ID   UGT2_GARJA              Reviewed;         481 AA.
AC   F8WKW1;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=7-deoxyloganetin glucosyltransferase;
DE            EC=2.4.1.324;
DE   AltName: Full=Genipin glucosyltransferase;
DE   AltName: Full=UDP-glucose glucosyltransferase 2;
DE            Short=GjUGT2;
DE   AltName: Full=UDP-glycosyltransferase 85A24;
GN   Name=UGT85A24; Synonyms=UGT2;
OS   Gardenia jasminoides (Cape jasmine) (Gardenia augusta).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Rubiaceae; Ixoroideae; Gardenieae complex;
OC   Gardenieae - Pavetteae clade; Gardenieae; Gardenia.
OX   NCBI_TaxID=114476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION BY METHYL JASMONATE, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=21799001; DOI=10.1074/jbc.m111.242586;
RA   Nagatoshi M., Terasaka K., Nagatsu A., Mizukami H.;
RT   "Iridoid-specific Glucosyltransferase from Gardenia jasminoides.";
RL   J. Biol. Chem. 286:32866-32874(2011).
CC   -!- FUNCTION: Iridoid glucosyltransferase acting on genipin and 7-
CC       deoxyloganetin. No activity with 7-deoxyloganetic acid. Involved in
CC       geniposide biosynthesis. {ECO:0000269|PubMed:21799001}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-deoxyloganetin + UDP-alpha-D-glucose = 7-deoxyloganin + H(+)
CC         + UDP; Xref=Rhea:RHEA:39899, ChEBI:CHEBI:15378, ChEBI:CHEBI:18370,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:76849;
CC         EC=2.4.1.324; Evidence={ECO:0000269|PubMed:21799001};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=8.82 mM for genipin {ECO:0000269|PubMed:21799001};
CC         KM=0.61 mM for 7-deoxyloganetin {ECO:0000269|PubMed:21799001};
CC         KM=0.17 mM for UPD-glucose {ECO:0000269|PubMed:21799001};
CC         Note=kcat is 1.04 sec(-1) for genipin. kcat is 0.13 sec(-1) for 7-
CC         deoxyloganetin. kcat is 0.16 sec(-1) for UPD-glucose.;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Very low expression in stems.
CC       {ECO:0000269|PubMed:21799001}.
CC   -!- DEVELOPMENTAL STAGE: Up-regulated during the early stage of fruit
CC       ripening. {ECO:0000269|PubMed:21799001}.
CC   -!- INDUCTION: Up-regulated by methyl jasmonate.
CC       {ECO:0000269|PubMed:21799001}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AB555732; BAK55737.1; -; mRNA.
DR   AlphaFoldDB; F8WKW1; -.
DR   SMR; F8WKW1; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   KEGG; ag:BAK55737; -.
DR   GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:UniProtKB.
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..481
FT                   /note="7-deoxyloganetin glucosyltransferase"
FT                   /id="PRO_0000430137"
FT   BINDING         304
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         361..363
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         378..386
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         400..403
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   481 AA;  53592 MW;  61C282149CC9F355 CRC64;
     MGSISLPEKH HAVCIPYPAQ GHINPMLKLA KILHHKGFHI TFVNTEFNHK RLLKSRGPDA
     LNGLPDFQFK TIPDGLPPSD VDATQDIPSL CESTTTRCLD PFRNLLAELN GPSSSQVPPV
     SCIVSDGVMS FTLEAAAELG VPEILFWTTS ACGFLGYMHY AKLIEKGLTP LKDASYLSNG
     YLEQSLDWIP GMKDIRLKDL PSFLRTTNPD DYMVKFVLQE TERAKKASAI ILNTFQELED
     DVINALSAIL PPIYTIGPLQ FLQKEVKDER LSVLGSNLWK EEPECLDWLD SKDPNSVVYV
     NFGSITVMTP GQLVEFAWGL ANSKQTFLWI IRPDLVSGDS AILPPEFLEE TKDRGLLASW
     CPQEQVLSHP AIGGFLTHSG WNSTLESICS GVPMICWPFF AEQQTNCWFC CTKWYNGLEI
     DNNVKRDEVE SLVTELMVGE KGMDMKKKAL EWKNKAEEAA KSSGGSSYSN LEKVVQVLLS
     K