U76C1_ARATH
ID U76C1_ARATH Reviewed; 464 AA.
AC Q9FI99; Q0WRJ5;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=UDP-glycosyltransferase 76C1;
DE EC=2.4.1.-;
DE AltName: Full=Cytokinin-N-glucosyltransferase 1;
GN Name=UGT76C1; OrderedLocusNames=At5g05870; ORFNames=K18J17.2;
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=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
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].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) 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, AND BIOPHYSICOCHEMICAL PROPERTIES.
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).
CC -!- FUNCTION: Involved in the N-glucosylation of cytokinins. Catalyzes the
CC formation of both the 7-N and the 9-N-glucosides.
CC {ECO:0000269|PubMed:15342621}.
CC -!- ACTIVITY REGULATION: Inhibited by olomoucine and 3-isobutyl-1-
CC methylxanthine.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.24 mM for trans-zeatin (at 30 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:15342621};
CC KM=0.16 mM for dihydrozeatin (at 30 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:15342621};
CC KM=0.13 mM for N6-isopentenyladenine (at 30 degrees Celsius and pH
CC 7.0) {ECO:0000269|PubMed:15342621};
CC KM=0.09 mM for N6-benzyladenine (at 30 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:15342621};
CC KM=0.21 mM for kinetin (at 30 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:15342621};
CC Vmax=4.06 nmol/sec/mg enzyme with trans-zeatin as substrate
CC {ECO:0000269|PubMed:15342621};
CC Vmax=6.34 nmol/sec/mg enzyme with dihydrozeatin as substrate
CC {ECO:0000269|PubMed:15342621};
CC Vmax=18.67 nmol/sec/mg enzyme with N6-isopentenyladenine as substrate
CC {ECO:0000269|PubMed:15342621};
CC Vmax=15.93 nmol/sec/mg enzyme with N6-benzyladenine as substrate
CC {ECO:0000269|PubMed:15342621};
CC Vmax=9.40 nmol/sec/mg enzyme with kinetin as substrate
CC {ECO:0000269|PubMed:15342621};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:15342621};
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB017060; BAB10792.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90934.1; -; Genomic_DNA.
DR EMBL; BT006473; AAP21281.1; -; mRNA.
DR EMBL; AK228311; BAF00254.1; -; mRNA.
DR RefSeq; NP_196206.1; NM_120669.4.
DR AlphaFoldDB; Q9FI99; -.
DR SMR; Q9FI99; -.
DR STRING; 3702.AT5G05870.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PaxDb; Q9FI99; -.
DR PRIDE; Q9FI99; -.
DR ProteomicsDB; 228647; -.
DR EnsemblPlants; AT5G05870.1; AT5G05870.1; AT5G05870.
DR GeneID; 830472; -.
DR Gramene; AT5G05870.1; AT5G05870.1; AT5G05870.
DR KEGG; ath:AT5G05870; -.
DR Araport; AT5G05870; -.
DR TAIR; locus:2153614; AT5G05870.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_0_0_1; -.
DR InParanoid; Q9FI99; -.
DR OMA; SVHGRDW; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q9FI99; -.
DR BioCyc; MetaCyc:AT5G05870-MON; -.
DR BRENDA; 2.4.1.118; 399.
DR BRENDA; 2.4.1.203; 399.
DR SABIO-RK; Q9FI99; -.
DR PRO; PR:Q9FI99; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FI99; baseline and differential.
DR Genevisible; Q9FI99; AT.
DR GO; GO:0047807; F:cytokinin 7-beta-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0080062; F:cytokinin 9-beta-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0080043; F:quercetin 3-O-glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0080044; F:quercetin 7-O-glucosyltransferase activity; IBA:GO_Central.
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..464
FT /note="UDP-glycosyltransferase 76C1"
FT /id="PRO_0000074153"
FT BINDING 279
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
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 464 AA; 52360 MW; 522E2121F643896D CRC64;
MEKRNERQVI LFPLPLQGCI NPMLQLAKIL YSRGFSITII HTRFNAPKSS DHPLFTFLQI
RDGLSESQTQ SRDLLLQLTL LNNNCQIPFR ECLAKLIKPS SDSGTEDRKI SCVIDDSGWV
FTQSVAESFN LPRFVLCAYK FSFFLGHFLV PQIRREGFLP VPDSEADDLV PEFPPLRKKD
LSRIMGTSAQ SKPLDAYLLK ILDATKPASG IIVMSCKELD HDSLAESNKV FSIPIFPIGP
FHIHDVPASS SSLLEPDQSC IPWLDMRETR SVVYVSLGSI ASLNESDFLE IACGLRNTNQ
SFLWVVRPGS VHGRDWIESL PSGFMESLDG KGKIVRWAPQ LDVLAHRATG GFLTHNGWNS
TLESICEGVP MICLPCKWDQ FVNARFISEV WRVGIHLEGR IERREIERAV IRLMVESKGE
EIRGRIKVLR DEVRRSVKQG GSSYRSLDEL VDRISIIIEP LVPT
