ID   UGT1_PUEML              Reviewed;         471 AA.
AC   A0A067YB04;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2014, sequence version 1.
DT   03-AUG-2022, entry version 21.
DE   RecName: Full=UDP-glycosyltransferase 1 {ECO:0000303|PubMed:24700248};
DE            Short=PlUGT1 {ECO:0000303|PubMed:24700248};
DE            EC=2.4.1.170 {ECO:0000269|PubMed:24700248};
DE   AltName: Full=Glycosyltransferase UGT88E12 {ECO:0000303|PubMed:24700248};
DE   AltName: Full=UDP-glucose:isoflavone 7-O-glucosyltransferase KGT1 {ECO:0000312|EMBL:AGZ84545.1};
GN   Name=UGT1 {ECO:0000303|PubMed:24700248};
GN   Synonyms=UGT88E12 {ECO:0000303|PubMed:24700248};
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:AGZ84545.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP   SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION BY METHYL JASMONATE,
RP   AND TISSUE SPECIFICITY.
RX   PubMed=24700248; DOI=10.1007/s00299-014-1606-7;
RA   Li J., Li Z., Li C., Gou J., Zhang Y.;
RT   "Molecular cloning and characterization of an isoflavone 7-O-
RT   glucosyltransferase from Pueraria lobata.";
RL   Plant Cell Rep. 33:1173-1185(2014).
CC   -!- FUNCTION: Isoflavone 7-O-glucosyltransferase converting daidzein to
CC       daidzin, genistein to genistin and formononetin to ononin
CC       (PubMed:24700248). Shows some activity toward the chalcone
CC       isoliquiritigenin, the flavanones liquiritigenin and naringenin, and
CC       the flavone apigenin, but not toward cyanidin, luteolin, kaempferol,
CC       quercetin, daidzin and puerarin (PubMed:24700248).
CC       {ECO:0000269|PubMed:24700248}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 7-hydroxyisoflavone + UDP-alpha-D-glucose = a 7-
CC         hydroxyisoflavone 7-O-beta-D-glucoside + H(+) + UDP;
CC         Xref=Rhea:RHEA:56344, ChEBI:CHEBI:15378, ChEBI:CHEBI:55465,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:140301;
CC         EC=2.4.1.170; Evidence={ECO:0000269|PubMed:24700248};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=20.4 uM for genistein {ECO:0000269|PubMed:24700248};
CC         KM=29.9 uM for daidzein {ECO:0000269|PubMed:24700248};
CC         Note=kcat is 1.1 sec(-1) with daidzein as substrate. kcat is 1.1
CC         sec(-1) with genistein as substrate. {ECO:0000269|PubMed:24700248};
CC   -!- TISSUE SPECIFICITY: Expressed in roots. Detected in stems and leaves.
CC       {ECO:0000269|PubMed:24700248}.
CC   -!- INDUCTION: Up-regulated by methyl jasmonate.
CC       {ECO:0000269|PubMed:24700248}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; KC473565; AGZ84545.1; -; mRNA.
DR   AlphaFoldDB; A0A067YB04; -.
DR   SMR; A0A067YB04; -.
DR   GO; GO:0050004; F:isoflavone 7-O-glucosyltransferase activity; IEA:UniProtKB-EC.
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..471
FT                   /note="UDP-glycosyltransferase 1"
FT                   /id="PRO_0000439664"
FT   BINDING         283
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         347..348
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         365..373
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         387..390
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
SQ   SEQUENCE   471 AA;  52195 MW;  B8E2F249BAEAC10F CRC64;
     MKDSIVLYSA LGRGHLVSMV ELGKLILSHH PSLSITILFL TPPPNQDTPT SPTAFTCDAT
     AKYIAAVTAA TPSITFHRIP QISIPTVLPP MALTFELCRA TGHHLRRILT SISQTSNLKA
     IVLDFMNYSA ARVTNTLQIP TYFYYTSGAS TLAVLFQQII IHQNNTKSIK DLNMHLLIPG
     LPKIHTDDMP EQVQDRENEG YEVFIDIATC MRDSDGVIVN TFEAMEGRVM EAFNEGLMEG
     PTPPLFCIGP VISSAPCRVD DDGCLSWLDS QPSHSVVFLS FGSMGRFSRT QLREIAIGLE
     KSEQRFLWVV RSEFEEGDSV EPPSLDELLP EGFLERTKGK GMVLRDWAPQ AAILSHDSVG
     GFVTHCGWNS VLEAVCEGVP MVAWPLYAEQ KLNKVILVEE MKVGLAVKQN KDGLVSSTEL
     GDRVRELMDS DRGKEIRQKI FKMKMSANEA MAKGGSSIMA LNRLVEVWRE H