ID   UGTK4_MANES             Reviewed;         483 AA.
AC   G3FIN8;
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 1 {ECO:0000305};
DE            EC=2.4.1.63 {ECO:0000269|PubMed:21736650};
DE   AltName: Full=Cyanohydrin UDP-glucosyltransferase UGT85K4 {ECO:0000303|PubMed:21736650};
GN   Name=UGT85K4 {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:AEO45781.1};
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; JF727883; AEO45781.1; -; mRNA.
DR   AlphaFoldDB; G3FIN8; -.
DR   SMR; G3FIN8; -.
DR   STRING; 3983.cassava4.1_006561m; -.
DR   KEGG; ag:AEO45781; -.
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 1"
FT                   /id="PRO_0000440668"
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;  54916 MW;  8879A89A997828D7 CRC64;
     MGSISPQKPP HAILVPYPAQ GHVNPLMQLG KLLHARGFYI TFVNTEHNHR RLIRSRGQEF
     IDGLPDFKFE AIPDGLPYTD RDATQHVPSL SDSTRKHCLA PFIDLIAKLK ASPDVPPITC
     IISDGVMAFA IDAARHFGIL EIQFWTTSAC GFMAYLHHIE LVRRGIVPFK DESFLHDGTL
     DQPVDFIPGM PNMKLRDMPS FIRVTDVNDI MFDFLGSEAH KSLKADAIIL NTFDELEQEV
     LDAIAARYSK NIYTVGPFIL LEKGIPEIKS KAFRSSLWKE DLSCLEWLDK REPDSVVYVN
     YGCVTTITNE QLNEFAWGLA NSKHPFLWIV RPDVVMGESA VLPEEFYEEI KDRGLLVSWV
     PQDRVLQHPA VGVFLSHCGW NSTIECISGG KPMICWPFFA EQQTNCKYAC DVWKTGVELS
     TNLKREELVS IIKEMMETEI GRERRRRAVE WRKKAEEAIS VGGVSYNNFD TFIKEVILQQ
     QTQ