ID   85A19_PRUDU             Reviewed;         483 AA.
AC   B2XBQ5; A0A5E4FTL8;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   02-DEC-2020, sequence version 2.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=(R)-mandelonitrile beta-glucosyltransferase {ECO:0000305};
DE            EC=2.4.1.354 {ECO:0000269|PubMed:32688778};
DE   AltName: Full=UDP-glycosyltransferase 85A19 {ECO:0000303|PubMed:32688778};
GN   Name=UGT85A19 {ECO:0000303|PubMed:32688778};
GN   ORFNames=ALMOND_2B036004 {ECO:0000312|EMBL:VVA30855.1};
OS   Prunus dulcis (Almond) (Amygdalus dulcis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=3755;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   TISSUE=Leaf;
RX   PubMed=32688778; DOI=10.1071/fp07275;
RA   Franks T.K., Yadollahi A., Wirthensohn M.G., Guerin J.R., Kaiser B.N.,
RA   Sedgley M., Ford C.M.;
RT   "A seed coat cyanohydrin glucosyltransferase is associated with bitterness
RT   in almond (Prunus dulcis) kernels.";
RL   Funct. Plant Biol. 35:236-246(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Texas;
RX   PubMed=31529539; DOI=10.1111/tpj.14538;
RA   Alioto T., Alexiou K.G., Bardil A., Barteri F., Castanera R., Cruz F.,
RA   Dhingra A., Duval H., Fernandez I Marti A., Frias L., Galan B.,
RA   Garcia J.L., Howad W., Gomez-Garrido J., Gut M., Julca I., Morata J.,
RA   Puigdomenech P., Ribeca P., Rubio Cabetas M.J., Vlasova A., Wirthensohn M.,
RA   Garcia-Mas J., Gabaldon T., Casacuberta J.M., Arus P.;
RT   "Transposons played a major role in the diversification between the closely
RT   related almond and peach genomes: results from the almond genome
RT   sequence.";
RL   Plant J. 101:455-472(2020).
CC   -!- FUNCTION: Involved in the biosynthesis of the cyanogenic glycoside (R)-
CC       prunasin, a precursor of (R)-amygdalin, which at high concentrations is
CC       associated with intense bitterness in kernels of almond
CC       (PubMed:32688778). Stereo-selectively glucosylates (R)-mandelonitrile
CC       to produce (R)-prunasin (PubMed:32688778).
CC       {ECO:0000269|PubMed:32688778}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-mandelonitrile + UDP-alpha-D-glucose = (R)-prunasin + H(+)
CC         + UDP; Xref=Rhea:RHEA:55984, ChEBI:CHEBI:15378, ChEBI:CHEBI:17396,
CC         ChEBI:CHEBI:18450, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885;
CC         EC=2.4.1.354; Evidence={ECO:0000269|PubMed:32688778};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55985;
CC         Evidence={ECO:0000305};
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; EU015987; ABV68925.1; -; mRNA.
DR   EMBL; CABIKO010000198; VVA30855.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2XBQ5; -.
DR   SMR; B2XBQ5; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   EnsemblPlants; VVA30855; VVA30855; Prudul26B036004.
DR   Gramene; VVA30855; VVA30855; Prudul26B036004.
DR   KEGG; ag:ABV68925; -.
DR   OMA; MGSHVVC; -.
DR   BioCyc; MetaCyc:MON-20308; -.
DR   Proteomes; UP000327085; Chromosome: 1.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IDA:UniProtKB.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   InterPro; IPR035595; UDP_glycos_trans_CS.
DR   Pfam; PF00201; UDPGT; 1.
DR   PROSITE; PS00375; UDPGT; 1.
PE   1: Evidence at protein level;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..483
FT                   /note="(R)-mandelonitrile beta-glucosyltransferase"
FT                   /id="PRO_0000451484"
FT   BINDING         304
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         360..361
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         378..386
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         400..403
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   CONFLICT        127
FT                   /note="T -> S (in Ref. 1; ABV68925)"
FT   CONFLICT        454
FT                   /note="M -> K (in Ref. 1; ABV68925)"
FT   CONFLICT        461
FT                   /note="A -> S (in Ref. 1; ABV68925)"
SQ   SEQUENCE   483 AA;  53697 MW;  2B6252C85CB4F203 CRC64;
     MSPVASKEKP HAVFVPFPAQ GHINPMLQLA KLLNYKGFHI TFVNTEFNHK RMLESQGSHA
     LDGLPSFRFE TIPDGLPPAD ADARRNLPLV CDSTSKTCLA PFEALLTKLN SSPDSPPVTC
     IVADGVTSFT LDAAEHFGIP EVLFWTTSAC GLMGYVQYYR LIEKGLTPFK DAKDFANGYL
     DTEIDWIPGM KDVRLKDMPS FIRTTDPNDI MLHYMVSETE RSKKASAIIL NTFDALEQEV
     VDALSTLLPP IYSIGPLQLP YSEIPSEYND LKAIGSNLWA ENTECLNWLD TKEPNSVVYV
     NFGSTTVMTN EQLVEFSWGL ANSKKPFLWI IRPGLVAGET AVVPPEFLEE TKERGMLASW
     CPQEQVLLHS AIGGFLTHSG WNSTLEALCG GVPLICWPFF AEQQTNVRYS CTQWGIGIEI
     DGEVKRDYID GLVRTLMDGE EGKKMRKKAL EWKMLAEDAT APKGSSYLAL ENVVSKVLLS
     PRD