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Protein

UDP-glycosyltransferase 78D1

Gene

UGT78D1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a UDP-rhamnose:flavonol-3-O-glucoside rhamnosyltransferase. Keampferol and quercitin are used as substrates. Possesses low quercetin 3-O-glucosyltransferase activity in vitro.2 Publications

Catalytic activityi

UDP-beta-L-rhamnose + a flavonol 3-O-beta-D-glucoside = UDP + a flavonol 3-O-(alpha-L-rhamnosyl-(1->6)-beta-D-glucoside).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei280 – 2801UDP-glucoseBy similarity

GO - Molecular functioni

GO - Biological processi

  • flavonoid glucuronidation Source: GO_Central
  • flavonol biosynthetic process Source: TAIR
  • response to karrikin Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciARA:AT1G30530-MONOMER.
MetaCyc:AT1G30530-MONOMER.

Protein family/group databases

CAZyiGT1. Glycosyltransferase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-glycosyltransferase 78D1 (EC:2.4.1.-)
Alternative name(s):
Flavonol-3-O-glucoside L-rhamnosyltransferase (EC:2.4.1.1591 Publication)
UDP-rhamnose:flavonol 3-O-glucoside rhamnosyltransferase
Gene namesi
Name:UGT78D1
Ordered Locus Names:At1g30530
ORF Names:F26G16.15
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G30530.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 453453UDP-glycosyltransferase 78D1PRO_0000074159Add
BLAST

Proteomic databases

PaxDbiQ9S9P6.
PRIDEiQ9S9P6.

Expressioni

Tissue specificityi

Expressed in leaves, flowers, siliques, and stems.1 Publication

Gene expression databases

ExpressionAtlasiQ9S9P6. baseline and differential.
GenevisibleiQ9S9P6. AT.

Interactioni

Protein-protein interaction databases

BioGridi25168. 3 interactions.
IntActiQ9S9P6. 1 interaction.
STRINGi3702.AT1G30530.1.

Structurei

3D structure databases

ProteinModelPortaliQ9S9P6.
SMRiQ9S9P6. Positions 10-452.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni333 – 3353UDP-glucose bindingBy similarity
Regioni350 – 3589UDP-glucose bindingBy similarity
Regioni372 – 3754UDP-glucose bindingBy similarity

Sequence similaritiesi

Belongs to the UDP-glycosyltransferase family.Curated

Phylogenomic databases

eggNOGiKOG1192. Eukaryota.
COG1819. LUCA.
HOGENOMiHOG000237564.
InParanoidiQ9S9P6.
KOiK15787.
OMAiGANSLCA.
PhylomeDBiQ9S9P6.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q9S9P6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKFSEPIRD SHVAVLAFFP VGAHAGPLLA VTRRLAAASP STIFSFFNTA
60 70 80 90 100
RSNASLFSSD HPENIKVHDV SDGVPEGTML GNPLEMVELF LEAAPRIFRS
110 120 130 140 150
EIAAAEIEVG KKVTCMLTDA FFWFAADIAA ELNATWVAFW AGGANSLCAH
160 170 180 190 200
LYTDLIRETI GLKDVSMEET LGFIPGMENY RVKDIPEEVV FEDLDSVFPK
210 220 230 240 250
ALYQMSLALP RASAVFISSF EELEPTLNYN LRSKLKRFLN IAPLTLLSST
260 270 280 290 300
SEKEMRDPHG CFAWMGKRSA ASVAYISFGT VMEPPPEELV AIAQGLESSK
310 320 330 340 350
VPFVWSLKEK NMVHLPKGFL DRTREQGIVV PWAPQVELLK HEAMGVNVTH
360 370 380 390 400
CGWNSVLESV SAGVPMIGRP ILADNRLNGR AVEVVWKVGV MMDNGVFTKE
410 420 430 440 450
GFEKCLNDVF VHDDGKTMKA NAKKLKEKLQ EDFSMKGSSL ENFKILLDEI

VKV
Length:453
Mass (Da):50,095
Last modified:May 1, 2000 - v1
Checksum:i2CCE13AFFEF54E77
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti330 – 3301V → D in AAM65321 (Ref. 4) Curated
Sequence conflicti430 – 4301Q → H in AAM65321 (Ref. 4) Curated
Sequence conflicti440 – 4401L → F in AAM65321 (Ref. 4) Curated
Sequence conflicti445 – 4451I → V in AAM65321 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC009917 Genomic DNA. Translation: AAF19756.1.
CP002684 Genomic DNA. Translation: AEE31240.1.
AY056312 mRNA. Translation: AAL07161.1.
AF360160 mRNA. Translation: AAK25870.1.
AY087785 mRNA. Translation: AAM65321.1.
PIRiD86430.
RefSeqiNP_564357.1. NM_102790.3.
UniGeneiAt.21995.

Genome annotation databases

EnsemblPlantsiAT1G30530.1; AT1G30530.1; AT1G30530.
GeneIDi839933.
GrameneiAT1G30530.1; AT1G30530.1; AT1G30530.
KEGGiath:AT1G30530.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC009917 Genomic DNA. Translation: AAF19756.1.
CP002684 Genomic DNA. Translation: AEE31240.1.
AY056312 mRNA. Translation: AAL07161.1.
AF360160 mRNA. Translation: AAK25870.1.
AY087785 mRNA. Translation: AAM65321.1.
PIRiD86430.
RefSeqiNP_564357.1. NM_102790.3.
UniGeneiAt.21995.

3D structure databases

ProteinModelPortaliQ9S9P6.
SMRiQ9S9P6. Positions 10-452.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi25168. 3 interactions.
IntActiQ9S9P6. 1 interaction.
STRINGi3702.AT1G30530.1.

Protein family/group databases

CAZyiGT1. Glycosyltransferase Family 1.

Proteomic databases

PaxDbiQ9S9P6.
PRIDEiQ9S9P6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G30530.1; AT1G30530.1; AT1G30530.
GeneIDi839933.
GrameneiAT1G30530.1; AT1G30530.1; AT1G30530.
KEGGiath:AT1G30530.

Organism-specific databases

TAIRiAT1G30530.

Phylogenomic databases

eggNOGiKOG1192. Eukaryota.
COG1819. LUCA.
HOGENOMiHOG000237564.
InParanoidiQ9S9P6.
KOiK15787.
OMAiGANSLCA.
PhylomeDBiQ9S9P6.

Enzyme and pathway databases

BioCyciARA:AT1G30530-MONOMER.
MetaCyc:AT1G30530-MONOMER.

Miscellaneous databases

PROiQ9S9P6.

Gene expression databases

ExpressionAtlasiQ9S9P6. baseline and differential.
GenevisibleiQ9S9P6. AT.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Phylogenetic analysis of the UDP-glycosyltransferase multigene family of Arabidopsis thaliana."
    Li Y., Baldauf S., Lim E.K., Bowles D.J.
    J. Biol. Chem. 276:4338-4343(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY.
  6. "UGT73C6 and UGT78D1, glycosyltransferases involved in flavonol glycoside biosynthesis in Arabidopsis thaliana."
    Jones P., Messner B., Nakajima J., Schaffner A.R., Saito K.
    J. Biol. Chem. 278:43910-43918(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
  7. "Arabidopsis glycosyltransferases as biocatalysts in fermentation for regioselective synthesis of diverse quercetin glucosides."
    Lim E.K., Ashford D.A., Hou B., Jackson R.G., Bowles D.J.
    Biotechnol. Bioeng. 87:623-631(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic diversity."
    Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M., Tohge T., Fernie A.R.
    Plant Physiol. Biochem. 72:21-34(2013)
    Cited for: REVIEW, NOMENCLATURE.

Entry informationi

Entry nameiU78D1_ARATH
AccessioniPrimary (citable) accession number: Q9S9P6
Secondary accession number(s): Q8LAI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2005
Last sequence update: May 1, 2000
Last modified: February 17, 2016
This is version 96 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

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. 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.