ID   C7916_PRUMU             Reviewed;         534 AA.
AC   A0A068Q7V0;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2014, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=Phenylalanine N-monooxygenase CYP79D16 {ECO:0000303|PubMed:25015725};
DE            EC=1.14.14.40 {ECO:0000269|PubMed:25015725};
DE   AltName: Full=Cytochrome P450 79D16 {ECO:0000303|PubMed:25015725};
DE   Flags: Precursor;
GN   Name=CYP79D16 {ECO:0000303|PubMed:25015725};
OS   Prunus mume (Japanese apricot) (Armeniaca mume).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=102107;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=cv. Nanko; TISSUE=Seedling;
RX   PubMed=25015725; DOI=10.1007/s11103-014-0225-6;
RA   Yamaguchi T., Yamamoto K., Asano Y.;
RT   "Identification and characterization of CYP79D16 and CYP71AN24 catalyzing
RT   the first and second steps in L-phenylalanine-derived cyanogenic glycoside
RT   biosynthesis in the Japanese apricot, Prunus mume Sieb. et Zucc.";
RL   Plant Mol. Biol. 86:215-223(2014).
CC   -!- FUNCTION: Involved in L-phenylalanine-derived cyanogenic glycoside
CC       biosynthesis, including prunasin and amygdalin defensive agents
CC       (PubMed:25015725). Catalyzes the conversion of L-phenylalanine (Phe)
CC       into phenylacetaldoxime (PAOx) (PubMed:25015725). Cannot use tyrosine
CC       (Tyr), tryptophan (Trp) and valine (Val) as substrates
CC       (PubMed:25015725). {ECO:0000269|PubMed:25015725}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-phenylalanine + 2 O2 + 2 reduced [NADPH--hemoprotein
CC         reductase] = (E)-phenylacetaldehyde oxime + CO2 + 2 H(+) + 3 H2O + 2
CC         oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:33263,
CC         Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:47793, ChEBI:CHEBI:57618, ChEBI:CHEBI:58095,
CC         ChEBI:CHEBI:58210; EC=1.14.14.40;
CC         Evidence={ECO:0000269|PubMed:25015725};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- TISSUE SPECIFICITY: Expressed in seedlings.
CC       {ECO:0000269|PubMed:25015725}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB920488; BAP15884.1; -; mRNA.
DR   RefSeq; NP_001313435.1; NM_001326506.1.
DR   AlphaFoldDB; A0A068Q7V0; -.
DR   SMR; A0A068Q7V0; -.
DR   GeneID; 103330459; -.
DR   BioCyc; MetaCyc:MON-20058; -.
DR   BRENDA; 1.14.14.40; 8044.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0102684; F:L-phenylalanine N-monooxygenase activity; IEA:UniProtKB-EC.
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   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..534
FT                   /note="Phenylalanine N-monooxygenase CYP79D16"
FT                   /id="PRO_0000449232"
FT   BINDING         472
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"
FT   CARBOHYD        500
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   534 AA;  60796 MW;  0B82BD62FA83C4C9 CRC64;
     MEANVGFLTL CLAITLVRFL MKRYWHQSKI NDKNNKAIKQ HYPLPPTPKG LRPWPIVGNL
     PEMLMNKPTF RWIHKLMEES NTQIACIRLA NVHVTPVSCP ILSREILKKQ DATFATRPLS
     ISTFLITKGY ITTVMVPFGE QWKKMRKVIT SELLSPMRHK WLTDKRIEEA DHLVRYVFNQ
     CNNDEGSGIV DLRLATQHYC ANVIKRMIFN QRYFTEEMKD GGPSVEEQNY VNAVFDMLRY
     IYAFSASDYI SCLRGLDLDG HEKIIKDCIK LTRKRQDPVI EERIREHQKL GGNKVPVDLL
     DILISLKDAS GQPLLSTDEI KGQVNEMIMA AVDNPSNAAE WAIAEMINQP HLFEKARQEL
     DAVVGKERQV QESDLSQLNF VKACAREAFR LHPVAPFNVP HVSMADTTVG DYFIPKGSHV
     MLSRIGLGRN PKIWDEPLKY KPERHLKDDG SGVVLTESEL RFISFSTGMR GCVASTLGTS
     MTVMLFARLL HGFTWEAPPN ESRIDLTEAD GELLLAKPLF ALAKPRLPAH VYQT