UGAT_BELPE
ID UGAT_BELPE Reviewed; 438 AA.
AC Q5NTH0;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Cyanidin-3-O-glucoside 2-O-glucuronosyltransferase;
DE Short=BpUGAT;
DE EC=2.4.1.254;
DE AltName: Full=UDP-glucuronic acid:anthocyanin glucuronosyltransferase;
GN Name=UGAT; Synonyms=UGT94B1;
OS Bellis perennis (Daisy).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Astereae;
OC South American lineages; Bellidinae; Bellis.
OX NCBI_TaxID=41492;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 102-112; 384-393 AND
RP 417-426, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, SUBUNIT, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15509561; DOI=10.1074/jbc.m410537200;
RA Sawada S., Suzuki H., Ichimaida F., Yamaguchi M.A., Iwashita T., Fukui Y.,
RA Hemmi H., Nishino T., Nakayama T.;
RT "UDP-glucuronic acid:anthocyanin glucuronosyltransferase from red daisy
RT (Bellis perennis) flowers. Enzymology and phylogenetics of a novel
RT glucuronosyltransferase involved in flower pigment biosynthesis.";
RL J. Biol. Chem. 280:899-906(2005).
RN [2]
RP FUNCTION, 3D-STRUCTURE MODELING, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF ARG-25; ASN-123; LEU-148; ASP-152; PRO-174 AND ILE-187.
RX PubMed=18829982; DOI=10.1104/pp.108.128256;
RA Osmani S.A., Bak S., Imberty A., Olsen C.E., Moeller B.L.;
RT "Catalytic key amino acids and UDP-sugar donor specificity of a plant
RT glucuronosyltransferase, UGT94B1: molecular modeling substantiated by site-
RT specific mutagenesis and biochemical analyses.";
RL Plant Physiol. 148:1295-1308(2008).
CC -!- FUNCTION: Involved in the production of glucuronosylated anthocyanins
CC that are the origin of the red coloration of flowers. Can use cyanidin
CC 3-O-6''-O-malonylglucoside, cyanidin 3-O-glucoside and delphinidin 3-O-
CC glucosideas substrates, but not pelargonidin 3-O-glucoside, cyanidin 3-
CC O-3'',6''-O-dimalonylglucoside, pelargonidin 3,5-O-diglucoside,
CC pelargonidin 3-O-6''-O-malonylglucoside-5-O-glucoside, quercetin 3-O-
CC glucoside, quercetin 3-O-6''-O-malonylglucoside, daidzin, genistin,7-O-
CC 6''-O-malonylglucosides of daidzein and genistein, cyanidin, quercetin,
CC daidzein, genistein p-Nitrophenyl beta-D-glucopyranoside, beta-
CC estradiol, 17alpha-estradiol, 1-naphthol, 2-naphthol, 4-
CC methylumbelliferone, and p-nitrophenol. Highly specific for UDP-
CC glucuronate (UDP-GlcUA). Arg-25 is decisive with respect to UDP-sugar
CC specificity. {ECO:0000269|PubMed:15509561,
CC ECO:0000269|PubMed:18829982}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cyanidin 3-O-beta-D-glucoside + UDP-alpha-D-glucuronate =
CC cyanidin 3-O-(2-O-beta-D-glucuronosyl)-beta-D-glucoside + H(+) + UDP;
CC Xref=Rhea:RHEA:28258, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:77824, ChEBI:CHEBI:77857;
CC EC=2.4.1.254; Evidence={ECO:0000269|PubMed:15509561};
CC -!- ACTIVITY REGULATION: Inhibited by copper, mercury, UDP, UTP and
CC partially by calcium, cadmium, iron and UMP. Not affected by cobalt,
CC magnesium, manganese, zinc, nickel, tin, uridine, sadium malonate and
CC glucose. {ECO:0000269|PubMed:15509561}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=19 uM for cyanidin 3-O-6''-O-malonylglucoside
CC {ECO:0000269|PubMed:15509561, ECO:0000269|PubMed:18829982};
CC KM=101 uM for UDP-glucuronate {ECO:0000269|PubMed:15509561,
CC ECO:0000269|PubMed:18829982};
CC KM=85 uM for cyanidin 3-O-glucoside {ECO:0000269|PubMed:15509561,
CC ECO:0000269|PubMed:18829982};
CC KM=730 uM for UDP-glucose {ECO:0000269|PubMed:15509561,
CC ECO:0000269|PubMed:18829982};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:15509561,
CC ECO:0000269|PubMed:18829982};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:15509561, ECO:0000269|PubMed:18829982};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15509561}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in petals. Not detected in sepals, stems,
CC leaves, tubular corollas and white petals.
CC {ECO:0000269|PubMed:15509561}.
CC -!- DEVELOPMENTAL STAGE: Peak of expression at stage 4 of flower
CC development. {ECO:0000269|PubMed:15509561}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB190262; BAD77944.1; -; mRNA.
DR AlphaFoldDB; Q5NTH0; -.
DR SMR; Q5NTH0; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR KEGG; ag:BAD77944; -.
DR BioCyc; MetaCyc:MON-15934; -.
DR BRENDA; 2.4.1.254; 11567.
DR SABIO-RK; Q5NTH0; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0102160; F:cyanidin-3-O-glucoside 2-O-glucuronosyltransferase activity; IEA:UniProtKB-EC.
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 Cytoplasm; Direct protein sequencing; Glycosyltransferase; Transferase.
FT CHAIN 1..438
FT /note="Cyanidin-3-O-glucoside 2-O-glucuronosyltransferase"
FT /id="PRO_0000412107"
FT BINDING 264
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT BINDING 315..316
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT BINDING 333..341
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT BINDING 355..358
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT MUTAGEN 25
FT /note="R->G: Decreased activity with UDP-GlcUA as donor.
FT Increased activity with UDP-Glc as donor."
FT /evidence="ECO:0000269|PubMed:18829982"
FT MUTAGEN 25
FT /note="R->K: Decreased activity with UDP-GlcUA as donor and
FT decreased affinity. Increased activity with UDP-Glc as
FT donor."
FT /evidence="ECO:0000269|PubMed:18829982"
FT MUTAGEN 25
FT /note="R->P: Decreased activity with UDP-GlcUA as donor."
FT /evidence="ECO:0000269|PubMed:18829982"
FT MUTAGEN 25
FT /note="R->S: Decreased activity with UDP-GlcUA as donor but
FT no changes of the affinity. Increased activity with UDP-Glc
FT as donor."
FT /evidence="ECO:0000269|PubMed:18829982"
FT MUTAGEN 123
FT /note="N->A: Strongly decreased activity."
FT /evidence="ECO:0000269|PubMed:18829982"
FT MUTAGEN 148
FT /note="L->A: Strongly decreased activity."
FT /evidence="ECO:0000269|PubMed:18829982"
FT MUTAGEN 152
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18829982"
FT MUTAGEN 174
FT /note="P->G: Strongly decreased activity."
FT /evidence="ECO:0000269|PubMed:18829982"
FT MUTAGEN 187
FT /note="I->A,S: Strongly decreased activity."
FT /evidence="ECO:0000269|PubMed:18829982"
SQ SEQUENCE 438 AA; 49645 MW; 9CAC3D1BC58471E7 CRC64;
MDSKIDSKTF RVVMLPWLAY SHISRFLVFA KRLTNHNFHI YICSSQTNMQ YLKNNLTSQY
SKSIQLIELN LPSSSELPLQ YHTTHGLPPH LTKTLSDDYQ KSGPDFETIL IKLNPHLVIY
DFNQLWAPEV ASTLHIPSIQ LLSGCVALYA LDAHLYTKPL DENLAKFPFP EIYPKNRDIP
KGGSKYIERF VDCMRRSCEI ILVRSTMELE GKYIDYLSKT LGKKVLPVGP LVQEASLLQD
DHIWIMKWLD KKEESSVVFV CFGSEYILSD NEIEDIAYGL ELSQVSFVWA IRAKTSALNG
FIDRVGDKGL VIDKWVPQAN ILSHSSTGGF ISHCGWSSTM ESIRYGVPII AMPMQFDQPY
NARLMETVGA GIEVGRDGEG RLKREEIAAV VRKVVVEDSG ESIREKAKEL GEIMKKNMEA
EVDGIVIENL VKLCEMNN
