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Protein

UDP-glycosyltransferase 89B1

Gene

UGT89B1

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

Functioni

Possesses quercetin 3-O-glucosyltransferase, 7-O-glucosyltransferase and 4'-O-glucosyltransferase activities in vitro. Also active in vitro on benzoates and benzoate derivatives.2 Publications

Catalytic activityi

UDP-glucose + a flavonol = UDP + a flavonol 3-O-D-glucoside.
UDP-glucose + a flavonol = UDP + a flavonol 7-O-D-glucoside.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei289 – 2891UDP-glucoseBy similarity

GO - Molecular functioni

  1. flavonol 3-O-glucosyltransferase activity Source: UniProtKB-EC
  2. quercetin 3-O-glucosyltransferase activity Source: TAIR
  3. quercetin 4'-O-glucosyltransferase activity Source: TAIR
  4. quercetin 7-O-glucosyltransferase activity Source: TAIR
  5. UDP-glucosyltransferase activity Source: TAIR

GO - Biological processi

  1. flavonoid biosynthetic process Source: GO_Central
  2. flavonoid glucuronidation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Protein family/group databases

CAZyiGT1. Glycosyltransferase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-glycosyltransferase 89B1 (EC:2.4.1.-)
Alternative name(s):
Flavonol 3-O-glucosyltransferase UGT89B1 (EC:2.4.1.91)
Flavonol 7-O-glucosyltransferase UGT89B1
Gene namesi
Name:UGT89B1
Ordered Locus Names:At1g73880
ORF Names:F2P9.25
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G73880.

Subcellular locationi

GO - Cellular componenti

  1. intracellular membrane-bounded organelle Source: GO_Central
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473UDP-glycosyltransferase 89B1PRO_0000409137Add
BLAST

Proteomic databases

PaxDbiQ9C9B0.
PRIDEiQ9C9B0.

Expressioni

Gene expression databases

GenevestigatoriQ9C9B0.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT1G73880.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9C9B0.
SMRiQ9C9B0. Positions 12-468.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni348 – 3503UDP-glucose bindingBy similarity
Regioni365 – 3739UDP-glucose bindingBy similarity
Regioni387 – 3904UDP-glucose bindingBy similarity

Sequence similaritiesi

Belongs to the UDP-glycosyltransferase family.Curated

Phylogenomic databases

eggNOGiNOG265147.
HOGENOMiHOG000237565.
InParanoidiQ9C9B0.
OMAiVAMLAWP.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q9C9B0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVNEENNKP TKTHVLIFPF PAQGHMIPLL DFTHRLALRG GAALKITVLV
60 70 80 90 100
TPKNLPFLSP LLSAVVNIEP LILPFPSHPS IPSGVENVQD LPPSGFPLMI
110 120 130 140 150
HALGNLHAPL ISWITSHPSP PVAIVSDFFL GWTKNLGIPR FDFSPSAAIT
160 170 180 190 200
CCILNTLWIE MPTKINEDDD NEILHFPKIP NCPKYRFDQI SSLYRSYVHG
210 220 230 240 250
DPAWEFIRDS FRDNVASWGL VVNSFTAMEG VYLEHLKREM GHDRVWAVGP
260 270 280 290 300
IIPLSGDNRG GPTSVSVDHV MSWLDAREDN HVVYVCFGSQ VVLTKEQTLA
310 320 330 340 350
LASGLEKSGV HFIWAVKEPV EKDSTRGNIL DGFDDRVAGR GLVIRGWAPQ
360 370 380 390 400
VAVLRHRAVG AFLTHCGWNS VVEAVVAGVL MLTWPMRADQ YTDASLVVDE
410 420 430 440 450
LKVGVRACEG PDTVPDPDEL ARVFADSVTG NQTERIKAVE LRKAALDAIQ
460 470
ERGSSVNDLD GFIQHVVSLG LNK
Length:473
Mass (Da):52,106
Last modified:May 31, 2011 - v2
Checksum:i293587240C506F6A
GO

Sequence cautioni

The sequence AAG52529.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAM12962.1 differs from that shown. Reason: Frameshift at position 8. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC016662 Genomic DNA. Translation: AAG52529.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE35520.1.
AY092963 mRNA. Translation: AAM12962.1. Frameshift.
BT006596 mRNA. Translation: AAP31940.1.
PIRiD96766.
RefSeqiNP_177529.2. NM_106048.3.
UniGeneiAt.43757.

Genome annotation databases

EnsemblPlantsiAT1G73880.1; AT1G73880.1; AT1G73880.
GeneIDi843725.
KEGGiath:AT1G73880.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC016662 Genomic DNA. Translation: AAG52529.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE35520.1.
AY092963 mRNA. Translation: AAM12962.1. Frameshift.
BT006596 mRNA. Translation: AAP31940.1.
PIRiD96766.
RefSeqiNP_177529.2. NM_106048.3.
UniGeneiAt.43757.

3D structure databases

ProteinModelPortaliQ9C9B0.
SMRiQ9C9B0. Positions 12-468.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT1G73880.1-P.

Protein family/group databases

CAZyiGT1. Glycosyltransferase Family 1.

Proteomic databases

PaxDbiQ9C9B0.
PRIDEiQ9C9B0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G73880.1; AT1G73880.1; AT1G73880.
GeneIDi843725.
KEGGiath:AT1G73880.

Organism-specific databases

TAIRiAT1G73880.

Phylogenomic databases

eggNOGiNOG265147.
HOGENOMiHOG000237565.
InParanoidiQ9C9B0.
OMAiVAMLAWP.

Gene expression databases

GenevestigatoriQ9C9B0.

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. "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.

Entry informationi

Entry nameiU89B1_ARATH
AccessioniPrimary (citable) accession number: Q9C9B0
Secondary accession number(s): Q8RWP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: May 31, 2011
Last modified: February 4, 2015
This is version 70 of the entry and version 2 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

External Data

Dasty 3

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 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.