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U70G2_CROXC
ID   U70G2_CROXC             Reviewed;         470 AA.
AC   A0A2Z5CV93;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2018, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=Myricetin 3-O-rhamnoside 1,2-glucosyltransferase UGT709G2;
DE            EC=2.4.1.- {ECO:0000269|PubMed:29967287};
DE   AltName: Full=UDP-glucosyltransferase 2 {ECO:0000303|PubMed:31004005};
DE            Short=CcUGT2 {ECO:0000303|PubMed:31004005};
GN   Name=UGT709G2 {ECO:0000303|PubMed:29967287};
GN   Synonyms=UGT2 {ECO:0000303|PubMed:31004005};
OS   Crocosmia x crocosmiiflora (Montbretia) (Crocosmia aurea x Crocosmia
OS   pottsii).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Iridaceae;
OC   Crocoideae; Freesieae; Crocosmia.
OX   NCBI_TaxID=1053288;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=29967287; DOI=10.1105/tpc.18.00406;
RA   Irmisch S., Jo S., Roach C.R., Jancsik S., Man Saint Yuen M., Madilao L.L.,
RA   O'Neil-Johnson M., Williams R., Withers S.G., Bohlmann J.;
RT   "Discovery of UDP-glycosyltransferases and BAHD-acyltransferases involved
RT   in the biosynthesis of the antidiabetic plant metabolite montbretin A.";
RL   Plant Cell 30:1864-1886(2018).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=31004005; DOI=10.1104/pp.19.00254;
RA   Irmisch S., Ruebsam H., Jancsik S., Man Saint Yuen M., Madilao L.L.,
RA   Bohlmann J.;
RT   "Flavonol biosynthesis genes and their use in engineering the plant
RT   antidiabetic metabolite montbretin A.";
RL   Plant Physiol. 180:1277-1290(2019).
CC   -!- FUNCTION: Glucosyltransferase involved in montbretin A (MbA)
CC       biosynthesis (PubMed:29967287, PubMed:31004005). Catalyzes the
CC       glucosylation of myricetin 3-O-alpha-L-rhamnoside (MR) to produce
CC       myricetin 3-O-[beta-D-glucosyl-(1->2)-alpha-L-rhamnoside] (MRG), a
CC       precursor of MbA (PubMed:29967287, PubMed:31004005). MbA is a potent
CC       inhibitor of human pancreatic alpha-amylase and is being developed as
CC       drug candidate to treat type-2 diabetes (PubMed:29967287,
CC       PubMed:31004005). In vitro, is able to transfer UDP-xylose with 50-fold
CC       less efficiency compared with UDP-glucose (PubMed:29967287). In vitro,
CC       can use myricetin 3-O-glucoside and quercetin 3-O-glucoside as
CC       substrates, although these two flavonoids may not be physiological
CC       substrates in vivo (PubMed:29967287). {ECO:0000269|PubMed:29967287,
CC       ECO:0000269|PubMed:31004005}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=myricetin 3-O-alpha-L-rhamnoside + UDP-alpha-D-glucose = H(+)
CC         + myricetin 3-O-[beta-D-glucosyl-(1->2)-alpha-L-rhamnoside] + UDP;
CC         Xref=Rhea:RHEA:61148, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58885, ChEBI:CHEBI:144429, ChEBI:CHEBI:144432;
CC         Evidence={ECO:0000269|PubMed:29967287, ECO:0000269|PubMed:31004005};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61149;
CC         Evidence={ECO:0000269|PubMed:29967287, ECO:0000269|PubMed:31004005};
CC   -!- PATHWAY: Flavonoid metabolism. {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in young cromes.
CC       {ECO:0000269|PubMed:29967287}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; MG938543; AXB26716.1; -; mRNA.
DR   AlphaFoldDB; A0A2Z5CV93; -.
DR   SMR; A0A2Z5CV93; -.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
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..470
FT                   /note="Myricetin 3-O-rhamnoside 1,2-glucosyltransferase
FT                   UGT709G2"
FT                   /id="PRO_0000448218"
FT   BINDING         20
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XT97"
FT   BINDING         287
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XT97"
FT   BINDING         357..365
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XT97"
FT   BINDING         381..382
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XT97"
SQ   SEQUENCE   470 AA;  52699 MW;  B3C89BA4DA474CBC CRC64;
     MAEKEAKHHV VLFPLPGQGH IGSMLKLAQL LSTAGFYITF VHTERNYRRF LLTSTSFNVP
     KFRFRTIPDG FPDNDPRSPL PFIELQESLD TKCKGYYREV LVAVDEEWPP VTCVVADTAL
     PLALEVPEEL GIPVMILAPH SAGSILTGYS IPQLIQGGEF PFPEDADMDE LLQGVLGLEG
     IVRRRDMSVR GFKSIDSPFV RFEVKMNQNL SRGRALILNT TESMDSLALR HIRSICPTTY
     TLGPFHVLLR NIKDQSHSAS LSEEDRSCIA WLDTKPNKSV VYVSFGSLAA MSREAFLEFQ
     QGLLDSGYHF LWVIRPDMVE GGLEECELTA SERRYFVKWA PQEEVLAHPA VGCFLTHSGW
     NSTLESIYAG VPMICWPFFA DQLINSRFVS EVWKIALDMK DLCGRSYVER MVKEVMSGEK
     GKELRKSICE MADMVKKSAE EGGSSYTNFK ELIGHIKSLS LPACSSTSGF
 
 
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