U76C2_ARATH
ID U76C2_ARATH Reviewed; 450 AA.
AC Q9FIA0;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=UDP-glycosyltransferase 76C2;
DE EC=2.4.1.-;
DE AltName: Full=Cytokinin-N-glucosyltransferase 2;
GN Name=UGT76C2; OrderedLocusNames=At5g05860; ORFNames=MJJ3.28;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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, 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=0.22 mM for trans-zeatin (at 30 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:15342621};
CC KM=0.22 mM for dihydrozeatin (at 30 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:15342621};
CC KM=0.07 mM for N6-isopentenyladenine (at 30 degrees Celsius and pH
CC 7.0) {ECO:0000269|PubMed:15342621};
CC KM=0.04 mM for N6-benzyladenine (at 30 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:15342621};
CC KM=0.07 mM for kinetin (at 30 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:15342621};
CC Vmax=5.91 nmol/sec/mg enzyme with trans-zeatin as substrate
CC {ECO:0000269|PubMed:15342621};
CC Vmax=10.78 nmol/sec/mg enzyme with dihydrozeatin as substrate
CC {ECO:0000269|PubMed:15342621};
CC Vmax=10.42 nmol/sec/mg enzyme with N6-isopentenyladenine as substrate
CC {ECO:0000269|PubMed:15342621};
CC Vmax=7.90 nmol/sec/mg enzyme with N6-benzyladenine as substrate
CC {ECO:0000269|PubMed:15342621};
CC Vmax=3.63 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}.
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DR EMBL; AB017060; BAB10791.1; -; Genomic_DNA.
DR EMBL; AB005237; BAB10791.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED90933.1; -; Genomic_DNA.
DR EMBL; AY045617; AAK73975.1; -; mRNA.
DR EMBL; AY143896; AAN28835.1; -; mRNA.
DR RefSeq; NP_196205.1; NM_120668.4.
DR AlphaFoldDB; Q9FIA0; -.
DR SMR; Q9FIA0; -.
DR STRING; 3702.AT5G05860.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PaxDb; Q9FIA0; -.
DR PRIDE; Q9FIA0; -.
DR ProteomicsDB; 228591; -.
DR EnsemblPlants; AT5G05860.1; AT5G05860.1; AT5G05860.
DR GeneID; 830471; -.
DR Gramene; AT5G05860.1; AT5G05860.1; AT5G05860.
DR KEGG; ath:AT5G05860; -.
DR Araport; AT5G05860; -.
DR TAIR; locus:2166444; AT5G05860.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_0_0_1; -.
DR InParanoid; Q9FIA0; -.
DR OMA; ICGSPFR; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q9FIA0; -.
DR BioCyc; MetaCyc:AT5G05860-MON; -.
DR BRENDA; 2.4.1.118; 399.
DR BRENDA; 2.4.1.203; 399.
DR SABIO-RK; Q9FIA0; -.
DR PRO; PR:Q9FIA0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIA0; baseline and differential.
DR Genevisible; Q9FIA0; 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 GO; GO:1901527; P:abscisic acid-activated signaling pathway involved in stomatal movement; IMP:TAIR.
DR GO; GO:0042631; P:cellular response to water deprivation; IMP:TAIR.
DR GO; GO:0009690; P:cytokinin metabolic process; IMP:TAIR.
DR GO; GO:1900000; P:regulation of anthocyanin catabolic process; IMP:TAIR.
DR GO; GO:0048316; P:seed development; IMP: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..450
FT /note="UDP-glycosyltransferase 76C2"
FT /id="PRO_0000074154"
FT BINDING 272
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 331..333
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 348..356
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 370..373
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
SQ SEQUENCE 450 AA; 50425 MW; B04568214C4CC857 CRC64;
MEEKRNGLRV ILFPLPLQGC INPMLQLANI LHVRGFSITV IHTRFNAPKA SSHPLFTFLQ
IPDGLSETEI QDGVMSLLAQ INLNAESPFR DCLRKVLLES KESERVTCLI DDCGWLFTQS
VSESLKLPRL VLCTFKATFF NAYPSLPLIR TKGYLPVSES EAEDSVPEFP PLQKRDLSKV
FGEFGEKLDP FLHAVVETTI RSSGLIYMSC EELEKDSLTL SNEIFKVPVF AIGPFHSYFS
ASSSSLFTQD ETCILWLDDQ EDKSVIYVSL GSVVNITETE FLEIACGLSN SKQPFLWVVR
PGSVLGAKWI EPLSEGLVSS LEEKGKIVKW APQQEVLAHR ATGGFLTHNG WNSTLESICE
GVPMICLPGG WDQMLNSRFV SDIWKIGIHL EGRIEKKEIE KAVRVLMEES EGNKIRERMK
VLKDEVEKSV KQGGSSFQSI ETLANHILLL
