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Protein

Cyanidin-3-O-glucoside 2-O-glucuronosyltransferase

Gene

UGAT

Organism
Bellis perennis (Daisy)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the production of glucuronosylated anthocyanins that are the origin of the red coloration of flowers. Can use cyanidin 3-O-6''-O-malonylglucoside, cyanidin 3-O-glucoside and delphinidin 3-O-glucosideas substrates, but not pelargonidin 3-O-glucoside, cyanidin 3-O-3'',6''-O-dimalonylglucoside, pelargonidin 3,5-O-diglucoside, pelargonidin 3-O-6''-O-malonylglucoside-5-O-glucoside, quercetin 3-O-glucoside, quercetin 3-O-6''-O-malonylglucoside, daidzin, genistin,7-O-6''-O-malonylglucosides of daidzein and genistein, cyanidin, quercetin, daidzein, genistein p-Nitrophenyl beta-D-glucopyranoside, beta-estradiol, 17alpha-estradiol, 1-naphthol, 2-naphthol, 4-methylumbelliferone, and p-nitrophenol. Highly specific for UDP-glucuronate (UDP-GlcUA). Arg-25 is decisive with respect to UDP-sugar specificity.2 Publications

Catalytic activityi

UDP-alpha-D-glucuronate + cyanidin 3-O-beta-D-glucoside = UDP + cyanidin 3-O-(2-O-beta-D-glucuronosyl)-beta-D-glucoside.1 Publication

Enzyme regulationi

Inhibited by copper, mercury, UDP, UTP and partially by calcium, cadmium, iron and UMP. Not affected by cobalt, magnesium, manganese, zinc, nickel, tin, uridine, sadium malonate and glucose.1 Publication

Kineticsi

  1. KM=19 µM for cyanidin 3-O-6''-O-malonylglucoside2 Publications
  2. KM=101 µM for UDP-glucuronate2 Publications
  3. KM=85 µM for cyanidin 3-O-glucoside2 Publications
  4. KM=730 µM for UDP-glucose2 Publications

    pH dependencei

    Optimum pH is 8.0.2 Publications

    Temperature dependencei

    Optimum temperature is 35 degrees Celsius.2 Publications

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-15934.
    BRENDAi2.4.1.254. 11567.
    SABIO-RKQ5NTH0.

    Protein family/group databases

    CAZyiGT1. Glycosyltransferase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyanidin-3-O-glucoside 2-O-glucuronosyltransferase (EC:2.4.1.254)
    Short name:
    BpUGAT
    Alternative name(s):
    UDP-glucuronic acid:anthocyanin glucuronosyltransferase
    Gene namesi
    Name:UGAT
    Synonyms:UGT94B1
    OrganismiBellis perennis (Daisy)
    Taxonomic identifieri41492 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsAsteralesAsteraceaeAsteroideaeAstereaeAstereae incertae sedisBellis

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi25 – 251R → G: Decreased activity with UDP-GlcUA as donor. Increased activity with UDP-Glc as donor. 1 Publication
    Mutagenesisi25 – 251R → K: Decreased activity with UDP-GlcUA as donor and decreased affinity. Increased activity with UDP-Glc as donor. 1 Publication
    Mutagenesisi25 – 251R → P: Decreased activity with UDP-GlcUA as donor. 1 Publication
    Mutagenesisi25 – 251R → S: Decreased activity with UDP-GlcUA as donor but no changes of the affinity. Increased activity with UDP-Glc as donor. 1 Publication
    Mutagenesisi123 – 1231N → A: Strongly decreased activity. 1 Publication
    Mutagenesisi148 – 1481L → A: Strongly decreased activity. 1 Publication
    Mutagenesisi152 – 1521D → A: Loss of activity. 1 Publication
    Mutagenesisi174 – 1741P → G: Strongly decreased activity. 1 Publication
    Mutagenesisi187 – 1871I → A or S: Strongly decreased activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 438438Cyanidin-3-O-glucoside 2-O-glucuronosyltransferasePRO_0000412107Add
    BLAST

    Expressioni

    Tissue specificityi

    Expressed in petals. Not detected in sepals, stems, leaves, tubular corollas and white petals.1 Publication

    Developmental stagei

    Peak of expression at stage 4 of flower development.1 Publication

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ5NTH0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni316 – 3183UDP-sugar bindingBy similarity
    Regioni333 – 3419UDP-sugar bindingBy similarity
    Regioni355 – 3584UDP-sugar bindingBy similarity

    Sequence similaritiesi

    Belongs to the UDP-glycosyltransferase family.Curated

    Phylogenomic databases

    KOiK12937.

    Family and domain databases

    InterProiIPR002213. UDP_glucos_trans.
    [Graphical view]
    PANTHERiPTHR11926. PTHR11926. 1 hit.
    PfamiPF00201. UDPGT. 1 hit.
    [Graphical view]
    PROSITEiPS00375. UDPGT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q5NTH0-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDSKIDSKTF RVVMLPWLAY SHISRFLVFA KRLTNHNFHI YICSSQTNMQ
    60 70 80 90 100
    YLKNNLTSQY SKSIQLIELN LPSSSELPLQ YHTTHGLPPH LTKTLSDDYQ
    110 120 130 140 150
    KSGPDFETIL IKLNPHLVIY DFNQLWAPEV ASTLHIPSIQ LLSGCVALYA
    160 170 180 190 200
    LDAHLYTKPL DENLAKFPFP EIYPKNRDIP KGGSKYIERF VDCMRRSCEI
    210 220 230 240 250
    ILVRSTMELE GKYIDYLSKT LGKKVLPVGP LVQEASLLQD DHIWIMKWLD
    260 270 280 290 300
    KKEESSVVFV CFGSEYILSD NEIEDIAYGL ELSQVSFVWA IRAKTSALNG
    310 320 330 340 350
    FIDRVGDKGL VIDKWVPQAN ILSHSSTGGF ISHCGWSSTM ESIRYGVPII
    360 370 380 390 400
    AMPMQFDQPY NARLMETVGA GIEVGRDGEG RLKREEIAAV VRKVVVEDSG
    410 420 430
    ESIREKAKEL GEIMKKNMEA EVDGIVIENL VKLCEMNN
    Length:438
    Mass (Da):49,645
    Last modified:February 1, 2005 - v1
    Checksum:i9CAC3D1BC58471E7
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB190262 mRNA. Translation: BAD77944.1.

    Genome annotation databases

    KEGGiag:BAD77944.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB190262 mRNA. Translation: BAD77944.1.

    3D structure databases

    ProteinModelPortaliQ5NTH0.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiGT1. Glycosyltransferase Family 1.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:BAD77944.

    Phylogenomic databases

    KOiK12937.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-15934.
    BRENDAi2.4.1.254. 11567.
    SABIO-RKQ5NTH0.

    Family and domain databases

    InterProiIPR002213. UDP_glucos_trans.
    [Graphical view]
    PANTHERiPTHR11926. PTHR11926. 1 hit.
    PfamiPF00201. UDPGT. 1 hit.
    [Graphical view]
    PROSITEiPS00375. UDPGT. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "UDP-glucuronic acid:anthocyanin glucuronosyltransferase from red daisy (Bellis perennis) flowers. Enzymology and phylogenetics of a novel glucuronosyltransferase involved in flower pigment biosynthesis."
      Sawada S., Suzuki H., Ichimaida F., Yamaguchi M.A., Iwashita T., Fukui Y., Hemmi H., Nishino T., Nakayama T.
      J. Biol. Chem. 280:899-906(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 102-112; 384-393 AND 417-426, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    2. "Catalytic key amino acids and UDP-sugar donor specificity of a plant glucuronosyltransferase, UGT94B1: molecular modeling substantiated by site-specific mutagenesis and biochemical analyses."
      Osmani S.A., Bak S., Imberty A., Olsen C.E., Moeller B.L.
      Plant Physiol. 148:1295-1308(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, 3D-STRUCTURE MODELING, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-25; ASN-123; LEU-148; ASP-152; PRO-174 AND ILE-187.

    Entry informationi

    Entry nameiUGAT_BELPE
    AccessioniPrimary (citable) accession number: Q5NTH0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 27, 2011
    Last sequence update: February 1, 2005
    Last modified: November 11, 2015
    This is version 31 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.