ID   UGT7_CATRO              Reviewed;         454 AA.
AC   U3UA11;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   11-DEC-2013, sequence version 1.
DT   03-AUG-2022, entry version 17.
DE   RecName: Full=UDP-glucose iridoid glucosyltransferase;
DE            EC=2.4.1.-;
DE   AltName: Full=UDP-glucose glucosyltransferase 7;
DE            Short=CrUGT7;
DE   AltName: Full=UDP-glycosyltransferase 76A2;
GN   Name=UGT76A2; Synonyms=UGT7;
OS   Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC   Catharanthinae; Catharanthus.
OX   NCBI_TaxID=4058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX   PubMed=24104568; DOI=10.1105/tpc.113.115154;
RA   Asada K., Salim V., Masada-Atsumi S., Edmunds E., Nagatoshi M.,
RA   Terasaka K., Mizukami H., De Luca V.;
RT   "A 7-deoxyloganetic Acid glucosyltransferase contributes a key step in
RT   secologanin biosynthesis in madagascar periwinkle.";
RL   Plant Cell 25:4123-4134(2013).
CC   -!- FUNCTION: Iridoid glucosyltransferase acting on a broad range of
CC       substrates, including both 7-deoxyloganetic acid and 7-deoxyloganetin,
CC       curcumin, genistein, luteolin and kaempferol.
CC       {ECO:0000269|PubMed:24104568}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.99 mM for 7-deoxyloganetin {ECO:0000269|PubMed:24104568};
CC         KM=0.120 mM for UPD-glucose {ECO:0000269|PubMed:24104568};
CC         Note=kcat is 0.00493 sec(-1) for 7-deoxyloganetin. kcat is 0.00512
CC         sec(-1) for UPD-glucose.;
CC   -!- TISSUE SPECIFICITY: Expressed in leaves. Low levels of expression in
CC       roots. {ECO:0000269|PubMed:24104568}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AB733666; BAO01108.1; -; mRNA.
DR   AlphaFoldDB; U3UA11; -.
DR   SMR; U3UA11; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:1900994; P:(-)-secologanin biosynthetic process; IDA:UniProtKB.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   Pfam; PF00201; UDPGT; 1.
PE   1: Evidence at protein level;
KW   Transferase.
FT   CHAIN           1..454
FT                   /note="UDP-glucose iridoid glucosyltransferase"
FT                   /id="PRO_0000430134"
FT   BINDING         274
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         350..358
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         372..375
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   454 AA;  50976 MW;  314C3681547C2E97 CRC64;
     MGSVSAKKGV IVLVPYCLQG HMTPMLQLAS ILHSKGFSII VAHTKFSSPN PSDHPEFIFH
     ALPDKLNGFD TSFMNLLNVM EAINSSCGGP LVDYLVEIMK DKGQVISCII HDAIMYFAEA
     VASQLNLPSM VLRTSNVAFM ESHRDILRLH SENRFPLPDS ELENPVPGLD PLRFKDLPVS
     VSSRIHDKII EFFESYMNIR SNAAIIWNTT QVLEKYALNK LHHHYKVPSF AVGPFHKMVP
     ASSSATSYIN EDRGCIEWLD KQAPNSVLYM SLGSLSTIDE KELEETAWGL ANSDQPFLWV
     IRPSSVNGSG WIEHLPEGFQ EMVGDRGLLV KWAPQKEVLA HPAVGGFWSH CGWNSTLESI
     CEAVPMICRP CFSDQIVNSR YITHVWKVGL ELEQPSDRRV VEKTIRRLMV ADSEEKEMRQ
     RMLDLKTQIE SSVQKGGSSY NSLNDLVKFI ASFP