ID   SOL6_ALTSO              Reviewed;         461 AA.
AC   D7UQ39;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Cytochrome P450 monooxygenase sol6 {ECO:0000303|PubMed:20486243};
DE            EC=1.-.-.- {ECO:0000305|PubMed:20486243};
DE   AltName: Full=Solanapyrone biosynthesis protein 6 {ECO:0000303|PubMed:20486243};
GN   Name=sol6;
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], AND FUNCTION.
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: Cytochrome P450 monooxygenase; 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   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Phytotoxin biosynthesis. {ECO:0000305|PubMed:20486243}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB514562; BAJ09784.1; -; Genomic_DNA.
DR   PRIDE; D7UQ39; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..461
FT                   /note="Cytochrome P450 monooxygenase sol6"
FT                   /id="PRO_0000438554"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         444
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P04798"
FT   CARBOHYD        307
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        324
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   461 AA;  52263 MW;  127AC3D3F1265085 CRC64;
     MFVPSNIGWL VLSCGLFVAY WVLLAIYRLH FHPLSRYRGP RVAAVSNSWY EWYWNYYLNG
     QMIFEIQRLH KQYGPVVRIG VNDLSIDDPE VYQAMTKVSS GFTKDPHFYR CISFPGTSIG
     ETDPAQSRIR RKVLTPALSG TRVQELAPAI LVKVERLLRR VDLCAQSAKT ICITSACKAL
     TMDIISKIVL GREIGCIEEP DFRNSFIENL NAAFETGWIA TAFPRLATLA LWMASMSDFS
     SYLEVFDPHS AVYVAREDVN VPSAIAAHAD RSAVIDMLMD PLTVKGHTVP SLEQLNDEAV
     ILLTAGNDTT SNSMIFGLYQ ICNNMSVYKT LFQELQGHFP SVDQQITYEE AKQLPYLTAT
     IKEILRLGTP LPGRLPRLIP SSGFQLYGQD LPPKTSIHTS PYLXNRHPSI WDNPNDFNPD
     RWLRKNSRDL DKYLATFNRG ARQCLGKEWV HSYQIAGLWQ D