ID   UGT2_PUEML              Reviewed;         472 AA.
AC   A0A172J2D0;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   07-SEP-2016, sequence version 1.
DT   03-AUG-2022, entry version 17.
DE   RecName: Full=UDP-glycosyltransferase 2 {ECO:0000303|PubMed:27066037};
DE            Short=PlUGT2 {ECO:0000303|PubMed:27066037};
DE            EC=2.4.1.- {ECO:0000269|PubMed:27066037};
DE   AltName: Full=UDP-glucose:isoflavone 4' 7-O-glucosyltransferase {ECO:0000312|EMBL:AMQ26112.1};
GN   Name=UGT2 {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:AMQ26112.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBSTRATE SPECIFICITY, AND TISSUE
RP   SPECIFICITY.
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).
CC   -!- FUNCTION: Glycosyltransferase that possesses isoflavonoids 4'-O- and 7-
CC       O-glucosyltransferase activities (PubMed:27066037). Shows a successive
CC       glucosylation toward the acceptors producing their corresponding 4',7-
CC       O-diglucosides (PubMed:27066037). Can use genistein, formononetin,
CC       daidzein, liquiritigenin and naringenin as substrates
CC       (PubMed:27066037). Shows also a 3'-O-glucosylation activity in vitro
CC       (PubMed:27066037). {ECO:0000269|PubMed:27066037}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in roots. Expressed in leaves and
CC       stems. {ECO:0000269|PubMed:27066037}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; KU311040; AMQ26112.1; -; mRNA.
DR   AlphaFoldDB; A0A172J2D0; -.
DR   SMR; A0A172J2D0; -.
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   2: Evidence at transcript level;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..472
FT                   /note="UDP-glycosyltransferase 2"
FT                   /id="PRO_0000439665"
FT   BINDING         283
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         348..349
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         366..374
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         388..391
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
SQ   SEQUENCE   472 AA;  51875 MW;  3968F1C7D9C4AF36 CRC64;
     MKDTIVLYPN IGRGHLVSMV ELGKLILTHH PSLSITILIL TPSTTPSTTT FACDSNAQYI
     ATVTATIPAI TFHHVPLATL PSNTPSLPPH LVSLELARHS TQNVAVAFQT LAKASNLKAI
     IIDLLNFNDP KTLTQNLNKN IHTYFYYTSG ASTLALLLHY PTIHETLTKN YVKDQPLQIQ
     IPGLRANITT DDFAKDSKDP SNYSSQAFLK IAETMRGSFG IIINTFEAIE EELIRALSED
     GTVPPLFCIG PVISAPYGED DKGCLSWLDS QPSQSVVLLC FGSMGSFSRT QLKEIAVGLE
     KSEQRFLWVV RAELDCADSV DEQPSLDELM PGGFLERTKE KGLVVRDWAP QVQILSHDSV
     GGFVTHCGWN SVLEAVCEGV PMAAWPLYAE QRVNRVIMVE DMKVALAVNE DKAGFVSATE
     LGDRVRELME SDKGKEIRQR TFKMKISAAE AMAEGGTSRV ALDKLAKLWK ES