ID   C7968_PRUMU             Reviewed;         533 AA.
AC   A0A068Q605;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2014, sequence version 1.
DT   03-AUG-2022, entry version 20.
DE   RecName: Full=Tryptophan N-monooxygenase CYP79A68 {ECO:0000303|PubMed:25015725};
DE            EC=1.14.14.156 {ECO:0000269|PubMed:25015725};
DE   AltName: Full=Cytochrome P450 79A68 {ECO:0000303|PubMed:25015725};
GN   Name=CYP79A68 {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: Catalyzes with low efficiency E and Z isomers of indole-3-
CC       acetaldoxime from tryptophan (Trp). {ECO:0000269|PubMed:25015725}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tryptophan + 2 O2 + 2 reduced [NADPH--hemoprotein reductase]
CC         = (E)-(indol-3-yl)acetaldehyde oxime + CO2 + 2 H(+) + 3 H2O + 2
CC         oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:33279,
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:17545, ChEBI:CHEBI:57618, ChEBI:CHEBI:57912,
CC         ChEBI:CHEBI:58210; EC=1.14.14.156;
CC         Evidence={ECO:0000269|PubMed:25015725};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Confined to buds. {ECO:0000269|PubMed:25015725}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB920487; BAP15883.1; -; mRNA.
DR   RefSeq; NP_001313445.1; NM_001326516.1.
DR   AlphaFoldDB; A0A068Q605; -.
DR   SMR; A0A068Q605; -.
DR   GeneID; 103339830; -.
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   1: Evidence at protein level;
KW   Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..533
FT                   /note="Tryptophan N-monooxygenase CYP79A68"
FT                   /id="PRO_0000449235"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         471
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        209
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   533 AA;  60416 MW;  B138C124D24E81F7 CRC64;
     MSLPYLFLDS EVTPPISLSL AFIIFMFLVK FILKTHNKNS VPVVPLPPGP SPWPIVGSLP
     EMWRNRPAHR WIHSLMKKLN TDIACIRLGN VHVIPVTSPE IAREFLKKND AVFASRPVTM
     ATKTLSSGYL TTVVGPWGDQ WRKMRRVLVA EAFNPSRVHW LLGKRNEEAD NLVKFLYNQC
     SANQNGAVVN VRIAAQFYSG SIMRKMIFNR TYFGKGREDG GPGVEEEEHV SALLTLLTYA
     YAFCVSDYLP WLRVFDIDGH EKKVRKAMNI VKKHQEPIVN ERLQEWRDGK RNEPDDLLDV
     FISLKDANGQ PLLSDEEIKA QTTELQLSTV DSPFNIAEWA LTEMLNQPEM LKKAEEELDR
     VVGKKTLVQE SHVPHLPYIR ACAKEVMRLH PVGPFNLPHV SIADAEVAGY FIPKGSNVIL
     SRLELGRNPR VWEEPLRFNP ERHLNIAVDQ QVDLEENDLR FVSFSTGRRG CMGVGLGSTI
     VVMLLARLLQ GFSWSLPPDV DKIDFTEDQI YLKKASPLLA QAKPRLPASV YPI