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Entry version 92 (11 Dec 2019)
Sequence version 2 (13 Oct 2009)
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Protein

Anthocyanidin 3-O-glucosyltransferase UFGT

Gene

UFGT

Organism
Vitis vinifera (Grape)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

In the presence of other necessary color factors, this glycosylation reaction allows the accumulation of anthocyanin pigments (Probable). Involved in the formation of red wine pigments (Probable). UDP-glucose (UDP-Glc) is the physiological sugar donor, and cyanidin is the natural acceptor in vivo (PubMed:9535914). Can glucosylate the anthocyanidins delphinidin, peonidin, pelargonidin and malvidin (PubMed:9535914). The flavonols quercitin and kaempferol can also be glucosylated in vitro, but with glucosylation rates 50-100 times lower than cyanidin (PubMed:9535914). In vitro, can use UDP-Glc, UDP-5SGlc, UDP-Xyl, UDP-Man, UDP-Gal, UDP-GlcNAc, GDP-Glc, dTDP-Glc and dTDP-Xyl as sugar donors, but not UDP-6OMeGal, UDP-Ara, UDP-6FGal, UDP-GlcN, UDP-2FGal, UDP-5SAra, GDP-Man, GDP-Fuc, UDP-Fuc or UDP-Rha (PubMed:16482224).2 Publications2 Publications

Miscellaneous

The expression of UFGT is not detected in white grapes.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by Mn2+ and Zn2+.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=1.9 mM for UDP-Glc (in the presence of quercitin)1 Publication
  2. KM=679 µM for UDP-Glc (in the presence of 100 µM quercitin)1 Publication
  3. KM=300 µM for dTDP-Glc (in the presence of 100 µM quercitin)1 Publication
  4. KM=166 µM for UDP-5SGlc (in the presence of 100 µM quercitin)1 Publication
  5. KM=194 µM for UDP-GlcNAc (in the presence of 100 µM quercitin)1 Publication
  6. KM=48.2 µM for UDP-Gal (in the presence of 100 µM quercitin)1 Publication
  7. KM=50.1 µM for UDP-Man (in the presence of 100 µM quercitin)1 Publication
  8. KM=167 µM for GDP-Glc (in the presence of 100 µM quercitin)1 Publication
  9. KM=166 µM for dTDP-Xyl (in the presence of 100 µM quercitin)1 Publication
  10. KM=219 µM for UDP-Xyl (in the presence of 100 µM quercitin)1 Publication
  11. KM=15 µM for quercitin (in the presence of UDP-Glc)1 Publication
  12. KM=30.8 µM for quercitin (in the presence of UDP-Glc)1 Publication
  13. KM=42.3 µM for kaempferol (in the presence of UDP-Glc)1 Publication
  14. KM=30 µM for cyanidin (in the presence of UDP-Glc)1 Publication
  15. KM=16 µM for delphinidin (in the presence of UDP-Glc)1 Publication
  16. KM=35.7 µM for malvidin (in the presence of UDP-Glc)1 Publication
  1. Vmax=18.9 nmol/sec/mg enzyme with quercitin as substrate1 Publication
  2. Vmax=905 nmol/sec/mg enzyme with cyanidin as substrate1 Publication

pH dependencei

Optimum pH is 8.0.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei18SubstrateCombined sources1 Publication1
Binding sitei19UDP-D-glucoseCombined sources1 Publication1
Binding sitei20SubstrateCombined sources1 Publication1
Binding sitei84SubstrateCombined sources1 Publication1
Binding sitei141UDP-D-glucoseCombined sources1 Publication1
Binding sitei150SubstrateCombined sources1 Publication1
Binding sitei188SubstrateCombined sources1 Publication1
Binding sitei280UDP-D-glucoseCombined sources1 Publication1
Binding sitei306UDP-D-glucoseCombined sources1 Publication1
Binding sitei333UDP-D-glucose; via amide nitrogen and carbonyl oxygenCombined sources1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGlycosyltransferase, Transferase

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.4.1.115 6671

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00009

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GT1 Glycosyltransferase Family 1

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Anthocyanidin 3-O-glucosyltransferase UFGTCurated (EC:2.4.1.1152 Publications)
Alternative name(s):
Flavonol 3-O-glucosyltransferaseCurated (EC:2.4.1.912 Publications)
UDP-glucose flavonoid 3-O-glucosyltransferase1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:UFGT1 Publication
Synonyms:AlUFGT1, AlUFGT2, FlUFGT1, FlUFGT2, ITUFGT1, ITUFGT2, RUUFGT1, RUUFGT2, VVGT1
ORF Names:GSVIVT00014047001, LOC100233099, VITISV_008354
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiVitis vinifera (Grape)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri29760 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsVitalesVitaceaeViteaeVitis

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000741511 – 456Anthocyanidin 3-O-glucosyltransferase UFGTAdd BLAST456

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected only in berry skin.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By light.1 Publication

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P51094 baseline and differential

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
29760.VIT_16s0039g02230.t01

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1456
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P51094

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P51094

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni350 – 358UDP-D-glucose bindingCombined sources1 Publication9
Regioni374 – 375UDP-D-glucose bindingCombined sources1 Publication2

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi32 – 35Poly-Ala4

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the UDP-glycosyltransferase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1192 Eukaryota
COG1819 LUCA

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002213 UDP_glucos_trans
IPR035595 UDP_glycos_trans_CS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00201 UDPGT, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00375 UDPGT, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i60BF6A70A3D17ABC
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CAA53582 differs from that shown. Reason: Frameshift.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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.

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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.

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2C1XX-ray1.90A1-456[»]
2C1ZX-ray1.90A1-456[»]
2C9ZX-ray2.10A1-456[»]
SMRiP51094
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi29760.VIT_16s0039g02230.t01

Protein family/group databases

CAZyiGT1 Glycosyltransferase Family 1

Phylogenomic databases

eggNOGiKOG1192 Eukaryota
COG1819 LUCA

Enzyme and pathway databases

UniPathwayiUPA00009
BRENDAi2.4.1.115 6671

Miscellaneous databases

EvolutionaryTraceiP51094

Gene expression databases

ExpressionAtlasiP51094 baseline and differential

Family and domain databases

InterProiView protein in InterPro
IPR002213 UDP_glucos_trans
IPR035595 UDP_glycos_trans_CS
PfamiView protein in Pfam
PF00201 UDPGT, 1 hit
PROSITEiView protein in PROSITE
PS00375 UDPGT, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiUFOG_VITVI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P51094
Secondary accession number(s): A5BVQ6
, A7PBD4, O22303, O22304, Q1G141, Q9AQV0, Q9AR43, Q9AR45
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 13, 2009
Last modified: December 11, 2019
This is version 92 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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
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