C7113_PRUMU
ID C7113_PRUMU Reviewed; 514 AA.
AC A0A068Q721;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Cytochrome P450 71AP13 {ECO:0000303|PubMed:25015725};
DE EC=1.14.-.- {ECO:0000305};
GN Name=CYP71AP13 {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 in fruit kernel, seedlings, leaves and
CC stems. {ECO:0000269|PubMed:25015725}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB920489; BAP15885.1; -; mRNA.
DR RefSeq; NP_001313441.1; NM_001326512.1.
DR AlphaFoldDB; A0A068Q721; -.
DR SMR; A0A068Q721; -.
DR GeneID; 103337960; -.
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..514
FT /note="Cytochrome P450 71AP13"
FT /id="PRO_0000449234"
FT TRANSMEM 20..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 455
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 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 514 AA; 58681 MW; BDFE7BEEC450F520 CRC64;
MYSVLVQETP MALLQLLKEH SSLFAFSLLI LLLKFIYKDK SRKRRVKLPP SPPKLPVIGN
LHQLGNKPHL SLRCLAEKYG PIIYLQLGEI PTVVVSSARL AKEVLKTHDL ALSSRPQIFS
AKHLFYNCTD VVFSPYGAYW RHIRKICILE LLSAKRVQSF SHVREEEVAR LVRRVAEFYP
GTTNLTKMLG LYANDVLCRV AFGRGFSEGG DYDRHGFQKM LEEYQELLGG FSIGDFFPSM
EFIHSLTGMK SRLQETFRRF DELFDQMVTD HLSPKREKEE HKDLVDVLLD IQKKESTEMP
LTMDNVKAII LDMFAAGTDT TFITLDWGMT ELLMNRKVLE RAQAEVRGVV GERRVVLESD
LPQLDYMKAV IKEIFRLHPP APVLVPRESM EDVTIDGYDI LAKTRIFVNA WAIGRDPESW
EDPEAFEPER FIGSTIDFKG QDFELIPFGA GRRGCPAVTF GTATIELALA QLLHTFDWEL
PLDTAAKDLD MTEVFGITMH RIANLIVVAR PRFP