ID   U76E1_SOLLC             Reviewed;         475 AA.
AC   K4D3V7;
DT   07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2012, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=UDP-glycosyltransferase 76E1 {ECO:0000303|PubMed:28482127};
DE            Short=SlUGT76E1 {ECO:0000303|PubMed:28482127};
DE            EC=2.4.1.263 {ECO:0000269|PubMed:28482127};
GN   Name=UGT76E1 {ECO:0000303|PubMed:28482127};
GN   OrderedLocusNames=Solyc10g085230.1.1 {ECO:0000305};
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Heinz 1706;
RX   PubMed=22660326; DOI=10.1038/nature11119;
RG   Tomato Genome Consortium;
RT   "The tomato genome sequence provides insights into fleshy fruit
RT   evolution.";
RL   Nature 485:635-641(2012).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DEVELOPMENTAL
RP   STAGE, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. MicroTom;
RX   PubMed=28482127; DOI=10.1111/tpj.13588;
RA   Sun Y., Ji K., Liang B., Du Y., Jiang L., Wang J., Kai W., Zhang Y.,
RA   Zhai X., Chen P., Wang H., Leng P.;
RT   "Suppressing ABA uridine diphosphate glucosyltransferase (SlUGT75C1) alters
RT   fruit ripening and the stress response in tomato.";
RL   Plant J. 91:574-589(2017).
CC   -!- FUNCTION: Glucosyltransferase acting on abscisic acid (ABA) but not on
CC       auxin (IAA). {ECO:0000269|PubMed:28482127}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-cis-(+)-abscisate + UDP-alpha-D-glucose = beta-D-
CC         glucopyranosyl cis-(+)-abscisate + UDP; Xref=Rhea:RHEA:31031,
CC         ChEBI:CHEBI:22151, ChEBI:CHEBI:37569, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58885; EC=2.4.1.263;
CC         Evidence={ECO:0000269|PubMed:28482127};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.2 mM for abscisic acid {ECO:0000269|PubMed:28482127};
CC         Vmax=0.007 umol/min/ug enzyme with abscisic acid as substrate (in the
CC         presence of UDP-glucose) {ECO:0000269|PubMed:28482127};
CC       pH dependence:
CC         Optimum pH is 3.87-7. {ECO:0000269|PubMed:28482127};
CC       Temperature dependence:
CC         Optimum temperature is 37 degrees Celsius.
CC         {ECO:0000269|PubMed:28482127};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28482127}. Nucleus
CC       {ECO:0000269|PubMed:28482127}.
CC   -!- TISSUE SPECIFICITY: Expressed in flowers and fruits.
CC       {ECO:0000269|PubMed:28482127}.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed during fruit ripening and flower
CC       development. {ECO:0000269|PubMed:28482127}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; CM001073; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004249656.1; XM_004249608.2.
DR   RefSeq; XP_019071658.1; XM_019216113.1.
DR   AlphaFoldDB; K4D3V7; -.
DR   SMR; K4D3V7; -.
DR   PaxDb; K4D3V7; -.
DR   PRIDE; K4D3V7; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   HOGENOM; CLU_001724_0_0_1; -.
DR   InParanoid; K4D3V7; -.
DR   OrthoDB; 508327at2759; -.
DR   PhylomeDB; K4D3V7; -.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; K4D3V7; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0010294; F:abscisic acid glucosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0080043; F:quercetin 3-O-glucosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0080044; F:quercetin 7-O-glucosyltransferase activity; IBA:GO_Central.
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   Cytoplasm; Glycosyltransferase; Nucleus; Reference proteome; Transferase.
FT   CHAIN           1..475
FT                   /note="UDP-glycosyltransferase 76E1"
FT                   /id="PRO_0000445699"
FT   BINDING         270
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         328..329
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         346..354
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         368..371
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
SQ   SEQUENCE   475 AA;  53527 MW;  CAF9B92237E54B77 CRC64;
     MKIERKQSVV LVPHPYQGHL TPMLQLGSIL HSQGFSVIVA HTQYNTPNYS NHPQFVFHSM
     DDGLQGIDMS FPSLENIYDM NENCKAPLRN YLVSMMEEEG DQLACIVYDN VMFFVDDVAT
     QLKLPSIVLR TFSAAYLHSM ITILQQPEIY LPFEDSQLLD PLPELHPLRF KDVPFPIINN
     TVPEPILDFC RAMSDIGSSV ATIWNTMQDL ESSMLLRLQE HYKVPFFPIG PVHKMASLVS
     STSILEEDNS CIEWLDRQAP NSVLYVSLGS LVRIDHKELI ETAWGLANSD QPFLWVIRPG
     SVSGFQCAEA LPDGFEKMVG ERGRIVKWAP QKQVLAHPAV AGFFTHCGWN STLESICEEV
     PMVCRPFLAD QLVNARYLSQ IYKVGFELEV IERTVIEKTI RKLMLSEEGK DVKKRVADMK
     QKIVAGMQID CTSHKNLNDL VDFISALPSR LAPPTPVFGA IMSSNHIASK CIIES