U78D1_ARATH
ID U78D1_ARATH Reviewed; 453 AA.
AC Q9S9P6; Q8LAI9;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Flavonol-3-O-rhamnosyltransferase {ECO:0000305};
DE EC=2.4.1.- {ECO:0000269|PubMed:12900416, ECO:0000269|PubMed:23549747};
DE AltName: Full=UDP-glycosyltransferase 78D1 {ECO:0000303|PubMed:11042215};
DE AltName: Full=UDP-rhamnose:flavonol 3-O-glucoside rhamnosyltransferase {ECO:0000305};
GN Name=UGT78D1 {ECO:0000303|PubMed:11042215};
GN OrderedLocusNames=At1g30530 {ECO:0000312|Araport:AT1G30530};
GN ORFNames=F26G16.15 {ECO:0000312|EMBL:AAF19756.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY.
RX PubMed=11042215; DOI=10.1074/jbc.m007447200;
RA Li Y., Baldauf S., Lim E.K., Bowles D.J.;
RT "Phylogenetic analysis of the UDP-glycosyltransferase multigene family of
RT Arabidopsis thaliana.";
RL J. Biol. Chem. 276:4338-4343(2001).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=12900416; DOI=10.1074/jbc.m303523200;
RA Jones P., Messner B., Nakajima J., Schaffner A.R., Saito K.;
RT "UGT73C6 and UGT78D1, glycosyltransferases involved in flavonol glycoside
RT biosynthesis in Arabidopsis thaliana.";
RL J. Biol. Chem. 278:43910-43918(2003).
RN [7]
RP FUNCTION.
RX PubMed=15352060; DOI=10.1002/bit.20154;
RA Lim E.K., Ashford D.A., Hou B., Jackson R.G., Bowles D.J.;
RT "Arabidopsis glycosyltransferases as biocatalysts in fermentation for
RT regioselective synthesis of diverse quercetin glucosides.";
RL Biotechnol. Bioeng. 87:623-631(2004).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23549747; DOI=10.1007/s00253-013-4844-7;
RA Kim H.J., Kim B.G., Ahn J.H.;
RT "Regioselective synthesis of flavonoid bisglycosides using Escherichia coli
RT harboring two glycosyltransferases.";
RL Appl. Microbiol. Biotechnol. 97:5275-5282(2013).
RN [9]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=23473981; DOI=10.1016/j.plaphy.2013.02.001;
RA Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M.,
RA Tohge T., Fernie A.R.;
RT "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic
RT diversity.";
RL Plant Physiol. Biochem. 72:21-34(2013).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=24251900; DOI=10.1111/nph.12558;
RA Yin R., Han K., Heller W., Albert A., Dobrev P.I., Zazimalova E.,
RA Schaeffner A.R.;
RT "Kaempferol 3-O-rhamnoside-7-O-rhamnoside is an endogenous flavonol
RT inhibitor of polar auxin transport in Arabidopsis shoots.";
RL New Phytol. 201:466-475(2014).
CC -!- FUNCTION: Flavonol 3-O-rhamnosyltransferase that catalyzes the transfer
CC of rhamnose from UDP-rhamnose to the 3-OH position of kaempferol and
CC quercetin (PubMed:12900416, PubMed:15352060, PubMed:23549747,
CC PubMed:24251900). Possesses low quercetin 3-O-glucosyltransferase
CC activity in vitro (PubMed:12900416). {ECO:0000269|PubMed:12900416,
CC ECO:0000269|PubMed:15352060, ECO:0000269|PubMed:23549747,
CC ECO:0000269|PubMed:24251900}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=kaempferol + UDP-beta-L-rhamnose = H(+) + kaempferol 3-O-
CC alpha-L-rhamnoside + UDP; Xref=Rhea:RHEA:61164, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58573, ChEBI:CHEBI:83836,
CC ChEBI:CHEBI:144433; Evidence={ECO:0000269|PubMed:12900416,
CC ECO:0000269|PubMed:23549747};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61165;
CC Evidence={ECO:0000269|PubMed:12900416, ECO:0000269|PubMed:23549747};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=quercetin + UDP-beta-L-rhamnose = H(+) + quercitrin + UDP;
CC Xref=Rhea:RHEA:61160, ChEBI:CHEBI:15378, ChEBI:CHEBI:57694,
CC ChEBI:CHEBI:58192, ChEBI:CHEBI:58223, ChEBI:CHEBI:83836;
CC Evidence={ECO:0000269|PubMed:12900416, ECO:0000269|PubMed:23549747};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61161;
CC Evidence={ECO:0000269|PubMed:12900416, ECO:0000269|PubMed:23549747};
CC -!- PATHWAY: Flavonoid metabolism. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, flowers, siliques, and stems
CC (PubMed:12900416). Expressed in the shoot apex (PubMed:24251900).
CC {ECO:0000269|PubMed:12900416, ECO:0000269|PubMed:24251900}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants exhibit altered flavonol glycoside
CC patter. {ECO:0000269|PubMed:24251900}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AC009917; AAF19756.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31240.1; -; Genomic_DNA.
DR EMBL; AY056312; AAL07161.1; -; mRNA.
DR EMBL; AF360160; AAK25870.1; -; mRNA.
DR EMBL; AY087785; AAM65321.1; -; mRNA.
DR PIR; D86430; D86430.
DR RefSeq; NP_564357.1; NM_102790.4.
DR AlphaFoldDB; Q9S9P6; -.
DR SMR; Q9S9P6; -.
DR BioGRID; 25168; 3.
DR IntAct; Q9S9P6; 1.
DR STRING; 3702.AT1G30530.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PaxDb; Q9S9P6; -.
DR PRIDE; Q9S9P6; -.
DR ProteomicsDB; 242619; -.
DR EnsemblPlants; AT1G30530.1; AT1G30530.1; AT1G30530.
DR GeneID; 839933; -.
DR Gramene; AT1G30530.1; AT1G30530.1; AT1G30530.
DR KEGG; ath:AT1G30530; -.
DR Araport; AT1G30530; -.
DR TAIR; locus:2028190; AT1G30530.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_0_2_1; -.
DR InParanoid; Q9S9P6; -.
DR OMA; NEMRERT; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q9S9P6; -.
DR BioCyc; ARA:AT1G30530-MON; -.
DR BioCyc; MetaCyc:AT1G30530-MON; -.
DR PRO; PR:Q9S9P6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S9P6; baseline and differential.
DR Genevisible; Q9S9P6; AT.
DR GO; GO:0080043; F:quercetin 3-O-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IDA:TAIR.
DR GO; GO:0103059; F:UDP-L-rhamnose:kaempferol 3-O-rhamnosyltransferase activity; IEA:RHEA.
DR GO; GO:0102824; F:UDP-L-rhamnose:quercetin 3-O-rhamnosyltransferase activity; IEA:RHEA.
DR GO; GO:0051555; P:flavonol biosynthetic process; IDA:TAIR.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR InterPro; IPR002213; UDP_glucos_trans.
DR Pfam; PF00201; UDPGT; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..453
FT /note="Flavonol-3-O-rhamnosyltransferase"
FT /id="PRO_0000074159"
FT BINDING 24
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9LNE6"
FT BINDING 280
FT /ligand="UDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:83836"
FT /evidence="ECO:0000250|UniProtKB:Q9LNE6"
FT BINDING 332..335
FT /ligand="UDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:83836"
FT /evidence="ECO:0000250|UniProtKB:Q9LNE6"
FT BINDING 350..358
FT /ligand="UDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:83836"
FT /evidence="ECO:0000250|UniProtKB:Q9LNE6"
FT BINDING 374..375
FT /ligand="UDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:83836"
FT /evidence="ECO:0000250|UniProtKB:Q9LNE6"
FT CONFLICT 330
FT /note="V -> D (in Ref. 4; AAM65321)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="Q -> H (in Ref. 4; AAM65321)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="L -> F (in Ref. 4; AAM65321)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="I -> V (in Ref. 4; AAM65321)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 453 AA; 50095 MW; 2CCE13AFFEF54E77 CRC64;
MTKFSEPIRD SHVAVLAFFP VGAHAGPLLA VTRRLAAASP STIFSFFNTA RSNASLFSSD
HPENIKVHDV SDGVPEGTML GNPLEMVELF LEAAPRIFRS EIAAAEIEVG KKVTCMLTDA
FFWFAADIAA ELNATWVAFW AGGANSLCAH LYTDLIRETI GLKDVSMEET LGFIPGMENY
RVKDIPEEVV FEDLDSVFPK ALYQMSLALP RASAVFISSF EELEPTLNYN LRSKLKRFLN
IAPLTLLSST SEKEMRDPHG CFAWMGKRSA ASVAYISFGT VMEPPPEELV AIAQGLESSK
VPFVWSLKEK NMVHLPKGFL DRTREQGIVV PWAPQVELLK HEAMGVNVTH CGWNSVLESV
SAGVPMIGRP ILADNRLNGR AVEVVWKVGV MMDNGVFTKE GFEKCLNDVF VHDDGKTMKA
NAKKLKEKLQ EDFSMKGSSL ENFKILLDEI VKV
