLGSVKPNL GHSEGASGIS SILKAIQAME HRTIPPNLNF NVPNPKIPFA ESNMVVPCAS
VPWPEGQPVR VSVNSFGIGG SNAHCILESV EEYLGAHGAP WMPIGTRLSN TYTSCFPRLN
FNKTDGGIST TSLSARSVNG MTNLIVHSTD EEMMQSPAVQ ARESYSNHHT LTETTNPSNN
TATNGVVGYQ PRKLLYVVSA GNATSLTAKI MDLHRYHQDH QAQAVDVAYT LCNRRDHLTH
RTYAIASAQP SEGCLSDPAL EFSPPAKINT TTPSHAVMVF TGQGAQWAGM ASELVSDYPV
FRATVSRLSR VLSQLEHAPA WNLLEELRKP EATSRIGEAE FSQPLVCAVQ VGLVDLLRHW
GLSAAAVIGH SSGEIGAAYA ADAITADEAI TIAYYRGYVN KSHTRQGGMA AIGLGVSQVA
PFLSEGVTIA CDNSPQSATI SGDKDVLRDV CSMIRRKQPD CLVRELKVPA AYHSHHMLDL
GGTLESLLKG KVHSQAPAIP FFSSVKVKEI REPGSLDAAY WRENLESPVQ FTGALKILLA
AQPSLSRTVF VEIGPHSALA GPLRQIFKAH GTGQEGYTPA MIRGKDCVDS VLSLVGDLFL
QGITLDLSRI SPPANVITDL PLYPWNHEKE FWSESRVGRD WRFRKYPNHE LLGSQTLESS
KLQPQWRNML KLEHVPWLRD HQVMNDTIFP CAGYLAMAVE AVRQATEAAD VEGFSLRNVV
VRAALVVTES KPVELLTALQ PVRLTNTLDS VWWEFSIMSH NGSVWQKHCN GQVRPGRDAH
HIKAAFSEQA VVSRDKQYPR PVDSLYSELY RLGLRYGPAF CGLNKVHCQP GGKQASAILM
ETIVSESSYA IHPTTIDHCL QLLFPASCEG IFYRAEKLCV PTGIDNLYLA DGKTRESEGA
RIEASSVARS GGAIFGAAKA FSKIDDALLL SLEGGKFSPI EVDDGIVEDL DPLASAHLVW
KPHLDFADMH DLIRPNQDLI NDRHNIDLVE RLTLVAMMFI QERMGSVSSP ANLDHIARFR
NWIDAQVAGL KNGTYSGLEK DVEELLSLKP NDRLPLLKEL EQIIIQSAPA STAVLICRII
DRCDDILQGR IDGIEVLQAD NGLTNFYNYI ESRTESVDFL TAAGHTQPTL RILEIGAGTG
GASQVVLDSL TNQAEHSRLY STYAYTDVSA GFFVAARERF KKYPALDFRV LDISKDPLEQ
GFHASSFDLI IANNVLHATP FLSQTLANVR KLLAPEGYLF LQELSPKMRM VNLIMGILPG
WWLGAAEGRS EEPYLSPEQW DSLLRQTGFS SVDVVYDAPS PYQVNANIIA RAASEPQARD
EKSNGALGAP KAVLLHAPGD EVSERAAQIR SSLEESGLDT SLISIEQFQA NATDTQGIIV
SLLDLTTPFF ASMSASKLTA IQSLVANLGS AHMMWILPRA QKDVSCSDDP AYGMSLGLIR
TLRSERSVAI TTVEVDTFDN AAFSAVARLA IKLAHQQQGD RTSISSGSDL DPDREFVLTK
GVLETGRFHP VSLTHEMAAH APASEATTLR IGRAGLLQTL KWVDLAIKEP EHNEVVVEPR
CVGLNFRDVL VCMGIVEAND VSIGLEGSGV VRKVGNGVTG LQAGDRVFYM ADNCFSSQIT
ISALRCVKIP SSLSFEQAAT MPCVYATVIH SLLDMGGLQS GQSVLIHSAC GGIGIAALNL
CRAMPGVEVY VTVGSEEKVQ YLMQEFGLAR EQIFHSRDTS FVEDVRAATG GRGVDVVLNS
LSGELLHASW ECVAPYGKML EIGKRDFIGK AQLAMDLFEA NRSFIGIDLA RFDAARCGRL
LQRTIDMYVA GAIQPVAPIK VFGATEAEAS FRYMQKGTHL GKIVVSIGKA AAAAATTRQA
VPTQLNPVAT YVLVGGLGGL GRAVATWMVE RGARHLLFLS RSAGQQAAHQ AFFTELQCQG
CSAQAVQGDV TLLGDVERAL AAAPAGKPVR GILQMAMVLR DKAFADMDLA DWHDTVTAKV
LGTWNLHRAA PADMDFFLAT GSISGLFGLP GQANYAAANS YLTALVQHRR AHGMPASVVH
IGMIEDVGYL AENPARADAL RAAGGFFLRT RQLLQAIDWA LAPPSHKPHH LDHELAIGLR
TTKPLLDPGN RVVWRSDPRM GLYHNLTATV ATTADDGSDD SDALRFFITS ITAEPALLDD
PASLDLVTRT IGTRIYTFML HPLDDIDSTA SLTALGVDSL VTIELRNWIK RNFAGLDFST
LEILDARTIA GLAKLILDAL KARFGSSTAD QQRLQSDYLN MKAP
