ID DUSKY_IPONI Reviewed; 459 AA.
AC Q53UH4; Q53UH2; Q53UH3;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Anthocyanidin 3-O-glucoside 2''-O-glucosyltransferase;
DE EC=2.4.1.297;
DE AltName: Full=3-O-glucoside-2''-O-glucosyltransferase;
DE Short=In3GGT;
DE AltName: Full=Protein dusky;
DE Short=Dy;
GN Name=3GGT;
OS Ipomoea nil (Japanese morning glory) (Pharbitis nil).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX NCBI_TaxID=35883;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP PATHWAY, AND MUTAGENESIS OF 444-SER--GLY-459.
RC STRAIN=KK/ZSK-2;
RX PubMed=15842621; DOI=10.1111/j.1365-313x.2005.02383.x;
RA Morita Y., Hoshino A., Kikuchi Y., Okuhara H., Ono E., Tanaka Y., Fukui Y.,
RA Saito N., Nitasaka E., Noguchi H., Iida S.;
RT "Japanese morning glory dusky mutants displaying reddish-brown or purplish-
RT gray flowers are deficient in a novel glycosylation enzyme for anthocyanin
RT biosynthesis, UDP-glucose:anthocyanidin 3-O-glucoside-2''-O-
RT glucosyltransferase, due to 4-bp insertions in the gene.";
RL Plant J. 42:353-363(2005).
CC -!- FUNCTION: Glycosyltransferase that mediates the glucosylation of
CC anthocyanidin 3-O-glucosides to yield anthocyanidin 3-O-sophorosides.
CC 3-O-sophoroside derivatives are required for the bright blue or red
CC color of flowers. {ECO:0000269|PubMed:15842621}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an anthocyanidin 3-O-beta-D-glucoside + UDP-alpha-D-glucose =
CC an anthocyanidin 3-O-sophoroside + 2 H(+) + UDP;
CC Xref=Rhea:RHEA:35419, ChEBI:CHEBI:15378, ChEBI:CHEBI:16307,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:77946;
CC EC=2.4.1.297; Evidence={ECO:0000269|PubMed:15842621};
CC -!- PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis.
CC {ECO:0000269|PubMed:15842621}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in the petals and tubes of flower
CC buds at around 24 hours before flower opening.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB192314; BAD95881.1; -; mRNA.
DR EMBL; AB192316; BAD95883.1; -; Genomic_DNA.
DR EMBL; AB192317; BAD95884.1; -; Genomic_DNA.
DR EMBL; AB192318; BAD95885.1; -; Genomic_DNA.
DR RefSeq; XP_019194233.1; XM_019338688.1.
DR AlphaFoldDB; Q53UH4; -.
DR SMR; Q53UH4; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GeneID; 109188143; -.
DR KEGG; ag:BAD95881; -.
DR KEGG; ini:109188143; -.
DR OrthoDB; 1213612at2759; -.
DR UniPathway; UPA00009; -.
DR GO; GO:0102455; F:anthocyanidin 3-O-glucoside 2''-O-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016758; F:hexosyltransferase activity; IDA:UniProtKB.
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; IDA:UniProtKB.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR002213; UDP_glucos_trans.
DR PANTHER; PTHR48049; GLYCOSYLTRANSFERASE; 1.
DR PANTHER; PTHR48049:SF34; UDP-GLYCOSYLTRANSFERASE 79B30; 1.
DR Pfam; PF00201; UDPGT; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Transferase.
FT CHAIN 1..459
FT /note="Anthocyanidin 3-O-glucoside 2''-O-
FT glucosyltransferase"
FT /id="PRO_0000422561"
FT ACT_SITE 20
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT ACT_SITE 117
FT /note="Charge relay"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 20
FT /ligand="an anthocyanidin"
FT /ligand_id="ChEBI:CHEBI:143576"
FT /evidence="ECO:0000250|UniProtKB:P51094"
FT BINDING 138
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 335
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 337
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 352
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 355
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 357
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 360
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 375
FT /ligand="an anthocyanidin"
FT /ligand_id="ChEBI:CHEBI:143576"
FT /evidence="ECO:0000250|UniProtKB:P51094"
FT BINDING 376
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 377
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT MUTAGEN 444..459
FT /note="SKYMDSFNQKLQDLLG->GFKVHGLFQSETAGSPWMNII: In dy-1;
FT reddish-brown or purplish-gray petals phenotype due to
FT accumulation of anthocyanidin 3-O-glucoside derivatives."
FT /evidence="ECO:0000269|PubMed:15842621"
FT MUTAGEN 444..459
FT /note="SKYMDSFNQKLQDLLG->RFKVHGLFQSETAGSPWMNII: In dy-2;
FT reddish-brown or purplish-gray petals phenotype due to
FT accumulation of anthocyanidin 3-O-glucoside derivatives."
FT /evidence="ECO:0000269|PubMed:15842621"
SQ SEQUENCE 459 AA; 51170 MW; 8F9BE029B37004EA CRC64;
MGSQATTYHM AMYPWFGVGH LTGFFRLANK LAGKGHRISF LIPKNTQSKL ESFNLHPHLI
SFVPIVVPSI PGLPPGAETT SDVPFPSTHL LMEAMDKTQN DIEIILKDLK VDVVFYDFTH
WLPSLARKIG IKSVFYSTIS PLMHGYALSP ERRVVGKQLT EADMMKAPAS FPDPSIKLHA
HEARGFTART VMKFGGDITF FDRIFTAVSE SDGLAYSTCR EIEGQFCDYI ETQFQKPVLL
AGPALPVPSK STMEQKWSDW LGKFKEGSVI YCAFGSECTL RKDKFQELLW GLELTGMPFF
AALKPPFEAE SIEAAIPEEL KEKIQGRGIV HGEWVQQQLF LQHPSVGCFV SHCGWASLSE
ALVNDCQIVL LPQVGDQIIN ARIMSVSLKV GVEVEKGEED GVFSRESVCK AVKAVMDEKS
EIGREVRGNH DKLRGFLLNA DLDSKYMDSF NQKLQDLLG
//
