ID   C7150_PRUMU             Reviewed;         497 AA.
AC   A0A068Q5V6;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2014, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Cytochrome P450 71AU50 {ECO:0000303|PubMed:25015725};
DE            EC=1.14.-.- {ECO:0000305};
GN   Name=CYP71AU50 {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 type II
CC       membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in fruit kernel, seedlings, leaves and
CC       stems. {ECO:0000269|PubMed:25015725}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB920490; BAP15886.1; -; mRNA.
DR   RefSeq; NP_001313432.1; NM_001326503.1.
DR   AlphaFoldDB; A0A068Q5V6; -.
DR   SMR; A0A068Q5V6; -.
DR   GeneID; 103326629; -.
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   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..497
FT                   /note="Cytochrome P450 71AU50"
FT                   /id="PRO_5001654157"
FT   TRANSMEM        1..21
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   BINDING         435
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"
SQ   SEQUENCE   497 AA;  56803 MW;  12717D7F7E7AB0EE CRC64;
     MVWIWATIGL LALVHILQAW WKNKKKRLPP GPRGFPIFGS LHLLGEFPNK DLHRLARKYG
     DIMYMRLGLM PTIVISSPEA AELFLKTHDL VFASRPPHEG SKHISFGQKN LIFSEYGAYW
     RDTRKMCTIE LLSNHKINSF KSMRREEVSL CVESIRAAAN NRGVAVDLSD KVSSLSVDMS
     CRMVLGKKYR DEEFDERGFK SVVREAIQLA SAPNLGDYIR FIAPLDLQGF TKRMKSVNKA
     FDNLFEKIIE EHLQPNDGER TMDFVDVMVG FMGSEESEYR IERPHIKAIM LDMLVASMDT
     SATTIEWALS ELMRHPKAMK KVQKELENVV GLDKMVEESD LEKLDYLNMV VKETFRLHPV
     APLLIPHASI EDCTVNGYHI PKKSRVLINV WAIGRDPNAW TDAEKFIPER FEGSSVDVRG
     NHFQLIPFGS GRRRCPGIQL GLTVVQLVLA QLVHCFDWEL PNNMLPEELD MTEEFGLTVP
     RAKHLLAIPS YRLRKSA