ID   PH1_PRUSE               Reviewed;          14 AA.
AC   P29263;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   11-DEC-2019, entry version 48.
DE   RecName: Full=Prunasin beta-glucosidase 1;
DE            EC=3.2.1.118;
DE   AltName: Full=Prunasin beta-glucosidase I;
DE   AltName: Full=Prunasin hydrolase isozyme I;
DE            Short=PH I;
DE   Flags: Fragment;
OS   Prunus serotina (Black cherry).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=23207;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Seed;
RX   PubMed=16652959; DOI=10.1104/pp.100.1.282;
RA   Li C.P., Swain E., Poulton J.E.;
RT   "Prunus serotina amygdalin hydrolase and prunasin hydrolase: purification,
RT   N-terminal sequencing, and antibody production.";
RL   Plant Physiol. 100:282-290(1992).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-prunasin + H2O = D-glucose + mandelonitrile;
CC         Xref=Rhea:RHEA:16489, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16910, ChEBI:CHEBI:17396; EC=3.2.1.118;
CC   -!- SUBUNIT: Monomer.
CC   -!- DEVELOPMENTAL STAGE: Absent from maturing black cherry fruits until 6
CC       weeks after flowering. Then, concomitant with cotyledon development,
CC       the level of enzyme increases with specificity for embryonal tissues.
CC   -!- PTM: Glycosylated.
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DR   GO; GO:0050224; F:prunasin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase.
FT   CHAIN           1..>14
FT                   /note="Prunasin beta-glucosidase 1"
FT                   /id="PRO_0000058367"
FT   NON_TER         14
SQ   SEQUENCE   14 AA;  1577 MW;  FB3D7F4FB90CA9CA CRC64;
     TYPPVVXATL XRTH