ID   ALT2_ALTSO              Reviewed;         537 AA.
AC   Q5KTN2;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Cytochrome P450 monooxygenase alt2 {ECO:0000303|PubMed:16356847};
DE            EC=1.-.-.- {ECO:0000305|PubMed:16356847};
DE   AltName: Full=Alternapyrone biosynthesis cluster protein 2 {ECO:0000303|PubMed:16356847};
GN   Name=alt2 {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; BAD83681.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5KTN2; -.
DR   SMR; Q5KTN2; -.
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..537
FT                   /note="Cytochrome P450 monooxygenase alt2"
FT                   /id="PRO_0000444925"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         474
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   537 AA;  60773 MW;  07E84D18A341A5E3 CRC64;
     MQTHLLILAA VVLLIIHIVN NFLIKPLQTL LKSRRLGCGP VPFEPTRWPL DIDTIRRSLK
     ADKEQRTPDF VAGRFETMGR YTWGLSLLGT SNLITAEPRN VQALLATQFD DFIMGTARRT
     NLKTALGRSI FAVDGKAWHR ARETMRPIFS RENVSRLELL EEHVQTMLQI IETKDEGLTT
     DANDRAWSAP VSLAVLLPRL TMDSATELFL GQSTHSLKKA LARQQQKSGN EEHDADSFDH
     AFERMLAILG TRMRLRSLYW LYGNKELQKC INALHAFVDS AIDAADQARK SGSSQLRYDF
     LETLRTRCSD RAEVREQVLG LLAAGRDTTA SLTAWVFYCL VRNPRVYKKL RDTVLAEFGP
     YSTNPGQKIT FEKLKGCTYL QHVLNETLRL HSVVPFNSRC AARDTTLPVG GGPDGSMPVF
     VPKGTEVNFS THVLHRRKDL WGEDADEFVP ERWEKKRPGM TWQYVPFNGG PRICIGQQFA
     LTEAGYVLVR MVQRYDVIEG LDIDVERDWH NFTVVCSPGS PVARDAAVMC RLRVAVE