Q9LFJ8 (U78D2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
UDP-glycosyltransferase 78D2
EC=2.4.1.-

Alternative name(s):
Anthocyanin 3-O-glucosyltransferase
Flavonol 3-O-glucosyltransferase.
EC=2.4.1.91
UDP glucose:flavonoid 3-O-glucosyltransferase

Gene names

Name:	UGT78D2
Synonyms:	AGT
Ordered Locus Names:	At5g17050
ORF Names:	F2K13.200

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	460 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the glycosylation of flavonoids from UDP-glucose. Catalyzes the glycosylation of anthocyanins from UDP-glucose. Possesses high quercetin 3-O-glucosyltransferase activity in vitro. Also active in vitro on benzoates and benzoate derivatives. Ref.5 Ref.6 Ref.7 Ref.8
Catalytic activity	UDP-glucose + a flavonol = UDP + a flavonol 3-O-D-glucoside.
Pathway	Secondary metabolite biosynthesis; flavonoid biosynthesis.
Induction	By PAP1. Ref.7
Sequence similarities	Belongs to the UDP-glycosyltransferase family.

Ontologies

Keywords
Biological process	Phenylpropanoid metabolism
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	flavonoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway response to karrikin Inferred from expression pattern PubMed 20351290. Source: TAIR
Molecular_function	anthocyanidin 3-O-glucosyltransferase activity Inferred from direct assay Ref.7. Source: TAIR flavonol 3-O-glucosyltransferase activity Inferred from electronic annotation. Source: EC quercetin 3-O-glucosyltransferase activity Inferred from direct assay Ref.6. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 460	460	UDP-glycosyltransferase 78D2		PRO_0000285275
Regions
	Region	339 – 341	3	UDP-glucose binding By similarity
	Region	356 – 364	9	UDP-glucose binding By similarity
	Region	378 – 381	4	UDP-glucose binding By similarity
Sites
	Binding site	286	1	UDP-glucose By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9LFJ8 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: E9DEAD19E4E05188	FASTA	460	50,486
	10 20 30 40 50 60 MTKPSDPTRD SHVAVLAFPF GTHAAPLLTV TRRLASASPS TVFSFFNTAQ SNSSLFSSGD 70 80 90 100 110 120 EADRPANIRV YDIADGVPEG YVFSGRPQEA IELFLQAAPE NFRREIAKAE TEVGTEVKCL 130 140 150 160 170 180 MTDAFFWFAA DMATEINASW IAFWTAGANS LSAHLYTDLI RETIGVKEVG ERMEETIGVI 190 200 210 220 230 240 SGMEKIRVKD TPEGVVFGNL DSVFSKMLHQ MGLALPRATA VFINSFEDLD PTLTNNLRSR 250 260 270 280 290 300 FKRYLNIGPL GLLSSTLQQL VQDPHGCLAW MEKRSSGSVA YISFGTVMTP PPGELAAIAE 310 320 330 340 350 360 GLESSKVPFV WSLKEKSLVQ LPKGFLDRTR EQGIVVPWAP QVELLKHEAT GVFVTHCGWN 370 380 390 400 410 420 SVLESVSGGV PMICRPFFGD QRLNGRAVEV VWEIGMTIIN GVFTKDGFEK CLDKVLVQDD 430 440 450 460 GKKMKCNAKK LKELAYEAVS SKGRSSENFR GLLDAVVNII

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F. Nature 408:823-826(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]	"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.
[5]	"The activity of Arabidopsis glycosyltransferases toward salicylic acid, 4-hydroxybenzoic acid, and other benzoates." Lim E.K., Doucet C.J., Li Y., Elias L., Worrall D., Spencer S.P., Ross J., Bowles D.J. J. Biol. Chem. 277:586-592(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"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.
[7]	"Functional genomics by integrated analysis of metabolome and transcriptome of Arabidopsis plants over-expressing an MYB transcription factor." Tohge T., Nishiyama Y., Hirai M.Y., Yano M., Nakajima J., Awazuhara M., Inoue E., Takahashi H., Goodenowe D.B., Kitayama M., Noji M., Yamazaki M., Saito K. Plant J. 42:218-235(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION BY PAP1.
[8]	"The formation of anthocyanic vacuolar inclusions in Arabidopsis thaliana and implications for the sequestration of anthocyanin pigments." Pourcel L., Irani N.G., Lu Y., Riedl K., Schwartz S., Grotewold E. Mol. Plant 3:78-90(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"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. 0:0-0(2013) Cited for: REVIEW, NOMENCLATURE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL391141 Genomic DNA. Translation: CAC01718.1. CP002688 Genomic DNA. Translation: AED92377.1. AY072325 mRNA. Translation: AAL61932.1. AY128739 mRNA. Translation: AAM91139.1.
IPI	IPI00524169.
PIR	T51560.
RefSeq	NP_197207.1. NM_121711.4.
UniGene	At.27563.
3D structure databases
HSSP	HSSP built from PDB template 2C1X based on UniProtKB O22304.
ProteinModelPortal	Q9LFJ8.
SMR	Q9LFJ8. Positions 10-456.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT5G17050.1-P.
Protein family/group databases
CAZy	GT1. Glycosyltransferase Family 1.
Proteomic databases
PaxDb	Q9LFJ8.
PRIDE	Q9LFJ8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G17050.1; AT5G17050.1; AT5G17050.
GeneID	831568.
KEGG	ath:AT5G17050.
Organism-specific databases
TAIR	At5g17050.
Phylogenomic databases
eggNOG	COG1819.
HOGENOM	HOG000237564.
InParanoid	Q9LFJ8.
KO	K10757.
OMA	THAGWAS.
PhylomeDB	Q9LFJ8.
ProtClustDB	CLSN2686314.
Enzyme and pathway databases
UniPathway	UPA00154.
Gene expression databases
Genevestigator	Q9LFJ8.
Family and domain databases
InterPro	IPR002213. UDP_glucos_trans. [Graphical view]
PANTHER	PTHR11926. PTHR11926. 1 hit.
Pfam	PF00201. UDPGT. 1 hit. [Graphical view]
PROSITE	PS00375. UDPGT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

U78D2_ARATH

Accession

Primary (citable) accession number: Q9LFJ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 2007
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program