ID   UGT43_PUEML             Reviewed;         469 AA.
AC   A0A172J2G3;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 2.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=UDP-glycosyltransferase 43 {ECO:0000303|PubMed:27066037};
DE            Short=PlUGT43 {ECO:0000303|PubMed:27066037};
DE            EC=2.4.1.- {ECO:0000269|PubMed:28207970};
DE   AltName: Full=UDP-glucose:daidzein C-glucosyltransferase {ECO:0000305};
GN   Name=UGT43 {ECO:0000303|PubMed:27066037};
OS   Pueraria montana var. lobata (Kudzu vine) (Pueraria lobata).
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; indigoferoid/millettioid clade; Phaseoleae; Pueraria.
OX   NCBI_TaxID=3893 {ECO:0000312|EMBL:AMQ26115.2};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Root;
RX   PubMed=27066037; DOI=10.3389/fpls.2016.00387;
RA   Wang X., Fan R., Li J., Li C., Zhang Y.;
RT   "Molecular Cloning and Functional Characterization of a Novel (Iso)flavone
RT   4',7-O-diglucoside Glucosyltransferase from Pueraria lobata.";
RL   Front. Plant Sci. 7:387-387(2016).
RN   [2]
RP   FUNCTION, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=28207970; DOI=10.1111/tpj.13510;
RA   Wang X., Li C., Zhou C., Li J., Zhang Y.;
RT   "Molecular characterization of the C-glucosylation for puerarin
RT   biosynthesis in Pueraria lobata.";
RL   Plant J. 90:535-546(2017).
CC   -!- FUNCTION: Glycosyltransferase that catalyzes the C-glucosylation of
CC       daidzein to puerarin (PubMed:28207970). Shows activity with the
CC       isoflavones daidzein and genistein, but has no activity towards
CC       flavonoids such as 2-hydroxynaringenin (PubMed:28207970). Can use UDP-
CC       glucose, but not UDP-galactose or UDP-glucuronic acid as sugar donor
CC       (PubMed:28207970). Does not require bivalent cations for activity
CC       (PubMed:28207970). {ECO:0000269|PubMed:28207970}.
CC   -!- ACTIVITY REGULATION: Inhibited by Cu(2+) or Zn(2+).
CC       {ECO:0000269|PubMed:28207970}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=32.8 uM for daidzein {ECO:0000269|PubMed:28207970};
CC         KM=12.16 uM for genistein {ECO:0000269|PubMed:28207970};
CC         Note=kcat is 0.35 sec(-1) with daidzein as substrate. kcat is 0.45
CC         sec(-1) with genistein as substrate. {ECO:0000269|PubMed:28207970};
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|PubMed:28207970};
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; KU317801; AMQ26115.2; -; mRNA.
DR   AlphaFoldDB; A0A172J2G3; -.
DR   SMR; A0A172J2G3; -.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
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; Transferase.
FT   CHAIN           1..469
FT                   /note="UDP-glycosyltransferase 43"
FT                   /id="PRO_0000439667"
FT   BINDING         280
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         345..346
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         363..371
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         385..388
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
SQ   SEQUENCE   469 AA;  52437 MW;  B4DEC90848AFE8B1 CRC64;
     MTRYEVVFIA IPTLGNLVPQ VEFANLLTKH DPRFSATILT VSMPQRPLMN TYVQARASSA
     ANIKLLQLPI VDPPAPEQYQ TLVGFLSLHM QNHKHHVKHA LLNLMKTTES NSSNSVRLAA
     IFVDMFSTTL IDVAAELAVP CYLFFASPAS CLGFTLDLPR FDLAESKSEF TVPCFKNLLP
     RSVFPNLVLD AKDGTFWLSY HARRYKETKG IVINTLQELE THALQSLHND SQLQRVYPIG
     PILDLVGSAQ WDPNPAQYKR IMEWLDQQPL SSVVLLCFGS MGSLEANQVE EIAIGLERAG
     VRFLWALRES PKAQLEYPRD YENHKDVLPD GFLERTNNIG LVCGWVPQAV VLAHKAVGGF
     VSHCGWNSIL ESLWHGVPVA TWPLYSEQQM NAFQMVRDLG LAVEISVDYR VGADLVRAEE
     VENGLRSLMK GGDEIRRKVK EMSDTCRGAL LENGSSYSNL VSLIQELTS