U73C5_ARATH
ID U73C5_ARATH Reviewed; 495 AA.
AC Q9ZQ94;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=UDP-glycosyltransferase 73C5;
DE EC=2.4.1.-;
DE AltName: Full=Cytokinin-O-glucosyltransferase 3;
DE AltName: Full=Deoxynivalenol-glucosyl-transferase 1;
DE AltName: Full=Zeatin O-glucosyltransferase 3;
DE Short=AtZOG3;
GN Name=UGT73C5; Synonyms=DOGT1, ZOG3; OrderedLocusNames=At2g36800;
GN ORFNames=F13K3.20;
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=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 [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, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=12970342; DOI=10.1074/jbc.m307552200;
RA Poppenberger B., Berthiller F., Lucyshyn D., Sieberer T., Schuhmacher R.,
RA Krska R., Kuchler K., Gloessl J., Luschnig C., Adam G.;
RT "Detoxification of the Fusarium mycotoxin deoxynivalenol by a UDP-
RT glucosyltransferase from Arabidopsis thaliana.";
RL J. Biol. Chem. 278:47905-47914(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 CLASSIFICATION, AND NOMENCLATURE.
RX PubMed=15241472; DOI=10.1038/sj.emboj.7600295;
RA Lim E.K., Bowles D.J.;
RT "A class of plant glycosyltransferases involved in cellular homeostasis.";
RL EMBO J. 23:2915-2922(2004).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=15342621; DOI=10.1074/jbc.m409569200;
RA Hou B., Lim E.-K., Higgins G.S., Bowles D.J.;
RT "N-glucosylation of cytokinins by glycosyltransferases of Arabidopsis
RT thaliana.";
RL J. Biol. Chem. 279:47822-47832(2004).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16214889; DOI=10.1073/pnas.0504279102;
RA Poppenberger B., Fujioka S., Soeno K., George G.L., Vaistij F.E.,
RA Hiranuma S., Seto H., Takatsuto S., Adam G., Yoshida S., Bowles D.;
RT "The UGT73C5 of Arabidopsis thaliana glucosylates brassinosteroids.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:15253-15258(2005).
CC -!- FUNCTION: Specifically catalyzes 23-O-glucosylation of
CC brassinosteroids, resulting probably in their inactivation. Also,
CC involved in the O-glucosylation of trans-zeatin and dihydrozeatin.
CC Active in vitro on cis-zeatin, dihydrozeatin-9-N-Glc, and olomoucine.
CC Also involved in the detoxification of the Fusarium mycotoxin
CC deoxynivalenol by the transfer of glucose from UDP-glucose to the
CC hydroxyl group at C-3. Possesses low quercetin 7-O-glucosyltransferase
CC and 4'-O-glucosyltransferase activities in vitro.
CC {ECO:0000269|PubMed:12970342, ECO:0000269|PubMed:15342621,
CC ECO:0000269|PubMed:15352060, ECO:0000269|PubMed:16214889}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Elongating hypocotyls and root-specific. Expressed
CC in the vascular system, in meristematic tissues of the root tip, and in
CC the vasculature of the hypocotyl right after germination. In late stage
CC of flower development, expressed in petals, and in abscission zones.
CC {ECO:0000269|PubMed:12970342, ECO:0000269|PubMed:16214889}.
CC -!- INDUCTION: Rapidly induced in response to deoxynivalenol exposure. Weak
CC induction by salicylic acid, jasmonic acid and 1-
CC aminocyclopropylcarbonic acid (ACC) treatments. Not induced by
CC cytokinin treatment. {ECO:0000269|PubMed:12970342,
CC ECO:0000269|PubMed:15342621}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AY573822; AAS87592.1; -; Genomic_DNA.
DR EMBL; AC006282; AAD20156.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09299.1; -; Genomic_DNA.
DR EMBL; AY062743; AAL32821.1; -; mRNA.
DR EMBL; BT003373; AAO30036.1; -; mRNA.
DR PIR; H84784; H84784.
DR RefSeq; NP_181218.1; NM_129235.4.
DR AlphaFoldDB; Q9ZQ94; -.
DR SMR; Q9ZQ94; -.
DR STRING; 3702.AT2G36800.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR iPTMnet; Q9ZQ94; -.
DR PaxDb; Q9ZQ94; -.
DR PRIDE; Q9ZQ94; -.
DR ProteomicsDB; 243204; -.
DR EnsemblPlants; AT2G36800.1; AT2G36800.1; AT2G36800.
DR GeneID; 818252; -.
DR Gramene; AT2G36800.1; AT2G36800.1; AT2G36800.
DR KEGG; ath:AT2G36800; -.
DR Araport; AT2G36800; -.
DR TAIR; locus:2040570; AT2G36800.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_2_2_1; -.
DR InParanoid; Q9ZQ94; -.
DR OMA; WKAIMEP; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q9ZQ94; -.
DR BioCyc; ARA:AT2G36800-MON; -.
DR BioCyc; MetaCyc:AT2G36800-MON; -.
DR BRENDA; 2.4.1.203; 399.
DR PRO; PR:Q9ZQ94; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZQ94; baseline and differential.
DR Genevisible; Q9ZQ94; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0050502; F:cis-zeatin O-beta-D-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0046527; F: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:0050403; F:trans-zeatin O-beta-D-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016131; P:brassinosteroid metabolic process; IDA:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0098754; P:detoxification; IDA:UniProtKB.
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; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..495
FT /note="UDP-glycosyltransferase 73C5"
FT /id="PRO_0000074157"
FT TRANSMEM 146..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 446..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..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"
SQ SEQUENCE 495 AA; 55798 MW; AAC9727F48C069A9 CRC64;
MVSETTKSSP LHFVLFPFMA QGHMIPMVDI ARLLAQRGVI ITIVTTPHNA ARFKNVLNRA
IESGLPINLV QVKFPYLEAG LQEGQENIDS LDTMERMIPF FKAVNFLEEP VQKLIEEMNP
RPSCLISDFC LPYTSKIAKK FNIPKILFHG MGCFCLLCMH VLRKNREILD NLKSDKELFT
VPDFPDRVEF TRTQVPVETY VPAGDWKDIF DGMVEANETS YGVIVNSFQE LEPAYAKDYK
EVRSGKAWTI GPVSLCNKVG ADKAERGNKS DIDQDECLKW LDSKKHGSVL YVCLGSICNL
PLSQLKELGL GLEESQRPFI WVIRGWEKYK ELVEWFSESG FEDRIQDRGL LIKGWSPQML
ILSHPSVGGF LTHCGWNSTL EGITAGLPLL TWPLFADQFC NEKLVVEVLK AGVRSGVEQP
MKWGEEEKIG VLVDKEGVKK AVEELMGESD DAKERRRRAK ELGDSAHKAV EEGGSSHSNI
SFLLQDIMEL AEPNN
