ID   IH5GT_IRIHO             Reviewed;         463 AA.
AC   Q767C8;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Cyanidin 3-O-rutinoside 5-O-glucosyltransferase;
DE            Short=Ih5GT;
DE            EC=2.4.1.116;
DE   AltName: Full=Anthocyanin 5-O-glucosyltransferase;
DE   AltName: Full=Cyanidin-3-rhamnosylglucoside 5-O-glucosyltransferase;
DE   AltName: Full=Uridine diphosphoglucose-cyanidin 3-rhamnosylglucoside 5-O-glucosyltransferase;
GN   Name=5GT;
OS   Iris hollandica (Dutch iris) (Iris tingitana x Iris xiphium).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Iridaceae;
OC   Iridoideae; Irideae; Iris.
OX   NCBI_TaxID=35876;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   TISSUE=Perianth;
RX   AGRICOLA=IND43654143;
RA   Imayama T., Yoshihara N., Fukuchi-Mizutani M., Tanaka Y., Ino I.,
RA   Yabuya T.;
RT   "Isolation and characterization of a cDNA clone of UDP-glucose: anthocyanin
RT   5-O-glucosyltransferase in Iris hollandica.";
RL   Plant Sci. 167:1243-1248(2004).
CC   -!- FUNCTION: Catalyzes the transfer of the glucosyl moiety from UDP-
CC       glucose to the 5-hydroxyl group of anthocyanin. Anthocyanins are
CC       ubiquitous colored pigments that are responsible for variations in
CC       petal color. Also acts on the 3-O-rutinosides of pelargonidin,
CC       delphinidin and malvidin, but not the corresponding glucosides or 6-
CC       acylglucosides. Does not catalyze the glucosylation of the 5-hydroxy
CC       group of cyanidin 3-glucoside. {ECO:0000269|Ref.1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cyanidin 3-O-rutinoside + UDP-alpha-D-glucose = cyanidin 3-O-
CC         rutinoside 5-O-beta-D-glucoside + H(+) + UDP; Xref=Rhea:RHEA:12144,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57830, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58546, ChEBI:CHEBI:58885; EC=2.4.1.116;
CC         Evidence={ECO:0000269|Ref.1};
CC   -!- PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AB113664; BAD06874.1; -; mRNA.
DR   AlphaFoldDB; Q767C8; -.
DR   SMR; Q767C8; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   KEGG; ag:BAD06874; -.
DR   UniPathway; UPA00009; -.
DR   GO; GO:0047214; F:cyanidin-3-rhamnosylglucoside 5-O-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009718; P:anthocyanin-containing compound biosynthetic process; IEA:UniProtKB-UniPathway.
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..463
FT                   /note="Cyanidin 3-O-rutinoside 5-O-glucosyltransferase"
FT                   /id="PRO_0000422567"
FT   BINDING         297
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         343..345
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         360..368
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         382..385
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   463 AA;  50129 MW;  B43260E8D6DEA99F CRC64;
     MAKQHFLVIT IGAQGHINPA RRLAARLIEA GGARVTLTVP ILAYRRMFPS AAAELEPREE
     KDDGLLTYMP YSDGVEDGLD PAANPAEFKR RIAESLRCIA AGFVARGRPI TCIVYALLLS
     MAAAVARDLG VPSVLFWIQS ATSFAVNYHY FAGGYDKLFS EAAADPSFLV ELPGLPAFRR
     KDLPTLLTGP RPEGTFYSFL HTLYGEVFET LRREVSAGEE KPRVILNTFR ALEEDVVAGF
     EASIDMVTVG PLVPPSLIMT SPEETATNDL YEHDTSNYME WLDGKEEGSV VYVSFGSYAT
     LKEEEREEVK KGLSASGRPY IWAMAKGGSG DDGGGLGVKV EWCEQARVLS HRSVGCFVTH
     CGWNSVAEAM ACGVPMVMLP QWTDQVTNAK LAEEEWGVGV RAEAVAGEEL RRCLDVVMGG
     GEADDGGIVM RRRAKAWSEK AREAAGDGGS SARNLAAFVV GGN