ID   ALT1_ALTSO              Reviewed;         524 AA.
AC   Q5KTN3;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Cytochrome P450 monooxygenase alt1 {ECO:0000303|PubMed:16356847};
DE            EC=1.-.-.- {ECO:0000305|PubMed:16356847};
DE   AltName: Full=Alternapyrone biosynthesis cluster protein 1 {ECO:0000303|PubMed:16356847};
GN   Name=alt1 {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB120221; BAD83680.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5KTN3; -.
DR   SMR; Q5KTN3; -.
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   SUPFAM; SSF48264; SSF48264; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..524
FT                   /note="Cytochrome P450 monooxygenase alt1"
FT                   /id="PRO_0000444924"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         469
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   524 AA;  60532 MW;  D62BD38196DE315E CRC64;
     MPAASELERR TKRSKSRNKI SKPIANMLSV IAFSICISPI VYFLIRSIYY LVFHPLSDYP
     GPKLWAISRI PWNYVNLQGD LAWRIRDMHL HYNSSVIRIA PDELSYTSST ALKKIDGTPP
     PREFLKCLDG RGIAPAVVNR RRSIVTETPE RHTILRRALQ PAFSERALRD QEDFFRDHTD
     RLIAQLRKPQ YGVTEQNILR WFALLSFDIM SDLAFGQPAG CLDLVDEPWL GVIGSRVKSI
     VWYQFAVYYR IEWILKWIMP KAAMEARKRH QALTLQKVQR RIEEERSGKR EGKKRDFMSY
     ILGNDKENLS NMDLFGMASA FIVAGSNTTT YTMTAFTFFV CRDSEVYAKV IAEVRDKFAS
     DTDITMVAAG DLPYLKACIE ETMRLSPPTP SALPRWVLEG GEEIDGKWVP GGVTVGVHNL
     AACHVPWNWH RPLEFIPERW LQTKEGEFTH DDRALHARFL MVDIMSLTCF LSSMAMNEMR
     LALAKLFWNF DISLSRNSGN WWITQKSYLV WEKKPLMVTI KPRH