5GT_GENTR
ID 5GT_GENTR Reviewed; 504 AA.
AC B2NID7;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Anthocyanidin 3-O-glucoside 5-O-glucosyltransferase;
DE EC=2.4.1.298;
DE AltName: Full=Anthocyanin 5-O-glucosyltransferase;
DE Short=Gt5GT7;
GN Name=5GT7;
OS Gentiana triflora (Clustered gentian).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Gentianaceae; Gentianeae; Gentianinae;
OC Gentiana.
OX NCBI_TaxID=55190;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=18375606; DOI=10.1093/jxb/ern031;
RA Nakatsuka T., Sato K., Takahashi H., Yamamura S., Nishihara M.;
RT "Cloning and characterization of the UDP-glucose:anthocyanin 5-O-
RT glucosyltransferase gene from blue-flowered gentian.";
RL J. Exp. Bot. 59:1241-1252(2008).
CC -!- FUNCTION: Catalyzes the glucosylation at the O-5 position of
CC anthocyanidin 3-glucosides to form anthocyanidin 3,5-di-O-glucosides
CC using UDP-glucose as sugar donor. Anthocyanidin 3,5-di-O-glucosides are
CC molecules that are responsible for pigmentation. Involved in
CC biosynsthesis of accumulate gentiodelphin, a unique polyacylated
CC delphinidin-type anthocyanin, in the petals. Also acts on anthocyanidin
CC 3-O-(6-O-malonylglucoside). Much less active with
CC hydroxycinnamoylglucose derivatives. No activity in the absence of the
CC 3-O-glucoside group. {ECO:0000269|PubMed:18375606}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an anthocyanidin 3-O-beta-D-glucoside + UDP-alpha-D-glucose =
CC an anthocyanidin 3,5-di-O-beta-D-glucoside + 2 H(+) + UDP;
CC Xref=Rhea:RHEA:35423, ChEBI:CHEBI:15378, ChEBI:CHEBI:16307,
CC ChEBI:CHEBI:57503, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885;
CC EC=2.4.1.298; Evidence={ECO:0000269|PubMed:18375606};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=29.5 mM for delphinidin 3-glucoside {ECO:0000269|PubMed:18375606};
CC KM=20.9 mM for cyanidin 3-glucoside {ECO:0000269|PubMed:18375606};
CC KM=12.2 mM for pelargonidin 3-glucoside
CC {ECO:0000269|PubMed:18375606};
CC KM=3.4 mM for malvidin 3-glucoside {ECO:0000269|PubMed:18375606};
CC Vmax=1.49 nmol/min/mg enzyme with delphinidin 3-glucoside as
CC substrate {ECO:0000269|PubMed:18375606};
CC Vmax=0.98 nmol/min/mg enzyme with cyanidin 3-glucoside as substrate
CC {ECO:0000269|PubMed:18375606};
CC Vmax=0.68 nmol/min/mg enzyme with pelargonidin 3-glucoside as
CC substrate {ECO:0000269|PubMed:18375606};
CC Vmax=0.52 nmol/min/mg enzyme with malvidin 3-glucoside as substrate
CC {ECO:0000269|PubMed:18375606};
CC -!- PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis.
CC {ECO:0000269|PubMed:18375606}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in petals and weakly in
CC filaments. Not expressed in leaves, stems and other floral organs.
CC {ECO:0000269|PubMed:18375606}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB363839; BAG32255.1; -; mRNA.
DR AlphaFoldDB; B2NID7; -.
DR SMR; B2NID7; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR KEGG; ag:BAG32255; -.
DR BioCyc; MetaCyc:MON-18003; -.
DR BRENDA; 2.4.1.298; 2412.
DR UniPathway; UPA00009; -.
DR GO; GO:0016758; F:hexosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0102816; F:UDP-D-glucose:delphinidin 3-O-glucosyl-5-O-caffeoylglucoside -O-beta-D-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR GO; GO:0009718; P:anthocyanin-containing compound biosynthetic process; IDA:UniProtKB.
DR GO; GO:0043473; P:pigmentation; TAS: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..504
FT /note="Anthocyanidin 3-O-glucoside 5-O-glucosyltransferase"
FT /id="PRO_0000422563"
FT REGION 107..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 317
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 375..377
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 392..400
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 414..417
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
SQ SEQUENCE 504 AA; 55291 MW; 3D07F3888649CDD3 CRC64;
MVGRGKGKGR EHVLLVVFPA QGHISPALQL AFKIVAHSSI DLTFLTSSSA VASILIGLPP
TAPALNFAAF SQGNLHNDDD DDDDAKDYMH TLCKHGSQSV RDIIHSTKKG QGQGQGQGQG
QGQGQGHPIT RILYTTLLPW AADVAREFRL PSVLLWTQPV TTFLTFHYYF TGYEDAINKV
RNQQGTEDDS TIQLPRLPLL SSRDLHSFML PSNPFKGAIN TFKEHLEALD AEETPPTILV
NSYDALEEEA LQAMIPKYKT MGIGPLIPSS VFDTRETTCE VVSLVPDLAQ KSKDDCQWHG
WLNSKAEGSV IYVSFGSHVK QSKAQTEEIA KGLLASGHPF LWVITSNEEE EGDEIMEQNL
VEEIQEKGMM IVPWCAQFQV LKHPSVGCFM THCGWNSTLE SIACGVPMIG FPKMFDQPTI
SKLIAHVWKV GVRVNAAVDG IVGQEVIKNC IESVMDPDGI GRELNENVRK FMSLGKKAAE
EGGSSHNNFK AFLQDMTGGT TTIN
