ID   UGT13_PUEML             Reviewed;         451 AA.
AC   A0A067YBQ3;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2014, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=UDP-glycosyltransferase 13 {ECO:0000303|PubMed:24700248};
DE            Short=PlUGT13 {ECO:0000303|PubMed:24700248};
DE            EC=2.4.1.170 {ECO:0000269|PubMed:24700248};
DE   AltName: Full=Glycosyltransferase UGT88H1 {ECO:0000303|PubMed:24700248};
DE   AltName: Full=UDP-glucose:isoflavone 7-O-glucosyltransferase KGT13 {ECO:0000312|EMBL:AGZ84546.1};
GN   Name=UGT13 {ECO:0000303|PubMed:24700248};
GN   Synonyms=UGT88H1 {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:AGZ84546.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP   SPECIFICITY, INDUCTION BY METHYL JASMONATE, 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 flavanones
CC       liquiritigenin and naringenin, but not toward cyanidin,
CC       isoliquiritigenin, apigenin, luteolin, kaempferol, quercetin, daidzin
CC       and puerarin (PubMed:24700248). {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   -!- TISSUE SPECIFICITY: Expressed in roots. Detected in stems and leaves.
CC       {ECO:0000269|PubMed:24700248}.
CC   -!- INDUCTION: Down-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; KC473566; AGZ84546.1; -; mRNA.
DR   AlphaFoldDB; A0A067YBQ3; -.
DR   SMR; A0A067YBQ3; -.
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..451
FT                   /note="UDP-glycosyltransferase 13"
FT                   /id="PRO_0000439666"
FT   BINDING         265
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         325..326
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         343..351
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         365..368
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
SQ   SEQUENCE   451 AA;  50258 MW;  F0C0BFCAF3B67FD0 CRC64;
     MKGTIVLYPA MGRGHIVPMV ELGKFLSTHH HATLSVKILL PSPPNSTTLR YITAVSAATP
     SITFLHLSPS QHLLRVLQTL ISQSSKPKAF ILDFFNHSAA DVTQTLNIPT YYYFPNAASC
     VALMLYTPTI HHNTKNGNSS YNDTLRRIPG LPPLSPEDMP APLLDRRSFE SFANMSIQMR
     KSDGIIVNTF EKLENKAFLA LKNGTCVSET SRSHSSTPET RKPRIFCVGP LVSNGGGEHD
     NDDSGCMSWL DLQPSRTVVF LSFGSYGRFS KSQIREIALG LERSGQRFLW VVRDPYERSE
     LSLEELLPKG FLERTKERGM VVKNWAPQVK VLSHDSVGGF VTHCGWNSVL EAVSWGVPMV
     AWPLYAEQRL NRVVMVEEMK VALPLKEVDE DGFVRASELE ERVRELMDSE RGRGKEVRKR
     VLGATNDAVA ALSDGGSSRI ELNDLVGLWM Q