ID   UGTK5_MANES             Reviewed;         483 AA.
AC   G3FIN9;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Linamarin synthase 2 {ECO:0000305};
DE            EC=2.4.1.63 {ECO:0000269|PubMed:21736650};
DE   AltName: Full=Cyanohydrin UDP-glucosyltransferase UGT85K5 {ECO:0000303|PubMed:21736650};
GN   Name=UGT85K5 {ECO:0000303|PubMed:21736650};
OS   Manihot esculenta (Cassava) (Jatropha manihot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC   Manihot.
OX   NCBI_TaxID=3983 {ECO:0000312|EMBL:AEO45782.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP   SPECIFICITY, AND SUBSTRATE SPECIFICITY.
RX   PubMed=21736650; DOI=10.1111/j.1365-313x.2011.04695.x;
RA   Kannangara R., Motawia M.S., Hansen N.K., Paquette S.M., Olsen C.E.,
RA   Moller B.L., Jorgensen K.;
RT   "Characterization and expression profile of two UDP-glucosyltransferases,
RT   UGT85K4 and UGT85K5, catalyzing the last step in cyanogenic glucoside
RT   biosynthesis in cassava.";
RL   Plant J. 68:287-301(2011).
CC   -!- FUNCTION: UDP-glucosyltransferase catalyzing in planta synthesis of
CC       cyanogenic glucosides. Able to glucosylate acetone cyanohydrin and 2-
CC       hydroxy-2-methylbutyronitrile, forming linamarin and lotaustralin.
CC       Accepts also to some extent, a wide range of potential acceptor
CC       substrates, including simple alcohols, flavonoids, isoflavonoids and
CC       other hydroxynitriles such as p-hydroxymandelonitrile, mandelonitrile,
CC       (E)-4-hydroxy-2-methylbut-2-enenitrile and (E)- 2-(hydroxymethyl)but-2-
CC       enenitrile. {ECO:0000269|PubMed:21736650}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-hydroxy-2-methylpropanenitrile + UDP-alpha-D-glucose = H(+)
CC         + linamarin + UDP; Xref=Rhea:RHEA:20009, ChEBI:CHEBI:15348,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16441, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58885; EC=2.4.1.63;
CC         Evidence={ECO:0000269|PubMed:21736650};
CC   -!- TISSUE SPECIFICITY: Expressed in the cortex, xylem and phloem
CC       parenchyma, and in specific cells in the endodermis of the petiole of
CC       the first unfolded leaf. {ECO:0000269|PubMed:21736650}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; JF727884; AEO45782.1; -; mRNA.
DR   AlphaFoldDB; G3FIN9; -.
DR   SMR; G3FIN9; -.
DR   STRING; 3983.cassava4.1_006558m; -.
DR   KEGG; ag:AEO45782; -.
DR   GO; GO:0050057; F:linamarin synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   Pfam; PF00201; UDPGT; 1.
PE   1: Evidence at protein level;
KW   Glycosyltransferase; Plant defense; Transferase.
FT   CHAIN           1..483
FT                   /note="Linamarin synthase 2"
FT                   /id="PRO_0000440669"
FT   BINDING         359..360
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         377..385
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         399..402
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
SQ   SEQUENCE   483 AA;  54862 MW;  70C896FE6E98FBB2 CRC64;
     MGSLASEIPP HAVLVPYPAQ GHVNPLMQLG KLLHSRGFYI TFVNTEHNHR RLIRSRGQEF
     IDGLPDFKFE AIPDGLPYTD RDATQHVPSL SDSTRKHCLA PFIDLIAKLK ASPDVPPITC
     IISDGVMAFA IDAARHFGIP EIQFWTTSAC GFMAYLHHIE LVRRGIVPFK DESFLHDGTL
     DQPVDFIPGM PNMKLRDMPS FIRVTDVNDI MFDFMGSEAH KSLKADAIIL NTYDELEQEV
     LDAIAARYSK NIYTVGPFIL LEKGIPEIKS KAFRSSLWKE DLSCIEWLDK REPDSVVYVN
     YGCVTTITNE QLNEFAWGLA NSKHPFLWIV RPDVVMGESA VLPEEFYEAI KDRGLLVSWV
     PQDRVLQHPA VGVFLSHCGW NSTIECISGG KPMICWPFFA EQQTNCKYAC DVWKTGVELS
     TNLKREELVS IIKEMMETEI GRERRRRAVE WRKKAEEATS VGGVSYNNFD RFIKEAILQH
     KTK