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 07-NOV-2018, entry version 100. 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; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC 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 RT reference 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., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., 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 RT of 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 RT endogenous 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 RT glycosyltransferases capable of glucosylating coniferyl aldehyde and RT 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 RT of 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 RT syringin, 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, CC PubMed:16995900, PubMed:21149736, PubMed:24667164). Glucosylates CC coniferyl alcohol to form coniferyl alcohol 4-O-glucoside CC (PubMed:11042211, PubMed:15907484, PubMed:16995900, CC PubMed:21149736, PubMed:24667164). Glucosylates sinapyl alcohol to CC form sinapyl alcohol 4-O-glucoside (PubMed:11042211, CC PubMed:12721858, PubMed:15907484, PubMed:21149736, CC PubMed:24667164). Glucosylates coniferyl aldehyde to form CC coniferyl aldehyde 4-O-glucoside (PubMed:15907484). Glucosylates CC sinapyl aldehyde to form sinapyl aldehyde 4-O-glucoside CC (PubMed:15907484). Possesses low activity with sinapate and CC ferulate as substrates (PubMed:11042211, PubMed:15907484). CC {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: UDP-glucose + trans-4-hydroxycinnamate = UDP + CC 4-O-beta-D-glucosyl-4-hydroxycinnamate. CC {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: UDP-glucose + coniferyl alcohol = UDP + CC coniferin. {ECO:0000269|PubMed:11042211, CC ECO:0000269|PubMed:15907484, ECO:0000269|PubMed:16995900, CC ECO:0000269|PubMed:21149736, ECO:0000269|PubMed:24667164}. CC -!- CATALYTIC ACTIVITY: UDP-alpha-D-glucose + trans-sinapyl alcohol = CC UDP + 4-O-(beta-D-glucosyl)-trans-4-sinapyl alcohol + H(+). CC {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: UDP-alpha-D-glucose + sinapate = UDP + 4-O- CC beta-D-glucosyl-trans-4-sinapate + H(+). CC {ECO:0000269|PubMed:11042211}. 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 CC these 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=Translation N-terminally extended.; 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 UniGene; At.27462; -. DR ProteinModelPortal; Q9LVR1; -. DR SMR; Q9LVR1; -. DR STRING; 3702.AT5G66690.1; -. DR CAZy; GT1; Glycosyltransferase Family 1. DR PaxDb; Q9LVR1; -. 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 eggNOG; COG1819; LUCA. DR HOGENOM; HOG000237568; -. DR InParanoid; Q9LVR1; -. DR KO; K12356; -. DR OMA; DEMEPRS; -. DR OrthoDB; EOG093609EQ; -. DR PhylomeDB; Q9LVR1; -. DR BioCyc; ARA:AT5G66690-MONOMER; -. DR BioCyc; MetaCyc: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:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central. 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: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:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central. DR GO; GO:0009808; P:lignin metabolic process; TAS:TAIR. 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 Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 481 UDP-glycosyltransferase 72E2. FT /FTId=PRO_0000409074. FT REGION 346 348 UDP-glucose binding. {ECO:0000250}. FT REGION 363 371 UDP-glucose binding. {ECO:0000250}. FT REGION 385 388 UDP-glucose binding. {ECO:0000250}. FT BINDING 272 272 UDP-glucose. {ECO:0000250}. FT CONFLICT 3 3 I -> N (in Ref. 4; AAM62659). FT {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 //