U71K3_FRAAN
ID U71K3_FRAAN Reviewed; 478 AA.
AC P0DO49;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 1.
DT 03-AUG-2022, entry version 2.
DE RecName: Full=UDP-glycosyltransferase 71K3 {ECO:0000303|PubMed:26859691};
DE EC=2.4.1.- {ECO:0000269|PubMed:26859691};
DE AltName: Full=Acylphloroglucinol glucosyltransferase {ECO:0000303|PubMed:26859691};
DE EC=2.4.1.358 {ECO:0000269|PubMed:26859691};
GN Name=UGT71K3 {ECO:0000303|PubMed:26859691};
OS Fragaria ananassa (Strawberry) (Fragaria chiloensis x Fragaria virginiana).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Rosoideae; Potentilleae; Fragariinae;
OC Fragaria.
OX NCBI_TaxID=3747;
RN [1]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=26859691; DOI=10.1111/tpj.13140;
RA Song C., Zhao S., Hong X., Liu J., Schulenburg K., Schwab W.;
RT "A UDP-glucosyltransferase functions in both acylphloroglucinol glucoside
RT and anthocyanin biosynthesis in strawberry (Fragaria x ananassa).";
RL Plant J. 85:730-742(2016).
CC -!- FUNCTION: Glycosyltransferase that catalyzes the glucosylation of
CC diverse hydroxycoumarins, naphthols, flavonoids, acylphloroglucinols,
CC and pelargonidin (PubMed:26859691). Involved in fruit ripening by
CC synthesizing acylphloroglucinol glucosides and anthocyanin
CC (PubMed:26859691). {ECO:0000269|PubMed:26859691}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-acylphloroglucinol + UDP-alpha-D-glucose = a 2-
CC acylphloroglucinol 1-O-beta-D-glucoside + UDP; Xref=Rhea:RHEA:56072,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:134386,
CC ChEBI:CHEBI:141060; EC=2.4.1.358;
CC Evidence={ECO:0000269|PubMed:26859691};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56073;
CC Evidence={ECO:0000269|PubMed:26859691};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=quercetin + UDP-alpha-D-glucose = H(+) + quercetin 3-O-beta-D-
CC glucoside + UDP; Xref=Rhea:RHEA:61180, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57694, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:144437; Evidence={ECO:0000269|PubMed:26859691};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61181;
CC Evidence={ECO:0000269|PubMed:26859691};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pelargonidin + UDP-alpha-D-glucose = pelargonidin 3-O-beta-D-
CC glucoside + UDP; Xref=Rhea:RHEA:61504, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:144777, ChEBI:CHEBI:144778;
CC Evidence={ECO:0000269|PubMed:26859691};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61505;
CC Evidence={ECO:0000269|PubMed:26859691};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=36 uM for 1-naphtol {ECO:0000269|PubMed:26859691};
CC KM=109 uM for kaempferol {ECO:0000269|PubMed:26859691};
CC KM=38 uM for quercetin {ECO:0000269|PubMed:26859691};
CC KM=284 uM for phloroglucinol {ECO:0000269|PubMed:26859691};
CC KM=24 uM for 2-acylphloroglucinol {ECO:0000269|PubMed:26859691};
CC KM=65 uM for pelargonidin {ECO:0000269|PubMed:26859691};
CC Vmax=0.61 nmol/sec/mg enzyme with 1-naphtol as substrate
CC {ECO:0000269|PubMed:26859691};
CC Vmax=2.45 nmol/sec/mg enzyme with kaempferol as substrate
CC {ECO:0000269|PubMed:26859691};
CC Vmax=0.82 nmol/sec/mg enzyme with quercetin as substrate
CC {ECO:0000269|PubMed:26859691};
CC Vmax=0.75 nmol/sec/mg enzyme with phloroglucinol as substrate
CC {ECO:0000269|PubMed:26859691};
CC Vmax=1.88 nmol/sec/mg enzyme with 2-acylphloroglucinol as substrate
CC {ECO:0000269|PubMed:26859691};
CC Vmax=1.44 nmol/sec/mg enzyme with pelargonidin as substrate
CC {ECO:0000269|PubMed:26859691};
CC -!- DISRUPTION PHENOTYPE: Loss of fruit pigmentation, and substantial
CC decrease of the levels of various acylphloroglucinol glucosides and an
CC anthocyanin. {ECO:0000269|PubMed:26859691}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009835; P:fruit ripening; IEA:UniProtKB-KW.
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.
PE 1: Evidence at protein level;
KW Fruit ripening; Glycosyltransferase; Transferase.
FT CHAIN 1..478
FT /note="UDP-glycosyltransferase 71K3"
FT /id="PRO_0000455390"
FT BINDING 281
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 478 AA; 52590 MW; FE7A2DDE2D6C4C4D CRC64;
MKKAELVFIP APGAGHLVSA LQFGKRLLQR DDRISITVLA IKSAAPSSLG SYTEALVASE
SRLQLIDVPQ AELPPLEFAK SPAKFFILNI ENHVPNVREA LTNYVSSKQD SVSIVGVVLD
FFCVSMIHVV NEFNLPSYLF MTSNAGYLSF EFHFPAQDSR TGRPPKDSDP DWLVPGIVPP
VPTKVLPVSL TDGSYYNYLG VASRFREAKG IIANTCVELE THAFNSFAED QTTPPVYPVG
PVLDLNDGQA RSNLNQAQRD KIISWLDDQP EESVVFLCFG SMGSFTEAQV KEIALGLEQS
GQRFLWSLRL TPPKGSKSLT PVDCSNLEEV LPDGFLERTR EKGLICGWAP QVDVLSHKAT
GGFVSHCGWN SILESLWHGV PIVTWPMYAE QQLNAFRLVK EMGLGLEMRL DYKRGGDEVV
KADEIGKAVA SVMENSEVRK KVKEIGVVCR KAVEDGGSSS VSLGRFIEDV LRNHFGSE
