SOL1_ALTSO
ID SOL1_ALTSO Reviewed; 2641 AA.
AC D7UQ44;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Prosolanapyrone synthase {ECO:0000303|PubMed:20486243};
DE Short=PSS {ECO:0000303|PubMed:20486243};
DE EC=3.2.1.- {ECO:0000269|PubMed:20486243};
DE AltName: Full=Highly reducing polyketide synthase sol1 {ECO:0000303|PubMed:20486243};
DE Short=HR-PKS sol1 {ECO:0000303|PubMed:20486243};
DE AltName: Full=Solanapyrone biosynthesis protein 1 {ECO:0000303|PubMed:20486243};
GN Name=sol1;
OS Alternaria solani.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Porri.
OX NCBI_TaxID=48100;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP DOMAIN.
RX PubMed=20486243; DOI=10.1002/cbic.201000173;
RA Kasahara K., Miyamoto T., Fujimoto T., Oguri H., Tokiwano T., Oikawa H.,
RA Ebizuka Y., Fujii I.;
RT "Solanapyrone synthase, a possible Diels-Alderase and iterative type I
RT polyketide synthase encoded in a biosynthetic gene cluster from Alternaria
RT solani.";
RL ChemBioChem 11:1245-1252(2010).
RN [2]
RP FUNCTION.
RX PubMed=9659400; DOI=10.1016/s0167-4838(98)00040-5;
RA Katayama K., Kobayashi T., Oikawa H., Honma M., Ichihara A.;
RT "Enzymatic activity and partial purification of solanapyrone synthase:
RT first enzyme catalyzing Diels-Alder reaction.";
RL Biochim. Biophys. Acta 1384:387-395(1998).
RN [3]
RP FUNCTION.
RX PubMed=18256508; DOI=10.1271/bbb.70600;
RA Katayama K., Kobayashi T., Chijimatsu M., Ichihara A., Oikawa H.;
RT "Purification and N-terminal amino acid sequence of solanapyrone synthase,
RT a natural Diels-Alderase from Alternaria solani.";
RL Biosci. Biotechnol. Biochem. 72:604-607(2008).
CC -!- FUNCTION: Prosolanapyrone synthase; part of the gene cluster that
CC mediates the biosynthesis of the phytotoxin solanapyrone, a causal
CC agent of early blight disease of potato and tomato (PubMed:20486243).
CC The prosolanapyrone synthase sol1 is a polyketide synthase that
CC produces the octaketide desmethylprosolanapyrone I via sequential
CC condensations of 7 malonyl-CoA units with one acetyl-CoA unit, and one
CC methylation step (PubMed:20486243). The octaketide backbone is further
CC methylated by the sol2 O-methyltransferase to yield prosolanapyrone I
CC (PubMed:20486243). Prosolanapyrone I is hydroxylated to prosolanapyrone
CC II by the cytochrome P450 monooxygenase sol6 (PubMed:20486243). The
CC solanapyrone synthase sol5 then catalyzes the oxidation of
CC prosolanapyrone II and the subsequent Diels Alder cycloisomerization of
CC the product prosolanapyrone III to solanapyrones A and D
CC (PubMed:9659400, PubMed:18256508). Solanapyrones A and D are then
CC converted into solanapyrones B and E, respectively, by the sol3
CC dehydrogenase (PubMed:20486243). {ECO:0000269|PubMed:18256508,
CC ECO:0000269|PubMed:20486243, ECO:0000269|PubMed:9659400}.
CC -!- PATHWAY: Phytotoxin biosynthesis. {ECO:0000305|PubMed:20486243}.
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DR EMBL; AB514562; BAJ09789.1; -; Genomic_DNA.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase 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: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; IPR013149; ADH-like_C.
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; PF00107; ADH_zinc_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; Hydrolase; Methyltransferase; Multifunctional enzyme;
KW NADP; Oxidoreductase; Phosphopantetheine; Phosphoprotein;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..2641
FT /note="Prosolanapyrone synthase"
FT /id="PRO_0000438550"
FT DOMAIN 2561..2639
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 17..443
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:20486243"
FT REGION 456..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..920
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:20486243"
FT REGION 1011..1309
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:20486243"
FT REGION 1477..1665
FT /note="Methyltransferase (MT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:20486243"
FT REGION 1894..2206
FT /note="Enoyl reductase (ER) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:20486243"
FT REGION 2231..2408
FT /note="Ketoreducrase (KR) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:20486243"
FT REGION 2522..2541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2598
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2641 AA; 286573 MW; 20F3C09580E98231 CRC64;
MTSQYGTNGA SADPEPIAIV GMGCRWPGGV RDASSLWELL KNKRSGYREF GDHRFSRKGF
HHPNSEHPGT VATEGGFLLA EDPRLFDHAF FGIGSLEVET MDPSQRKLLE VVYEAFENSG
EPWDSFSGST TGVFVGNFSS DHLIIQGRDT DHPRPYASVG TGTSILSNRV NYIFNLRGPS
VTIDTACSSS MYALHLAISA IRNGDCDSAI VAASNTIIDP STXLMMTKLG VLSPTSTSHT
FDSSADGYAR GEGFSALYLK RMSTAVDGDY PIRALVRGSA LNANGRTGGI THPGREGQEA
VIRKAYENAG NLPMKDTTFF ECHGTGTPVG DPIEISAIGN VFGSATTPEK PLLVGSIKTN
IGHTEPASAI AGIMKVVLAL ENGFIPPSIG IKKLNPKLDL KGGRINILTE NTPWPDGRVR
RASVNSFGYG GANGHCIIDD VRTVLPDYKK RTANTSIGHI NGHTNGHTNG HTNGHTNGHT
NGHTNGHTNG AHASDGHNGH HQNGMNGNSA SHMSEKADKV HYPFSYKPTL VKDFNAKPRR
RVLIPFSAHN EASLDLNITA ISEAIKRENL ADVAYTLAAK RSRFMQRTFR IVDSESPANG
FAVKEKVLAS GTQTARLGFV FTGQGAQWHA MGADLFEYAV FRTSIEYLDS ILASLPTPSA
WKIEDILAGN CDPNDIHKPE VSQTVCTAVQ IGLVDLLYTW NVRPSAAVGH SSGEIAATYA
AGRITAAQAI AAAYFRGQAV SKNKSKGLML AVGLGLDKAE AYISGLDSSV RIAAINSPDS
VTLSGDESTI KDVAAKLNED KVFNRELKTG GNAYHSHHML ALGEFYNSTL SEGLDYVKSL
GQAEPSQLYA TRPWMSSVYP SKSTENPPVS PSYWRANLES PVRFSEALAN MLNLPDPIDV
LVEIGPHPAL KGPVGQISRS VDKSLPYFPT LNRGTNGGIS LLQLAGSLFS LNAEVDLTAV
NAVDVISANQ LKLVHGTTAT NLPPYQYAYG PVIYHESRFS KEFRGRDIVR HDLLGSKLPG
NAKLRPQWRN ILRLKDLPWL NDHKLLPYPV FPAAGYIATV IEAASRIYNE QSEPLDITGY
KLRNVTFSSA MRLPDDDFGL EIITSLELAD AANPKAPTWA TFSISSVARE AGTWTEHCSG
RVRVIAGTSV ANEKMSTEMD ARTLDTKAWY KKFAEIGLGY GPTFQPLSNI RADPSKGLAV
AQLALHTTRD TVEGGESNYP LHPASLDAVF QLSLVASHGG QIDRVCNAFV PVHIDQLYVR
NGVSQDSAVA IALGSMKGLR SAHAKLQVLD KSEQVVLDVG NLRCVTYTEV LPSTGADKEA
FSIPFLRLSW KPDIRAMDNE QVQRRFPPPT ENVEKAYLFD KLERLGTLYV AEIHERYAGQ
GQFSSAPAHI DNFLSWVRRR MKDDNKWVAE ANSLTSSQRG ILIKELFAEV GHISDVKIAN
KVFNNMEDIL NERKTGLEVV IPDNLLHGMY EDGLIMTGAY PQLVRFFDLF GYANPNMRIL
EIGAGTGGAT RKILKTLIGP HGIKRYQDYT FTDISSGFLA QAREAFADFQ DMKYSVLDIQ
ENPLEHGYEA VYDVVVACEC LHATPSIVKT LTNCRKLVKP GGRLVVVENT RAVIGHGLVL
GHLSGYWDGI PDGRVESPFL HLEGWNASLN QTGFAGAELV LDDYPAPYTT ARTIVSSAVE
EPAKVGQSPN GTVHLVHGDN RPELLSRIEH ELTERGTEFK VISIGDVETH LPDNSRTVAF
ADSKSLLVNA SENDLKSFKA LIRKSANLVW VTFGGIVHGH DPDASITTGL LRTLGTENPA
SQFLSIDVSP DSDFQEIRLT RTILDQELAL SDRIAGESRD YEFVWQEDCL WVSRLVPDVA
LQDKLELSES RPSRAEMLPL DSQGSVQAAF ETPGLLTSLY FKPYEETWKS LPDDWIQVKV
AAVGLNWKDL LTSAGRFDMN TFSSEYSGVV AQVGLNVTNV AVGDRVYGYG RGHFGNYVRA
PANFAYRMLP GEDFVKMATI PLVGMTAIYS FECVTQLKDQ ERLLIQSATG GLGLSAIQLA
KAKGAEIFAT AGTQEKRRYL IDVVGIPASH VFSSRDPADF AKLMEATDGK GFNVILSTSS
GELLYDSIKM LAPMGRIIDV GRIDVQNSTS LALELFKRNA TFTSFDLAVA DDADRALGPA
LMKAVNKRVR AGQMGPLSSI TTYDVSQLDQ ALMAFSKGTH VGKLVVTFQN PDALVKMVPA
APHAQFARNA NYLITGGLGG LGRSIVNFMA ERGARHFTVL SRSRKINSEG QMLIDKLATS
GTVVECVSCD VSDSKDVARA VQDAAVVRPI KGIVHAAVSY QDLSFDKLAI EQWTSALAAK
VQGTKNLHEA TKTHALDFFL MTTTIESFVA LATQSAYTAA NNFQDYFARW RRQQGLPAST
VSFGLIRDVG HLSTNSTTLA LMARNKVMDI SEYNFLRLLE PAFLNNESAL DPAASKEPYT
GAVDDPLSVT NVVTCFDPAT MATRKREEAA ENNGNTGNSP RWYTDARVSL IMRAFDDAER
YQASAGGGGD GGNERGNNAG VASLRSEFGE AVKAGPAERS RTVALVTDAI VKTVAQMLFV
DASGVDASRT VADYGVDSLI AAELRNWFNV AFGADVSMLE MLDTATSMKI LANKIVDGAL
A
