ID   U78D3_ARATH             Reviewed;         459 AA.
AC   Q9LFK0;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=UDP-glycosyltransferase 78D3;
DE            EC=2.4.1.-;
GN   Name=UGT78D3; OrderedLocusNames=At5g17030; ORFNames=F2K13.180;
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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].
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   [4]
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   [5]
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   [6]
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).
CC   -!- FUNCTION: Possesses low quercetin 3-O-glucosyltransferase activity in
CC       vitro. {ECO:0000269|PubMed:15352060}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AL391141; CAC01716.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED92375.1; -; Genomic_DNA.
DR   EMBL; AY088168; AAM65712.1; -; mRNA.
DR   PIR; T51558; T51558.
DR   RefSeq; NP_197205.1; NM_121709.2.
DR   AlphaFoldDB; Q9LFK0; -.
DR   SMR; Q9LFK0; -.
DR   STRING; 3702.AT5G17030.1; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   iPTMnet; Q9LFK0; -.
DR   PaxDb; Q9LFK0; -.
DR   PRIDE; Q9LFK0; -.
DR   ProteomicsDB; 243210; -.
DR   EnsemblPlants; AT5G17030.1; AT5G17030.1; AT5G17030.
DR   GeneID; 831566; -.
DR   Gramene; AT5G17030.1; AT5G17030.1; AT5G17030.
DR   KEGG; ath:AT5G17030; -.
DR   Araport; AT5G17030; -.
DR   TAIR; locus:2148231; AT5G17030.
DR   eggNOG; KOG1192; Eukaryota.
DR   HOGENOM; CLU_001724_0_2_1; -.
DR   InParanoid; Q9LFK0; -.
DR   OMA; CILTDAF; -.
DR   OrthoDB; 508327at2759; -.
DR   PhylomeDB; Q9LFK0; -.
DR   PRO; PR:Q9LFK0; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LFK0; baseline and differential.
DR   Genevisible; Q9LFK0; AT.
DR   GO; GO:0080059; F:flavonol 3-O-arabinosyltransferase activity; IMP:TAIR.
DR   GO; GO:0080043; F:quercetin 3-O-glucosyltransferase activity; IDA:TAIR.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   InterPro; IPR035595; UDP_glycos_trans_CS.
DR   Pfam; PF00201; UDPGT; 1.
DR   PROSITE; PS00375; UDPGT; 1.
PE   2: Evidence at transcript level;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..459
FT                   /note="UDP-glycosyltransferase 78D3"
FT                   /id="PRO_0000409105"
FT   BINDING         338..340
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         355..363
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         377..380
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   459 AA;  49967 MW;  506AC830C32DF4FA CRC64;
     MAKPSQPTRD SHVAVLVFPF GTHAAPLLAV TCRLATAAPS TVFSFFSTAR SNSSLLSSDI
     PTNIRVHNVD DGVPEGFVLT GNPQHAVELF LEAAPEIFRR EIKAAETEVG RKFKCILTDA
     FLWLAAETAA AEMKASWVAY YGGGATSLTA HLYTDAIREN VGVKEVGERM EETIGFISGM
     EKIRVKDTQE GVVFGNLDSV FSKTLHQMGL ALPRATAVFI NSFEELDPTF TNDFRSEFKR
     YLNIGPLALL SSPSQTSTLV HDPHGCLAWI EKRSTASVAY IAFGRVATPP PVELVAIAQG
     LESSKVPFVW SLQEMKMTHL PEGFLDRTRE QGMVVPWAPQ VELLNHEAMG VFVSHGGWNS
     VLESVSAGVP MICRPIFGDH AINARSVEAV WEIGVTISSG VFTKDGFEES LDRVLVQDDG
     KKMKVNAKKL EELAQEAVST KGSSFENFGG LLDEVVNFG