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Protein

Anthocyanidin 3-O-glucosyltransferase 2

Gene

UFGT

Organism
Vitis vinifera (Grape)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

In the presence of other necessary color factors, this glycosylation reaction allows the accumulation of anthocyanin pigments. Involved in the formation of red wine pigments. Can use UDP-Glc, UDP-5SGlc, UDP-Xyl, UDP-Man, UDP-Gal, UDP-GlcNAc, GDP-Glc, dTDP-Glc and dTDP-Xyl as sugar donor, but not UDP-6OMeGal, UDP-Ara, UDP-6FGal, UDP-GlcN, UDP-2FGal, UDP-5SAra, GDP-Man, GDPFuc, UDP-Fuc or UDP-Rha. Cyanidin is the natural acceptor, but quercitin and kaempferol can also be glucosylated.

Catalytic activityi

UDP-D-glucose + an anthocyanidin = UDP + an anthocyanidin-3-O-beta-D-glucoside.

Enzyme regulationi

Inhibited by Mn2+ and Zn2+.1 Publication

Kineticsi

  1. KM=679 µM for UDP-Glc (in the presence of 100 µM quercitin)2 Publications
  2. KM=300 µM for dTDP-Glc (in the presence of 100 µM quercitin)2 Publications
  3. KM=166 µM for UDP-5SGlc (in the presence of 100 µM quercitin)2 Publications
  4. KM=194 µM for UDP-GlcNAc (in the presence of 100 µM quercitin)2 Publications
  5. KM=48.2 µM for UDP-Gal (in the presence of 100 µM quercitin)2 Publications
  6. KM=50.1 µM for UDP-Man (in the presence of 100 µM quercitin)2 Publications
  7. KM=167 µM for GDP-Glc (in the presence of 100 µM quercitin)2 Publications
  8. KM=166 µM for dTDP-Xyl (in the presence of 100 µM quercitin)2 Publications
  9. KM=219 µM for UDP-Xyl (in the presence of 100 µM quercitin)2 Publications
  10. KM=30.8 µM for quercitin (in the presence of UDP-Glc)2 Publications
  11. KM=42.3 µM for kaempferol (in the presence of UDP-Glc)2 Publications
  12. KM=30 µM for cyanidin (in the presence of UDP-Glc)2 Publications
  13. KM=16 µM for delphinidin (in the presence of UDP-Glc)2 Publications
  14. KM=35.7 µM for malvidin (in the presence of UDP-Glc)2 Publications
  1. Vmax=18.9 nmol/sec/mg enzyme with quercitin as substrate2 Publications
  2. Vmax=905 nmol/sec/mg enzyme with cyanidin as substrate2 Publications

pH dependencei

Optimum pH is 8.0.2 Publications

Pathwayi: anthocyanin biosynthesis

This protein is involved in the pathway anthocyanin biosynthesis, which is part of Pigment biosynthesis.
View all proteins of this organism that are known to be involved in the pathway anthocyanin biosynthesis and in Pigment biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei18Substrate1
Binding sitei19UDP-D-glucose1 Publication1
Binding sitei20Substrate1
Binding sitei84Substrate1
Binding sitei141UDP-D-glucose1 Publication1
Binding sitei150Substrate1
Binding sitei188Substrate1
Binding sitei280UDP-D-glucose1 Publication1
Binding sitei306UDP-D-glucose1 Publication1
Binding sitei333UDP-D-glucose; via amide nitrogen and carbonyl oxygen1 Publication1

GO - Molecular functioni

  • anthocyanidin 3-O-glucosyltransferase activity Source: UniProtKB

GO - Biological processi

  • anthocyanin-containing compound biosynthetic process Source: UniProtKB
  • cyanidin 3-O-glucoside biosynthetic process Source: UniProtKB
  • kaempferol O-glucoside biosynthetic process Source: UniProtKB
  • quercetin O-glucoside biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.4.1.115. 6671.
UniPathwayiUPA00009.

Protein family/group databases

CAZyiGT1. Glycosyltransferase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
Anthocyanidin 3-O-glucosyltransferase 2 (EC:2.4.1.115)
Alternative name(s):
Flavonol 3-O-glucosyltransferase
UDP-glucose flavonoid 3-O-glucosyltransferase
Gene namesi
Name:UFGT
Synonyms:AlUFGT1, AlUFGT2, FlUFGT1, FlUFGT2, ITUFGT1, ITUFGT2, RUUFGT1, RUUFGT2, VVGT1
ORF Names:GSVIVT00014047001, LOC100233099, VITISV_008354
OrganismiVitis vinifera (Grape)
Taxonomic identifieri29760 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsVitalesVitaceaeVitis

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi20H → A: Loss of catalytic activity. 1 Publication1
Mutagenesisi141T → A: 6-fold decrease in catalytic efficiency. 1 Publication1
Mutagenesisi374D → A: Loss of catalytic activity. 1 Publication1
Mutagenesisi375Q → H: Loss of catalytic activity. 1 Publication1
Mutagenesisi375Q → N: Impaired catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000741511 – 456Anthocyanidin 3-O-glucosyltransferase 2Add BLAST456

Proteomic databases

PRIDEiP51094.

Expressioni

Tissue specificityi

Detected only in berry skin.1 Publication

Inductioni

By light.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi29760.VIT_16s0039g02230.t01.

Structurei

Secondary structure

1456
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 13Combined sources5
Beta strandi17 – 20Combined sources4
Helixi21 – 34Combined sources14
Beta strandi38 – 44Combined sources7
Helixi46 – 52Combined sources7
Beta strandi64 – 68Combined sources5
Helixi85 – 109Combined sources25
Beta strandi115 – 119Combined sources5
Helixi125 – 132Combined sources8
Beta strandi135 – 140Combined sources6
Helixi144 – 151Combined sources8
Helixi153 – 160Combined sources8
Helixi184 – 186Combined sources3
Beta strandi191 – 194Combined sources4
Helixi199 – 210Combined sources12
Helixi211 – 213Combined sources3
Beta strandi217 – 221Combined sources5
Helixi223 – 225Combined sources3
Helixi227 – 236Combined sources10
Beta strandi240 – 242Combined sources3
Helixi246 – 249Combined sources4
Helixi261 – 266Combined sources6
Beta strandi273 – 277Combined sources5
Helixi286 – 299Combined sources14
Beta strandi303 – 306Combined sources4
Helixi309 – 314Combined sources6
Helixi319 – 323Combined sources5
Turni324 – 326Combined sources3
Beta strandi327 – 331Combined sources5
Helixi335 – 339Combined sources5
Beta strandi344 – 349Combined sources6
Helixi353 – 362Combined sources10
Beta strandi366 – 368Combined sources3
Helixi375 – 384Combined sources10
Beta strandi389 – 391Combined sources3
Helixi393 – 395Combined sources3
Helixi399 – 411Combined sources13
Helixi413 – 432Combined sources20
Helixi438 – 450Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2C1XX-ray1.90A1-456[»]
2C1ZX-ray1.90A1-456[»]
2C9ZX-ray2.10A1-456[»]
ProteinModelPortaliP51094.
SMRiP51094.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51094.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni350 – 358UDP-D-glucose binding9
Regioni374 – 375UDP-D-glucose binding2

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi32 – 35Poly-Ala4

Sequence similaritiesi

Belongs to the UDP-glycosyltransferase family.Curated

Phylogenomic databases

eggNOGiKOG1192. Eukaryota.
COG1819. LUCA.

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.

P51094-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQTTTNPHV AVLAFPFSTH AAPLLAVVRR LAAAAPHAVF SFFSTSQSNA
60 70 80 90 100
SIFHDSMHTM QCNIKSYDIS DGVPEGYVFA GRPQEDIELF TRAAPESFRQ
110 120 130 140 150
GMVMAVAETG RPVSCLVADA FIWFAADMAA EMGLAWLPFW TAGPNSLSTH
160 170 180 190 200
VYIDEIREKI GVSGIQGRED ELLNFIPGMS KVRFRDLQEG IVFGNLNSLF
210 220 230 240 250
SRMLHRMGQV LPKATAVFIN SFEELDDSLT NDLKSKLKTY LNIGPFNLIT
260 270 280 290 300
PPPVVPNTTG CLQWLKERKP TSVVYISFGT VTTPPPAEVV ALSEALEASR
310 320 330 340 350
VPFIWSLRDK ARVHLPEGFL EKTRGYGMVV PWAPQAEVLA HEAVGAFVTH
360 370 380 390 400
CGWNSLWESV AGGVPLICRP FFGDQRLNGR MVEDVLEIGV RIEGGVFTKS
410 420 430 440 450
GLMSCFDQIL SQEKGKKLRE NLRALRETAD RAVGPKGSST ENFITLVDLV

SKPKDV
Length:456
Mass (Da):50,150
Last modified:October 13, 2009 - v2
Checksum:i60BF6A70A3D17ABC
GO

Sequence cautioni

The sequence CAA53582 differs from that shown. Reason: Frameshift at positions 307, 309, 341 and 344.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti47Q → Z in strain: cv. Pinot noir. 1
Natural varianti69I → V in strain: cv. Italia, cv. Pinot noir and cv. Ruby Okuyama. 1
Natural varianti74P → A in strain: cv. Pinot noir / PN40024. 1
Natural varianti91T → M in strain: cv. Flame Muscat, cv. Italia, cv. Muscat of Alexandria, cv. Pinot noir, cv. Pinot noir / PN40024, cv. Red Globe and cv. Ruby Okuyama. 1
Natural varianti134L → V in strain: cv. Flame Muscat, cv. Italia, cv. Muscat of Alexandria, cv. Pinot noir, cv. Pinot noir / PN40024, cv. Red Globe and cv. Ruby Okuyama. 1 Publication1
Natural varianti153I → T in strain: cv. Flame Muscat, cv. Italia, cv. Muscat of Alexandria, cv. Pinot noir / PN40024, cv. Red Globe and cv. Ruby Okuyama. 1
Natural varianti161G → A in cv. Red Globe. 1
Natural varianti163S → SG in strain: cv. Pinot noir / PN40024. 1
Natural varianti255V → I in strain: cv. Italia, cv. Pinot noir / PN40024 and cv. Ruby Okuyama. 1
Natural varianti289V → L in strain: cv. Flame Muscat, cv. Italia, cv. Muscat of Alexandria, cv. Pinot noir, cv. Pinot noir / PN40024, cv. Red Globe and cv. Ruby Okuyama. 1
Natural varianti293S → A in strain: cv. Flame Muscat, cv. Italia, cv. Muscat of Alexandria, cv. Pinot noir, cv. Pinot noir / PN40024, cv. Red Globe and cv. Ruby Okuyama. 1
Natural varianti312R → S in strain: cv. Flame Muscat, cv. Lambrusco Foglia Frastagliata and cv. Muscat of Alexandria. 1
Natural varianti326Y → H in cv. Red Globe. 1
Natural varianti372F → Y in strain: cv. Pinot noir / PN40024. 1
Natural varianti385V → A in strain: cv. Flame Muscat, cv. Italia, cv. Muscat of Alexandria, cv. Pinot noir, cv. Pinot noir / PN40024, cv. Red Globe and cv. Ruby Okuyama. 1
Natural varianti399 – 400KS → EN in strain: cv. Flame Muscat and cv. Muscat of Alexandria. 2
Natural varianti399K → E in strain: cv. Flame Muscat, cv. Italia, cv. Muscat of Alexandria, cv. Pinot noir, cv. Pinot noir / PN40024 and cv. Ruby Okuyama. 1
Natural varianti423R → G in strain: cv. Pinot noir / PN40024. 1
Natural varianti444I → K in strain: cv. Flame Muscat, cv. Italia, cv. Lambrusco Foglia Frastagliata, cv. Muscat of Alexandria, cv. Pinot noir, cv. Pinot noir / PN40024, cv. Red Globe and cv. Ruby Okuyama. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF000371 mRNA. Translation: AAB81682.1.
AF000372 mRNA. Translation: AAB81683.1.
AB047092 Genomic DNA. Translation: BAB41019.1.
AB047093 Genomic DNA. Translation: BAB41020.1.
AB047094 Genomic DNA. Translation: BAB41021.1.
AB047095 Genomic DNA. Translation: BAB41022.1.
AB047096 Genomic DNA. Translation: BAB41023.1.
AB047097 Genomic DNA. Translation: BAB41024.1.
AB047098 Genomic DNA. Translation: BAB41025.1.
AB047099 Genomic DNA. Translation: BAB41026.1.
DQ513314 Genomic DNA. Translation: ABF59818.1.
AM472935 Genomic DNA. Translation: CAN61846.1.
X75968 mRNA. Translation: CAA53582.1. Frameshift.
UniGeneiVvi.17.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF000371 mRNA. Translation: AAB81682.1.
AF000372 mRNA. Translation: AAB81683.1.
AB047092 Genomic DNA. Translation: BAB41019.1.
AB047093 Genomic DNA. Translation: BAB41020.1.
AB047094 Genomic DNA. Translation: BAB41021.1.
AB047095 Genomic DNA. Translation: BAB41022.1.
AB047096 Genomic DNA. Translation: BAB41023.1.
AB047097 Genomic DNA. Translation: BAB41024.1.
AB047098 Genomic DNA. Translation: BAB41025.1.
AB047099 Genomic DNA. Translation: BAB41026.1.
DQ513314 Genomic DNA. Translation: ABF59818.1.
AM472935 Genomic DNA. Translation: CAN61846.1.
X75968 mRNA. Translation: CAA53582.1. Frameshift.
UniGeneiVvi.17.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2C1XX-ray1.90A1-456[»]
2C1ZX-ray1.90A1-456[»]
2C9ZX-ray2.10A1-456[»]
ProteinModelPortaliP51094.
SMRiP51094.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi29760.VIT_16s0039g02230.t01.

Protein family/group databases

CAZyiGT1. Glycosyltransferase Family 1.

Proteomic databases

PRIDEiP51094.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1192. Eukaryota.
COG1819. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00009.
BRENDAi2.4.1.115. 6671.

Miscellaneous databases

EvolutionaryTraceiP51094.

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...

Entry informationi

Entry nameiUFOG_VITVI
AccessioniPrimary (citable) accession number: P51094
Secondary accession number(s): A5BVQ6
, A7PBD4, O22303, O22304, Q1G141, Q9AQV0, Q9AR43, Q9AR45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 13, 2009
Last modified: November 2, 2016
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

The expression of UFGT is not detected in white grapes.

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.