HMNGT_SORBI
ID HMNGT_SORBI Reviewed; 492 AA.
AC Q9SBL1;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Cyanohydrin beta-glucosyltransferase;
DE EC=2.4.1.85 {ECO:0000269|PubMed:10585420, ECO:0000269|PubMed:12946413, ECO:0000269|PubMed:16169969};
DE AltName: Full=UDP-glucose-p-hydroxymandelonitrile glucosyltransferase;
GN Name=UGT85B1; Synonyms=HMNGT;
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 3-9; 58-95; 100-138;
RP 377-414 AND 471-492, FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION.
RC STRAIN=cv. MR31;
RX PubMed=10585420; DOI=10.1074/jbc.274.50.35483;
RA Jones P.R., Moeller B.L., Hoej P.B.;
RT "The UDP-glucose:p-hydroxymandelonitrile-O-glucosyltransferase that
RT catalyzes the last step in synthesis of the cyanogenic glucoside dhurrin in
RT Sorghum bicolor. Isolation, cloning, heterologous expression, and substrate
RT specificity.";
RL J. Biol. Chem. 274:35483-35491(1999).
RN [2]
RP FUNCTION.
RX PubMed=11474068; DOI=10.1126/science.1062249;
RA Tattersall D.B., Bak S., Jones P.R., Olsen C.E., Nielsen J.K., Hansen M.L.,
RA Hoej P.B., Moeller B.L.;
RT "Resistance to an herbivore through engineered cyanogenic glucoside
RT synthesis.";
RL Science 293:1826-1828(2001).
RN [3]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RX PubMed=12946413; DOI=10.1016/s0031-9422(03)00261-9;
RA Hansen K.S., Kristensen C., Tattersall D.B., Jones P.R., Olsen C.E.,
RA Bak S., Moeller B.L.;
RT "The in vitro substrate regiospecificity of recombinant UGT85B1, the
RT cyanohydrin glucosyltransferase from Sorghum bicolor.";
RL Phytochemistry 64:143-151(2003).
RN [4]
RP 3D-STRUCTURE MODELING, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND MUTAGENESIS OF ARG-201; SER-391 AND GLU-410.
RX PubMed=16169969; DOI=10.1104/pp.105.063842;
RA Thorsoee K.S., Bak S., Olsen C.E., Imberty A., Breton C., Moeller B.L.;
RT "Determination of catalytic key amino acids and UDP sugar donor specificity
RT of the cyanohydrin glycosyltransferase UGT85B1 from Sorghum bicolor.
RT Molecular modeling substantiated by site-specific mutagenesis and
RT biochemical analyses.";
RL Plant Physiol. 139:664-673(2005).
RN [5]
RP FUNCTION.
RX PubMed=15665094; DOI=10.1073/pnas.0409233102;
RA Kristensen C., Morant M., Olsen C.E., Ekstroem C.T., Galbraith D.W.,
RA Moeller B.L., Bak S.;
RT "Metabolic engineering of dhurrin in transgenic Arabidopsis plants with
RT marginal inadvertent effects on the metabolome and transcriptome.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:1779-1784(2005).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=17706731; DOI=10.1016/j.phytochem.2007.06.033;
RA Nielsen K.A., Tattersall D.B., Jones P.R., Moeller B.L.;
RT "Metabolon formation in dhurrin biosynthesis.";
RL Phytochemistry 69:88-98(2008).
CC -!- FUNCTION: Involved in the biosynthesis of the cyanogenic glucoside
CC dhurrin. Prevents the dissociation and release of toxic hydrogen
CC cyanide. Mandelonitrile, p-hydroxymandelonitrile, benzyl alcohol,
CC benzoic acid and geraniol, but not hydroquinone(1,4-benzenediol),
CC alpha-terpinol, linalool or farnesol are utilized as acceptor
CC substrates. UDP-glucose, but not UDP-xylose or UDP-glucuronic acid can
CC be used as sugar donor. {ECO:0000269|PubMed:10585420,
CC ECO:0000269|PubMed:11474068, ECO:0000269|PubMed:15665094}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-4-hydroxymandelonitrile + UDP-alpha-D-glucose = dhurrin +
CC H(+) + UDP; Xref=Rhea:RHEA:12853, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16660, ChEBI:CHEBI:27826, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885; EC=2.4.1.85;
CC Evidence={ECO:0000269|PubMed:10585420, ECO:0000269|PubMed:12946413,
CC ECO:0000269|PubMed:16169969};
CC -!- ACTIVITY REGULATION: Inhibited by p-hydroxybenzaldehyde.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.14 mM for geraniol {ECO:0000269|PubMed:12946413,
CC ECO:0000269|PubMed:16169969};
CC KM=0.13 mM for beta-citronellol {ECO:0000269|PubMed:12946413,
CC ECO:0000269|PubMed:16169969};
CC KM=1.13 mM for nerol {ECO:0000269|PubMed:12946413,
CC ECO:0000269|PubMed:16169969};
CC KM=0.66 mM for 1-hexanol {ECO:0000269|PubMed:12946413,
CC ECO:0000269|PubMed:16169969};
CC KM=0.73 mM for cis-3-hexen-1-ol {ECO:0000269|PubMed:12946413,
CC ECO:0000269|PubMed:16169969};
CC KM=0.84 mM for mandelonitrile {ECO:0000269|PubMed:12946413,
CC ECO:0000269|PubMed:16169969};
CC KM=6.33 mM for 2-hydroxy-3-methoxybenzyl alcohol
CC {ECO:0000269|PubMed:12946413, ECO:0000269|PubMed:16169969};
CC KM=0.69 mM for 3-methyl-3-buten-1-ol {ECO:0000269|PubMed:12946413,
CC ECO:0000269|PubMed:16169969};
CC KM=10.3 mM for 3-methyl-2-buten-1-ol {ECO:0000269|PubMed:12946413,
CC ECO:0000269|PubMed:16169969};
CC KM=0.8 mM for UDP-glucose {ECO:0000269|PubMed:12946413,
CC ECO:0000269|PubMed:16169969};
CC -!- PATHWAY: Secondary metabolite biosynthesis; dhurrin biosynthesis;
CC dhurrin from L-tyrosine: step 3/3.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17706731}.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:17706731};
CC Peripheral membrane protein {ECO:0000269|PubMed:17706731}; Cytoplasmic
CC side {ECO:0000269|PubMed:17706731}. Note=In the presence of CYP79A1 and
CC CYP71E1, moves toward the surface of the ER membranes in order to form
CC a metabolon.
CC -!- PTM: The N-terminus is partially blocked.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AF199453; AAF17077.1; -; mRNA.
DR RefSeq; XP_002463518.1; XM_002463473.1.
DR AlphaFoldDB; Q9SBL1; -.
DR SMR; Q9SBL1; -.
DR STRING; 4558.Sb01g001220.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR EnsemblPlants; EER90516; EER90516; SORBI_3001G012400.
DR GeneID; 8060874; -.
DR Gramene; EER90516; EER90516; SORBI_3001G012400.
DR KEGG; sbi:8060874; -.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_0_0_1; -.
DR OMA; KEMMAGE; -.
DR OrthoDB; 508327at2759; -.
DR BioCyc; MetaCyc:MON-523; -.
DR BRENDA; 2.4.1.85; 5768.
DR SABIO-RK; Q9SBL1; -.
DR UniPathway; UPA00757; UER00746.
DR ExpressionAtlas; Q9SBL1; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047792; F:cyanohydrin beta-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0010132; P:dhurrin biosynthetic process; IEA:UniProtKB-UniPathway.
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 Cytoplasm; Direct protein sequencing; Endoplasmic reticulum;
KW Glycosyltransferase; Membrane; Transferase.
FT CHAIN 1..492
FT /note="Cyanohydrin beta-glucosyltransferase"
FT /id="PRO_0000365608"
FT MUTAGEN 201
FT /note="R->A: 20-fold reduction in activity."
FT /evidence="ECO:0000269|PubMed:16169969"
FT MUTAGEN 391
FT /note="S->A: 185-fold reduction in activity."
FT /evidence="ECO:0000269|PubMed:16169969"
FT MUTAGEN 410
FT /note="E->A: 225-fold reduction in activity."
FT /evidence="ECO:0000269|PubMed:16169969"
SQ SEQUENCE 492 AA; 52916 MW; ABC6A57AC51E9BE7 CRC64;
MGSNAPPPPT PHVVLVPFPG QGHVAPLMQL ARLLHARGAR VTFVYTQYNY RRLLRAKGEA
AVRPPATSSA RFRIEVIDDG LSLSVPQNDV GGLVDSLRKN CLHPFRALLR RLGQEVEGQD
APPVTCVVGD VVMTFAAAAA REAGIPEVQF FTASACGLLG YLHYGELVER GLVPFRDASL
LADDDYLDTP LEWVPGMSHM RLRDMPTFCR TTDPDDVMVS ATLQQMESAA GSKALILNTL
YELEKDVVDA LAAFFPPIYT VGPLAEVIAS SDSASAGLAA MDISIWQEDT RCLSWLDGKP
AGSVVYVNFG SMAVMTAAQA REFALGLASC GSPFLWVKRP DVVEGEEVLL PEALLDEVAR
GRGLVVPWCP QAAVLKHAAV GLFVSHCGWN SLLEATAAGQ PVLAWPCHGE QTTNCRQLCE
VWGNGAQLPR EVESGAVARL VREMMVGDLG KEKRAKAAEW KAAAEAAARK GGASWRNVER
VVNDLLLVGG KQ
