ID   C7317_PRUMU             Reviewed;         518 AA.
AC   A0A068Q6L2;
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=Cytochrome P450 736A117 {ECO:0000303|PubMed:25015725};
DE            EC=1.14.-.- {ECO:0000305};
GN   Name=CYP736A117 {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], AND TISSUE 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   -!- 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: Expressed at similar levels in fruit kernel,
CC       seedlings, leaves, stems and buds. {ECO:0000269|PubMed:25015725}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB920491; BAP15887.1; -; mRNA.
DR   RefSeq; NP_001313443.1; NM_001326514.1.
DR   AlphaFoldDB; A0A068Q6L2; -.
DR   SMR; A0A068Q6L2; -.
DR   GeneID; 103338182; -.
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   2: Evidence at transcript level;
KW   Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..518
FT                   /note="Cytochrome P450 736A117"
FT                   /id="PRO_0000449233"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         460
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        12
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        185
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        275
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        356
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   518 AA;  58182 MW;  813AA3E0C00C9E93 CRC64;
     MLNPLQVLQE LNESSSFLQP LAFTLLAIFL VLLYTWYSST KTTTQKSTQP PSPPKLPIIG
     NLHQIGSYPH RSLQALSQRH GPLMLLHFGS VPVLVVSSAE AAREILKTHD LTFSDRPKST
     IFEKLLYNYK DVASAPYGEY WRQVRSICVL NLLSNRRVRS FRSVREEETK SMIRNIKGSS
     SSVLNLSEMF VRLTNDVVCK VALGRKYSDG EGGESGRMFK EILGEFGDLL GTVNIGDYVP
     WLSWLSHVNG LGAKLDKVAK QLDDFIDTVV QEHMNHSSRS GDDDQKDFLD ILLAIQKETS
     AGIPIDGVSV KGIILDMFAA GTDTTYSALE WAMTELLRHP RVMNKLQNEV RGIVGNRTDV
     ITEDDLVEMH YLKAVTKETL RLHPPIPLLV PRMSTRDVEV NGYNIKANTQ VFISAWQIGR
     DPKLYDKPEE FEPERFLNNG IDYKGNDFEL IPFGAGRRVC PGIQFAMAVN EIALANIVHK
     FDWALPDEAS GEDLDMTETT GLTAHKKYPL KAVAFPHF