UGFGT_MEDTR
ID UGFGT_MEDTR Reviewed; 454 AA.
AC A6XNC6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Flavonoid 3-O-glucosyltransferase;
DE EC=2.4.1.-;
DE AltName: Full=UDP glucose:flavonoid 3-O-glucosyltransferase;
DE AltName: Full=UDP-glycosyltransferase 78G1;
GN Name=UGT78G1; Synonyms=GT83F;
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INDUCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17437063; DOI=10.1007/s11103-007-9167-6;
RA Modolo L.V., Blount J.W., Achnine L., Naoumkina M.A., Wang X., Dixon R.A.;
RT "A functional genomics approach to (iso)flavonoid glycosylation in the
RT model legume Medicago truncatula.";
RL Plant Mol. Biol. 64:499-518(2007).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH MYRICETIN AND UDP.
RX PubMed=19683002; DOI=10.1016/j.jmb.2009.08.017;
RA Modolo L.V., Li L., Pan H., Blount J.W., Dixon R.A., Wang X.;
RT "Crystal structures of glycosyltransferase UGT78G1 reveal the molecular
RT basis for glycosylation and deglycosylation of (iso)flavonoids.";
RL J. Mol. Biol. 392:1292-1302(2009).
CC -!- FUNCTION: Catalyzes the glycosylation of flavonoids at the 3-O-
CC position. Glycosylates the 7-O-position if the 3-O-position is not
CC available. Also able to perform 3-O-glycosylation of anthocyanidins.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=89.8 uM for kaempferol {ECO:0000269|PubMed:17437063};
CC KM=28.7 uM for quercitin {ECO:0000269|PubMed:17437063};
CC KM=52.0 uM for pelargonidin {ECO:0000269|PubMed:17437063};
CC KM=71.8 uM for cyanidin {ECO:0000269|PubMed:17437063};
CC KM=1.5 uM for apigenin {ECO:0000269|PubMed:17437063};
CC KM=36.7 uM for genistein {ECO:0000269|PubMed:17437063};
CC KM=1.6 uM for daidzein {ECO:0000269|PubMed:17437063};
CC KM=11.7 uM for biochanin A {ECO:0000269|PubMed:17437063};
CC KM=1.5 uM for formononetin {ECO:0000269|PubMed:17437063};
CC Vmax=1.5830 umol/min/ug enzyme toward kaempferol
CC {ECO:0000269|PubMed:17437063};
CC Vmax=0.8557 umol/min/ug enzyme toward quercitin
CC {ECO:0000269|PubMed:17437063};
CC Vmax=0.2025 umol/min/ug enzyme toward pelargonidin
CC {ECO:0000269|PubMed:17437063};
CC Vmax=0.1698 umol/min/ug enzyme toward cyanidin
CC {ECO:0000269|PubMed:17437063};
CC Vmax=0.0688 umol/min/ug enzyme toward apigenin
CC {ECO:0000269|PubMed:17437063};
CC Vmax=1.2050 umol/min/ug enzyme toward genistein
CC {ECO:0000269|PubMed:17437063};
CC Vmax=0.0530 umol/min/ug enzyme toward daidzein
CC {ECO:0000269|PubMed:17437063};
CC Vmax=0.3666 umol/min/ug enzyme toward biochanin A
CC {ECO:0000269|PubMed:17437063};
CC Vmax=0.0879 umol/min/ug enzyme toward formononetin
CC {ECO:0000269|PubMed:17437063};
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC -!- TISSUE SPECIFICITY: Highly expressed in flower buds, flowers and pods.
CC Lower expression in leaves, petioles and stems.
CC {ECO:0000269|PubMed:17437063}.
CC -!- DEVELOPMENTAL STAGE: Expressed in developing seeds, with a maximum at
CC 16 days after pollination. Not expressed in nodules.
CC {ECO:0000269|PubMed:17437063}.
CC -!- INDUCTION: Strongly down-regulated by wounding or by methyl jasmonate.
CC {ECO:0000269|PubMed:17437063}.
CC -!- MISCELLANEOUS: For the flavonols kaempferol and quercetin, a
CC significant activity was also observed with UDP-galactose as sugar
CC donor. The reverse reaction (deglycosylation) is observed, but not with
CC formononetin 7-O-glucoside.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; DQ875464; ABI94025.1; -; mRNA.
DR RefSeq; XP_003610163.1; XM_003610115.2.
DR PDB; 3HBF; X-ray; 2.10 A; A=1-454.
DR PDB; 3HBJ; X-ray; 2.10 A; A=1-454.
DR PDBsum; 3HBF; -.
DR PDBsum; 3HBJ; -.
DR AlphaFoldDB; A6XNC6; -.
DR SMR; A6XNC6; -.
DR STRING; 3880.AES92360; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR EnsemblPlants; AES92360; AES92360; MTR_4g128690.
DR GeneID; 11445564; -.
DR Gramene; AES92360; AES92360; MTR_4g128690.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_0_2_1; -.
DR OMA; YGTHAAP; -.
DR OrthoDB; 508327at2759; -.
DR UniPathway; UPA00154; -.
DR EvolutionaryTrace; A6XNC6; -.
DR ExpressionAtlas; A6XNC6; differential.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009698; P:phenylpropanoid metabolic process; 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 3D-structure; Glycosyltransferase; Phenylpropanoid metabolism; Transferase.
FT CHAIN 1..454
FT /note="Flavonoid 3-O-glucosyltransferase"
FT /id="PRO_0000328919"
FT BINDING 25
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000305|PubMed:19683002"
FT BINDING 89
FT /ligand="myricetin"
FT /ligand_id="ChEBI:CHEBI:58395"
FT /evidence="ECO:0000269|PubMed:19683002,
FT ECO:0007744|PDB:3HBF"
FT BINDING 155
FT /ligand="myricetin"
FT /ligand_id="ChEBI:CHEBI:58395"
FT /evidence="ECO:0000269|PubMed:19683002,
FT ECO:0007744|PDB:3HBF"
FT BINDING 192
FT /ligand="myricetin"
FT /ligand_id="ChEBI:CHEBI:58395"
FT /evidence="ECO:0000269|PubMed:19683002,
FT ECO:0007744|PDB:3HBF"
FT BINDING 282
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000305|PubMed:19683002"
FT BINDING 308
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000305|PubMed:19683002"
FT BINDING 334..337
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000305|PubMed:19683002"
FT BINDING 356..360
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000305|PubMed:19683002"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:3HBF"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:3HBF"
FT HELIX 27..40
FT /evidence="ECO:0007829|PDB:3HBF"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:3HBF"
FT HELIX 52..57
FT /evidence="ECO:0007829|PDB:3HBF"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:3HBF"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:3HBF"
FT HELIX 90..114
FT /evidence="ECO:0007829|PDB:3HBF"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:3HBF"
FT HELIX 130..136
FT /evidence="ECO:0007829|PDB:3HBF"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:3HBF"
FT HELIX 149..156
FT /evidence="ECO:0007829|PDB:3HBF"
FT HELIX 158..163
FT /evidence="ECO:0007829|PDB:3HBF"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:3HBF"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:3HBF"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:3HBF"
FT HELIX 201..212
FT /evidence="ECO:0007829|PDB:3HBF"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:3HBF"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:3HBF"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:3HBF"
FT HELIX 229..236
FT /evidence="ECO:0007829|PDB:3HBF"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:3HBF"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:3HBF"
FT HELIX 263..268
FT /evidence="ECO:0007829|PDB:3HBF"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:3HBF"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:3HBJ"
FT HELIX 288..301
FT /evidence="ECO:0007829|PDB:3HBF"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:3HBF"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:3HBF"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:3HBF"
FT TURN 325..328
FT /evidence="ECO:0007829|PDB:3HBF"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:3HBF"
FT HELIX 337..342
FT /evidence="ECO:0007829|PDB:3HBF"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:3HBF"
FT HELIX 355..364
FT /evidence="ECO:0007829|PDB:3HBF"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:3HBF"
FT HELIX 377..385
FT /evidence="ECO:0007829|PDB:3HBF"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:3HBF"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:3HBF"
FT HELIX 401..412
FT /evidence="ECO:0007829|PDB:3HBF"
FT HELIX 415..434
FT /evidence="ECO:0007829|PDB:3HBF"
FT HELIX 440..452
FT /evidence="ECO:0007829|PDB:3HBF"
SQ SEQUENCE 454 AA; 50158 MW; 5026E098D8F2EAE6 CRC64;
MSTFKNEMNG NNLLHVAVLA FPFGTHAAPL LSLVKKIATE APKVTFSFFC TTTTNDTLFS
RSNEFLPNIK YYNVHDGLPK GYVSSGNPRE PIFLFIKAMQ ENFKHVIDEA VAETGKNITC
LVTDAFFWFG ADLAEEMHAK WVPLWTAGPH SLLTHVYTDL IREKTGSKEV HDVKSIDVLP
GFPELKASDL PEGVIKDIDV PFATMLHKMG LELPRANAVA INSFATIHPL IENELNSKFK
LLLNVGPFNL TTPQRKVSDE HGCLEWLDQH ENSSVVYISF GSVVTPPPHE LTALAESLEE
CGFPFIWSFR GDPKEKLPKG FLERTKTKGK IVAWAPQVEI LKHSSVGVFL THSGWNSVLE
CIVGGVPMIS RPFFGDQGLN TILTESVLEI GVGVDNGVLT KESIKKALEL TMSSEKGGIM
RQKIVKLKES AFKAVEQNGT SAMDFTTLIQ IVTS
