U73C6_ARATH
ID U73C6_ARATH Reviewed; 495 AA.
AC Q9ZQ95; Q8GYL0;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=UDP-glycosyltransferase 73C6;
DE EC=2.4.1.-;
DE AltName: Full=Flavonol-3-O-glycoside-7-O-glucosyltransferase 1;
DE AltName: Full=Zeatin O-glucosyltransferase 2;
GN Name=UGT73C6; Synonyms=ZOG2; OrderedLocusNames=At2g36790;
GN ORFNames=F13K3.19;
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 [GENOMIC DNA].
RA Martin R.C., Mok M.C., Mok D.W.S.;
RT "Arabidopsis genes encoding zeatin O-glucosyltransferases.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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, 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 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: Acts as a UDP-glucose:flavonol-3-O-glycoside-7-O-
CC glucosyltransferase. 6- and 7-hydroxyflavone, but not 3- or 5-
CC hydroxyflavone are accepted as substrates. Possesses low quercetin 3-O-
CC glucosyltransferase, 7-O-glucosyltransferase and 4'-O-
CC glucosyltransferase activities in vitro. {ECO:0000269|PubMed:12900416,
CC ECO:0000269|PubMed:15352060}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and flowers, and at a very low
CC level in roots. {ECO:0000269|PubMed:12900416}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally (Ref.1) thought to be a zeatin O-
CC glucosyltransferases and was named ZOG2. {ECO:0000305}.
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DR EMBL; AY573821; AAS87591.1; -; Genomic_DNA.
DR EMBL; AC006282; AAD20155.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09298.1; -; Genomic_DNA.
DR EMBL; AK117534; BAC42195.1; -; mRNA.
DR PIR; G84784; G84784.
DR RefSeq; NP_181217.1; NM_129234.2.
DR AlphaFoldDB; Q9ZQ95; -.
DR SMR; Q9ZQ95; -.
DR STRING; 3702.AT2G36790.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PaxDb; Q9ZQ95; -.
DR PRIDE; Q9ZQ95; -.
DR ProteomicsDB; 228615; -.
DR EnsemblPlants; AT2G36790.1; AT2G36790.1; AT2G36790.
DR GeneID; 818251; -.
DR Gramene; AT2G36790.1; AT2G36790.1; AT2G36790.
DR KEGG; ath:AT2G36790; -.
DR Araport; AT2G36790; -.
DR TAIR; locus:2040540; AT2G36790.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_2_2_1; -.
DR InParanoid; Q9ZQ95; -.
DR OMA; MSNIRIH; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q9ZQ95; -.
DR PRO; PR:Q9ZQ95; -.
DR Proteomes; UP000006548; Chromosome 2.
DR Genevisible; Q9ZQ95; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0080043; F:quercetin 3-O-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0080046; F:quercetin 4'-O-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0080044; F:quercetin 7-O-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0051555; P:flavonol biosynthetic process; 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..495
FT /note="UDP-glycosyltransferase 73C6"
FT /id="PRO_0000074158"
FT REGION 449..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 296
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 356..358
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 373..381
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 395..398
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT CONFLICT 61
FT /note="A -> T (in Ref. 4; BAC42195)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 495 AA; 55929 MW; 10AB8E66C332FA92 CRC64;
MAFEKNNEPF PLHFVLFPFM AQGHMIPMVD IARLLAQRGV LITIVTTPHN AARFKNVLNR
AIESGLPINL VQVKFPYQEA GLQEGQENMD LLTTMEQITS FFKAVNLLKE PVQNLIEEMS
PRPSCLISDM CLSYTSEIAK KFKIPKILFH GMGCFCLLCV NVLRKNREIL DNLKSDKEYF
IVPYFPDRVE FTRPQVPVET YVPAGWKEIL EDMVEADKTS YGVIVNSFQE LEPAYAKDFK
EARSGKAWTI GPVSLCNKVG VDKAERGNKS DIDQDECLEW LDSKEPGSVL YVCLGSICNL
PLSQLLELGL GLEESQRPFI WVIRGWEKYK ELVEWFSESG FEDRIQDRGL LIKGWSPQML
ILSHPSVGGF LTHCGWNSTL EGITAGLPML TWPLFADQFC NEKLVVQILK VGVSAEVKEV
MKWGEEEKIG VLVDKEGVKK AVEELMGESD DAKERRRRAK ELGESAHKAV EEGGSSHSNI
TFLLQDIMQL AQSNN
