ID   ALT3_ALTSO              Reviewed;         509 AA.
AC   Q5KTN1;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Cytochrome P450 monooxygenase alt3 {ECO:0000303|PubMed:16356847};
DE            EC=1.-.-.- {ECO:0000305|PubMed:16356847};
DE   AltName: Full=Alternapyrone biosynthesis cluster protein 3 {ECO:0000303|PubMed:16356847};
GN   Name=alt3 {ECO:0000303|PubMed:16356847};
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.
RC   STRAIN=584;
RX   PubMed=16356847; DOI=10.1016/j.chembiol.2005.09.015;
RA   Fujii I., Yoshida N., Shimomaki S., Oikawa H., Ebizuka Y.;
RT   "An iterative type I polyketide synthase PKSN catalyzes synthesis of the
RT   decaketide alternapyrone with regio-specific octa-methylation.";
RL   Chem. Biol. 12:1301-1309(2005).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of alternapyrone derivatives
CC       (PubMed:16356847). Alternapyrone is a decaketide with octa-methylation
CC       from methionine on every C2 unit except the third unit
CC       (PubMed:16356847). All the domains in the polyketide synthase alt5 are
CC       apparently involved in alternapyrone synthesis, that is, the 8 CMeT, 7
CC       KR, 7 DH, and 4 ER reactions in the 9 KS-mediated condensation steps
CC       required for alternapyrone synthesis (PubMed:16356847). the
CC       alternapyrone produced by alt5 might be intensively modified by
CC       cytochrome P450 monooxygenases alt1, alt2 and alt3 and FAD-dependent
CC       oxidoreductase alt4 present in the alt gene cluster (PubMed:16356847).
CC       {ECO:0000269|PubMed:16356847}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:16356847}.
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; AB120221; BAD83682.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5KTN1; -.
DR   SMR; Q5KTN1; -.
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; IPR017972; Cyt_P450_CS.
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.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..509
FT                   /note="Cytochrome P450 monooxygenase alt3"
FT                   /id="PRO_0000444926"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         450
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"
SQ   SEQUENCE   509 AA;  57907 MW;  673E7751336D66BC CRC64;
     MALSSALDSL WHQLDQLLSL INRNIITGII VLPVLYVLLK VIYNLYLSPL AGYPGPKLWA
     VSRLPWNRAN MKGRISWKIR ELHDKYGPVV RIAPDELSYT TSGAWKKIYG QRNPEFVKAL
     DGRGIAPASI GGQRSLMTEH QDKHLRLRRA IDPAFSQRAL REQESYFQDH SDNLVQKLKQ
     RCKDGPLDMT TWYNLVAFDI VSDLAFGEPS GCVNNPDQPW IQAILARAKA IVWFQLAVQY
     GFMGLLNWMT PKYVTESRKK HIAMTEAKLK ARVEAKNPGK DFMSYILEND EKLNHLELVM
     LSSNFIVAGS GTSAGGMSGL TYLLLRNPDK LEKLKQEIRG LFKSRADMTL QAVTSCKYLR
     ACLNEGMRLY PPTPGSLPRF VPGKGEMIEG KWVPGGYAVG VNQLAAGHSE RNFKKAREFH
     PERWLDEPDS EFKDDDRSAV QPFSYGQRGC IGRSMAYAEM SLTMAKLVWY FDWELDEPDN
     DWWNQQGTYL VWEKLPLQVK LTPVSDVVE