U72E2_ARATH
ID U72E2_ARATH Reviewed; 481 AA.
AC Q9LVR1; Q8LEG2;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=UDP-glycosyltransferase 72E2 {ECO:0000303|PubMed:11042215};
DE EC=2.4.1.111 {ECO:0000269|PubMed:11042211, ECO:0000269|PubMed:15907484, ECO:0000269|PubMed:16995900, ECO:0000269|PubMed:21149736, ECO:0000269|PubMed:24667164};
DE AltName: Full=Hydroxycinnamate 4-beta-glucosyltransferase UGT72E2 {ECO:0000305};
DE EC=2.4.1.126 {ECO:0000269|PubMed:11042211, ECO:0000269|PubMed:15907484, ECO:0000269|PubMed:16995900, ECO:0000269|PubMed:21149736, ECO:0000269|PubMed:24667164};
GN Name=UGT72E2 {ECO:0000303|PubMed:11042215};
GN OrderedLocusNames=At5g66690 {ECO:0000312|Araport:AT5G66690};
GN ORFNames=MSN2.8 {ECO:0000312|EMBL:BAA97275.1};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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].
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].
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 [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, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11042211; DOI=10.1074/jbc.m007263200;
RA Lim E.K., Li Y., Parr A., Jackson R., Ashford D.A., Bowles D.J.;
RT "Identification of glucosyltransferase genes involved in sinapate
RT metabolism and lignin synthesis in Arabidopsis.";
RL J. Biol. Chem. 276:4344-4349(2001).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12721858; DOI=10.1007/s00425-002-0969-0;
RA Messner B., Thulke O., Schaeffner A.R.;
RT "Arabidopsis glucosyltransferases with activities toward both endogenous
RT and xenobiotic substrates.";
RL Planta 217:138-146(2003).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15907484; DOI=10.1016/j.febslet.2005.04.016;
RA Lim E.K., Jackson R.G., Bowles D.J.;
RT "Identification and characterisation of Arabidopsis glycosyltransferases
RT capable of glucosylating coniferyl aldehyde and sinapyl aldehyde.";
RL FEBS Lett. 579:2802-2806(2005).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=16995900; DOI=10.1111/j.1365-313x.2006.02872.x;
RA Lanot A., Hodge D., Jackson R.G., George G.L., Elias L., Lim E.K.,
RA Vaistij F.E., Bowles D.J.;
RT "The glucosyltransferase UGT72E2 is responsible for monolignol 4-O-
RT glucoside production in Arabidopsis thaliana.";
RL Plant J. 48:286-295(2006).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21149736; DOI=10.1073/pnas.1007747108;
RA Miao Y.C., Liu C.J.;
RT "ATP-binding cassette-like transporters are involved in the transport of
RT lignin precursors across plasma and vacuolar membranes.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:22728-22733(2010).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24667164; DOI=10.1016/j.phytochem.2014.03.003;
RA Chu Y., Kwon T., Nam J.;
RT "Enzymatic and metabolic engineering for efficient production of syringin,
RT sinapyl alcohol 4-O-glucoside, in Arabidopsis thaliana.";
RL Phytochemistry 102:55-63(2014).
CC -!- FUNCTION: Involved in the O-glucosylation of monolignols (alcohol
CC monomers of lignin) (PubMed:11042211, PubMed:15907484, PubMed:16995900,
CC PubMed:21149736, PubMed:24667164). Glucosylates coniferyl alcohol to
CC form coniferyl alcohol 4-O-glucoside (PubMed:11042211, PubMed:15907484,
CC PubMed:16995900, PubMed:21149736, PubMed:24667164). Glucosylates
CC sinapyl alcohol to form sinapyl alcohol 4-O-glucoside (PubMed:11042211,
CC PubMed:12721858, PubMed:15907484, PubMed:21149736, PubMed:24667164).
CC Glucosylates coniferyl aldehyde to form coniferyl aldehyde 4-O-
CC glucoside (PubMed:15907484). Glucosylates sinapyl aldehyde to form
CC sinapyl aldehyde 4-O-glucoside (PubMed:15907484). Possesses low
CC activity with sinapate and ferulate as substrates (PubMed:11042211,
CC PubMed:15907484). {ECO:0000269|PubMed:11042211,
CC ECO:0000269|PubMed:12721858, ECO:0000269|PubMed:15907484,
CC ECO:0000269|PubMed:16995900, ECO:0000269|PubMed:21149736,
CC ECO:0000269|PubMed:24667164}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-coumarate + UDP-alpha-D-glucose = 4-O-(beta-D-glucosyl)-
CC trans-4-coumarate + H(+) + UDP; Xref=Rhea:RHEA:21636,
CC ChEBI:CHEBI:12876, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:79066; EC=2.4.1.126;
CC Evidence={ECO:0000269|PubMed:11042211, ECO:0000269|PubMed:15907484,
CC ECO:0000269|PubMed:16995900, ECO:0000269|PubMed:21149736,
CC ECO:0000269|PubMed:24667164};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-coniferol + UDP-alpha-D-glucose = 4-O-(beta-D-glucosyl)-
CC trans-coniferol + H(+) + UDP; Xref=Rhea:RHEA:23944,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16220, ChEBI:CHEBI:17745,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.111;
CC Evidence={ECO:0000269|PubMed:11042211, ECO:0000269|PubMed:15907484,
CC ECO:0000269|PubMed:16995900, ECO:0000269|PubMed:21149736,
CC ECO:0000269|PubMed:24667164};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-sinapyl alcohol + UDP-alpha-D-glucose = 4-O-(beta-D-
CC glucosyl)-trans-4-sinapoyl alcohol + H(+) + UDP;
CC Xref=Rhea:RHEA:57460, ChEBI:CHEBI:9380, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:64557;
CC Evidence={ECO:0000269|PubMed:11042211, ECO:0000269|PubMed:12721858,
CC ECO:0000269|PubMed:15907484, ECO:0000269|PubMed:16995900,
CC ECO:0000269|PubMed:21149736, ECO:0000269|PubMed:24667164};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=E-sinapate + UDP-alpha-D-glucose = 4-O-(beta-D-glucosyl)-
CC trans-sinapate + H(+) + UDP; Xref=Rhea:RHEA:57456, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30023, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:141763; Evidence={ECO:0000269|PubMed:11042211};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-coniferaldehyde + UDP-alpha-D-glucose = 4-O-(beta-D-
CC glucosyl)-4-trans-coniferyl aldehyde + H(+) + UDP;
CC Xref=Rhea:RHEA:57708, ChEBI:CHEBI:15378, ChEBI:CHEBI:16547,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:136949;
CC Evidence={ECO:0000269|PubMed:15907484};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-sinapaldehyde + UDP-alpha-D-glucose = 4-O-(beta-D-
CC glucosyl)-4-trans-sinapoyl aldehyde + H(+) + UDP;
CC Xref=Rhea:RHEA:57712, ChEBI:CHEBI:15378, ChEBI:CHEBI:27949,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:142126;
CC Evidence={ECO:0000269|PubMed:15907484};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20 uM for coniferyl aldehyde {ECO:0000269|PubMed:15907484};
CC KM=20 uM for sinapyl aldehyde {ECO:0000269|PubMed:15907484};
CC KM=60 uM for coniferyl alcohol {ECO:0000269|PubMed:15907484};
CC KM=150 uM for sinapyl alcohol {ECO:0000269|PubMed:15907484};
CC KM=260 uM for coniferyl alcohol {ECO:0000269|PubMed:11042211};
CC KM=240 uM for sinapyl alcohol {ECO:0000269|PubMed:11042211};
CC KM=450 uM for ferulate {ECO:0000269|PubMed:11042211};
CC KM=900 uM for sinapate {ECO:0000269|PubMed:11042211};
CC -!- TISSUE SPECIFICITY: Expressed in seedlings and roots.
CC {ECO:0000269|PubMed:16995900}.
CC -!- MISCELLANEOUS: Plants overexpressing UGT72E2 show increased
CC accumulation of monolignol glucosides in roots and appearance of these
CC glucosides in leaves. {ECO:0000269|PubMed:16995900}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM62659.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB018119; BAA97275.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98252.1; -; Genomic_DNA.
DR EMBL; AY062636; AAL32714.1; -; mRNA.
DR EMBL; AY064651; AAL47362.1; -; mRNA.
DR EMBL; AY085432; AAM62659.1; ALT_INIT; mRNA.
DR RefSeq; NP_201470.1; NM_126067.3.
DR AlphaFoldDB; Q9LVR1; -.
DR SMR; Q9LVR1; -.
DR STRING; 3702.AT5G66690.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PaxDb; Q9LVR1; -.
DR PRIDE; Q9LVR1; -.
DR ProteomicsDB; 228589; -.
DR EnsemblPlants; AT5G66690.1; AT5G66690.1; AT5G66690.
DR GeneID; 836802; -.
DR Gramene; AT5G66690.1; AT5G66690.1; AT5G66690.
DR KEGG; ath:AT5G66690; -.
DR Araport; AT5G66690; -.
DR TAIR; locus:2173664; AT5G66690.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_3_2_1; -.
DR InParanoid; Q9LVR1; -.
DR OMA; WDEMEPR; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q9LVR1; -.
DR BioCyc; ARA:AT5G66690-MON; -.
DR BioCyc; MetaCyc:AT5G66690-MON; -.
DR SABIO-RK; Q9LVR1; -.
DR PRO; PR:Q9LVR1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LVR1; baseline and differential.
DR Genevisible; Q9LVR1; AT.
DR GO; GO:0047209; F:coniferyl-alcohol glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0102359; F:daphnetin 4-O-beta-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102361; F:esculetin 4-O-beta-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0047218; F:hydroxycinnamate 4-beta-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102952; F:UDP-glucose:coniferaldehyde 4-beta-D-glucosyltransferase activity; IEA:RHEA.
DR GO; GO:0102956; F:UDP-glucose:sinapaldehyde 4-beta-D-glucosyltransferase activity; IEA:RHEA.
DR GO; GO:0009808; P:lignin metabolic process; TAS: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 1: Evidence at protein level;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..481
FT /note="UDP-glycosyltransferase 72E2"
FT /id="PRO_0000409074"
FT BINDING 272
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 346..348
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 363..371
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 385..388
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT CONFLICT 3
FT /note="I -> N (in Ref. 4; AAM62659)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 481 AA; 52992 MW; EE46B76C4BD14745 CRC64;
MHITKPHAAM FSSPGMGHVI PVIELGKRLS ANNGFHVTVF VLETDAASAQ SKFLNSTGVD
IVKLPSPDIY GLVDPDDHVV TKIGVIMRAA VPALRSKIAA MHQKPTALIV DLFGTDALCL
AKEFNMLSYV FIPTNARFLG VSIYYPNLDK DIKEEHTVQR NPLAIPGCEP VRFEDTLDAY
LVPDEPVYRD FVRHGLAYPK ADGILVNTWE EMEPKSLKSL LNPKLLGRVA RVPVYPIGPL
CRPIQSSETD HPVLDWLNEQ PNESVLYISF GSGGCLSAKQ LTELAWGLEQ SQQRFVWVVR
PPVDGSCCSE YVSANGGGTE DNTPEYLPEG FVSRTSDRGF VVPSWAPQAE ILSHRAVGGF
LTHCGWSSTL ESVVGGVPMI AWPLFAEQNM NAALLSDELG IAVRLDDPKE DISRWKIEAL
VRKVMTEKEG EAMRRKVKKL RDSAEMSLSI DGGGLAHESL CRVTKECQRF LERVVDLSRG
A
