ID   PID9_FUSVN              Reviewed;         515 AA.
AC   Q12645; Q02289;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Pisatin demethylase;
DE            EC=1.14.-.-;
DE   AltName: Full=Cytochrome P450 57A1;
GN   Name=PDAT9; Synonyms=CYP57A1, PDA1;
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=T9;
RX   PubMed=8208242; DOI=10.1007/bf00284198;
RA   Maloney A.P., Vanetten H.D.;
RT   "A gene from the fungal plant pathogen Nectria haematococca that encodes
RT   the phytoalexin-detoxifying enzyme pisatin demethylase defines a new
RT   cytochrome P450 family.";
RL   Mol. Gen. Genet. 243:506-514(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60.
RX   PubMed=8012044; DOI=10.1094/mpmi-7-0256;
RA   Straney D.C., Vanetten H.D.;
RT   "Characterization of the PDA1 promoter of Nectria haematococca and
RT   identification of a region that binds a pisatin-responsive DNA binding
RT   factor.";
RL   Mol. Plant Microbe Interact. 7:256-266(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; L20976; AAC01762.1; -; Genomic_DNA.
DR   EMBL; S70757; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; S45583; S45583.
DR   AlphaFoldDB; Q12645; -.
DR   SMR; Q12645; -.
DR   PRIDE; Q12645; -.
DR   OMA; WKTLWFT; -.
DR   BioCyc; MetaCyc:MON-19130; -.
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..515
FT                   /note="Pisatin demethylase"
FT                   /id="PRO_0000052043"
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   515 AA;  58186 MW;  BD227B090F472675 CRC64;
     MLVDTGLGLI SELQAKLGWA VLLQIVPITI VAYNLLWFIY ASFFSSLRKI PGPFLARISR
     VWEMKKTATG NIHEIMMDLH RRHGAIVRIG PRRYDFDTME ALKIIYRIGN ALPKADYYKP
     FGLPSFPNLF DEQNPARHSA IKKQVASLYT MTALLSYEEG VDGQTAILKE QLQRFCDQKQ
     VIDLPRFLQY YAFDVIGVIT VGKSMGMMES NSDTNGACSA LDGMWHYASM MAYIPNMHAW
     WLRLSSLLPI EVPIKGLTEY VERRIIQYRL KAAEFGDDAA LKGENNFLAK LLLMEKKGTV
     TPVETQQAVG LNIGAGSDTT ANALSTILYY LYTNPRTLHT LREELERYVK DGPISFQQSQ
     SMPYLQAVIK EALRLHPGVG TQLTRVVPKG GLVIEGQFFP EGTEVGVNGW ALYHNKAIFG
     NDASIFRPER WLEANENINI GGSFAFGAGS RSCIGKNISI LEMSKAIPQI VRNFDIEINH
     GDMTWKNECW WFVKPEYKAM IKPRRCCLSR DESLV