ID   C71Z3_PASSA             Reviewed;         504 AA.
AC   A0A2Z5D850;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2018, sequence version 1.
DT   03-AUG-2022, entry version 10.
DE   RecName: Full=6,7,8-trihydroxycoumarin synthase {ECO:0000303|PubMed:29971079};
DE            EC=1.14.14.- {ECO:0000269|PubMed:29971079};
DE   AltName: Full=Cytochrome P450 CYP71AZ3 {ECO:0000303|PubMed:29971079};
GN   Name=CYP71AZ3 {ECO:0000303|PubMed:29971079};
OS   Pastinaca sativa (Wild parsnip) (Anethum pastinaca).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC   Tordylieae; Tordyliinae; Pastinaca.
OX   NCBI_TaxID=4041;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, REVIEW, AND PATHWAY.
RC   STRAIN=cv. Demi-long de Guernesey;
RX   PubMed=29971079; DOI=10.3389/fpls.2018.00820;
RA   Krieger C., Roselli S., Kellner-Thielmann S., Galati G., Schneider B.,
RA   Grosjean J., Olry A., Ritchie D., Matern U., Bourgaud F., Hehn A.;
RT   "The CYP71AZ P450 subfamily: A driving factor for the diversification of
RT   coumarin biosynthesis in apiaceous plants.";
RL   Front. Plant Sci. 9:820-820(2018).
CC   -!- FUNCTION: Involved in the biosynthesis of coumarins and furanocoumarins
CC       (FCs), natural products required for defense responses against attacks
CC       by predators with potential medical and agroindustrial usages such as
CC       anticoagulant, rodenticide and artificial vanilla substitutes
CC       (PubMed:29971079). Able to catalyze the hydroxylation of esculetin to
CC       produce 6,7,8-trihydroxycoumarin (PubMed:29971079).
CC       {ECO:0000269|PubMed:29971079, ECO:0000303|PubMed:29971079}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:Q94IP1};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=248.6 uM for esculetin (at pH 7.4 and 28 degrees Celsius)
CC         {ECO:0000269|PubMed:29971079};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:29971079}.
CC   -!- SUBCELLULAR LOCATION: Microsome membrane
CC       {ECO:0000250|UniProtKB:Q6QNI4}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; MH000218; AXB38860.1; -; mRNA.
DR   KEGG; ag:AXB38860; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
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   GO; GO:0009805; P:coumarin biosynthetic process; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..504
FT                   /note="6,7,8-trihydroxycoumarin synthase"
FT                   /id="PRO_0000454520"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          363..368
FT                   /note="Substrate specificity"
FT                   /evidence="ECO:0000269|PubMed:29971079"
FT   BINDING         444
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:Q94IP1"
FT   SITE            118
FT                   /note="Substrate specificity"
FT                   /evidence="ECO:0000269|PubMed:29971079"
FT   SITE            299
FT                   /note="Substrate specificity"
FT                   /evidence="ECO:0000269|PubMed:29971079"
FT   SITE            303
FT                   /note="Substrate specificity"
FT                   /evidence="ECO:0000269|PubMed:29971079"
SQ   SEQUENCE   504 AA;  57695 MW;  B8168E19181409DC CRC64;
     MEPVFLFLIL AFPIASVYLL FYHKKRVVGL SAPPGPPGLP FIGNFHQLYK ASSTHEYLWS
     LSKQYGSLVT LRMGSVPILV VSSPKMAKEV LQTQDLIYCS RPAMTGMQKL SYNGLDVAFS
     PYTDQWRHTR KFCTLELFTQ KRAQLNFRPV REQEVSRMIA RLSETAAASK DVNAYEWFSN
     LATCIISRVA FGKRYDEDGI GKERFQRMLS EIDAMFIGFF VSDFFPMFGW IDKLSGMRDR
     LDRTFKDLDM FYQELIDEHL KPNRLESPTE DLIDVMLKNE GSSLTKDSMK AILLNVFNGG
     TGTTATVLAW AMTALLRNQG VMKKAQEEIR SVIGKKGKVD EDDFPSLPYL RAVVKETMRL
     YPPAPVLVPR ETMESSIIGE DKDHMYMVKP KTVVYISMWA IGRDPKTWKN PMEFVPERFL
     ERPDINYKGQ QFEYVPFGAG RRICAGINLG VTTVELALAN LLYTFDWEPP AGMRFEDIDD
     ETTNGLALQK KNALYIRPKK YMFP