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 23-FEB-2022, entry version 116. 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)-sinapoyl 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)-sinapoaldehyde + 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}; 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; 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 SMR; Q9LVR1; -. DR STRING; 3702.AT5G66690.1; -. DR CAZy; GT1; Glycosyltransferase Family 1. DR PaxDb; 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; DEMEPRS; -. DR OrthoDB; 508327at2759; -. DR PhylomeDB; Q9LVR1; -. DR BioCyc; ARA:AT5G66690-MONOMER; -. 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 REGION 346..348 FT /note="UDP-glucose binding" FT /evidence="ECO:0000250" FT REGION 363..371 FT /note="UDP-glucose binding" FT /evidence="ECO:0000250" FT REGION 385..388 FT /note="UDP-glucose binding" FT /evidence="ECO:0000250" FT BINDING 272 FT /note="UDP-glucose" 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 //