ID   PID6_FUSVN              Reviewed;         506 AA.
AC   P38364;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Pisatin demethylase;
DE            EC=1.14.-.-;
DE   AltName: Full=Cytochrome P450 57A2;
GN   Name=PDA6-1; Synonyms=CYP57A2;
OS   Fusarium vanettenii (Neocosmospora pisi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=2747968;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=156-30-6;
RX   PubMed=8076822; DOI=10.1016/0378-1119(94)90296-8;
RA   Reimmann C., Vanetten H.D.;
RT   "Cloning and characterization of the PDA6-1 gene encoding a fungal
RT   cytochrome P-450 which detoxifies the phytoalexin pisatin from garden
RT   pea.";
RL   Gene 146:221-226(1994).
CC   -!- FUNCTION: Can detoxify the phytoalexin pisatin from garden pea. Pisatin
CC       is an antimicrobial compound produced by pea in response to infection
CC       by plant pathogens.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; X73145; CAA51665.1; -; Genomic_DNA.
DR   PIR; S34286; S34286.
DR   AlphaFoldDB; P38364; -.
DR   SMR; P38364; -.
DR   PRIDE; P38364; -.
DR   BioCyc; MetaCyc:MON-19131; -.
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; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..506
FT                   /note="Pisatin demethylase"
FT                   /id="PRO_0000052044"
FT   BINDING         453
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"
SQ   SEQUENCE   506 AA;  56877 MW;  576BD6E0D5C08D5C CRC64;
     MLVDTGLGLI SELRARLGWA ALLQIVPVTV VAYNLLWFIY TSFFSSLRKI PGPFLARISR
     VWEIKKAATG NIHEIVMDLH RCHGPIVRIG PNRYDFDTME ALKIIYRIGN ALPKADYYIP
     FGLPSSPNLF DVQNPARHSA MKKQVASLYT MTALLSYEAG VDGQTIILKE QLQRFCDQKQ
     VIDLPQFLQY YAFDVIGVIT VGKSMGMMET NSDTNGACGA LDAMWHYSSM MAFIPHMHAW
     WLRLSSLLPI DVPIKGLTEY VEQRIIQYRL KAAEFGDDDA LKGENNFLAK LILMERQGTV
     TSTETQQAVG LNIGAGSDTT ANALSSILYF LYTNPRTLRR LREELDTHVK EDPIRFQQSQ
     SMPYLQAVIK EALRLHPGVG TQLTRVVPKG GLVIEGQFFP EGAEVGVNGW ALYHNKAIFG
     NDASVFRPER WLETKGNLNI GGSFAFGAGS RSCIGKNISI LEMSKAIPQI VRNFDIEINH
     GDMTWKNECW WFVKPEYKAM IKPRAA