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U72E3_ARATH
ID   U72E3_ARATH             Reviewed;         481 AA.
AC   O81498;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=UDP-glycosyltransferase 72E3 {ECO:0000303|PubMed:11042215};
DE            EC=2.4.1.111 {ECO:0000269|PubMed:15907484, ECO:0000269|PubMed:24667164};
DE   AltName: Full=Hydroxycinnamate 4-beta-glucosyltransferase UGT72E3 {ECO:0000305};
DE            EC=2.4.1.126 {ECO:0000269|PubMed:11042211, ECO:0000269|PubMed:15907484, ECO:0000269|PubMed:24667164};
GN   Name=UGT72E3 {ECO:0000303|PubMed:11042215};
GN   OrderedLocusNames=At5g26310 {ECO:0000312|Araport:AT5G26310};
GN   ORFNames=F9D12.4 {ECO:0000312|EMBL:AAC26233.1};
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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;
RA   Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
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   [6]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
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   [7]
RP   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   [8]
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,
CC       PubMed:24667164). Glucosylates coniferyl alcohol to form coniferyl
CC       alcohol 4-O-glucoside (PubMed:15907484, PubMed:24667164). Glucosylates
CC       sinapyl alcohol to form sinapyl alcohol 4-O-glucoside (PubMed:11042211,
CC       PubMed:15907484, PubMed:24667164). Possesses low activity with sinapate
CC       as substrate (PubMed:11042211, PubMed:15907484).
CC       {ECO:0000269|PubMed:11042211, ECO:0000269|PubMed:15907484,
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: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:15907484,
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:15907484, 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         ECO:0000269|PubMed:15907484};
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=180 uM for sinapate {ECO:0000269|PubMed:11042211};
CC         KM=850 uM for sinapyl alcohol {ECO:0000269|PubMed:11042211};
CC   -!- TISSUE SPECIFICITY: Expressed in seedlings and roots, and at lower
CC       levels in flowers and siliques. {ECO:0000269|PubMed:16995900}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AF077407; AAC26233.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED93550.1; -; Genomic_DNA.
DR   EMBL; BT030376; ABO38789.1; -; mRNA.
DR   PIR; T01850; T01850.
DR   RefSeq; NP_198003.1; NM_122532.3.
DR   AlphaFoldDB; O81498; -.
DR   SMR; O81498; -.
DR   STRING; 3702.AT5G26310.1; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   PaxDb; O81498; -.
DR   PRIDE; O81498; -.
DR   ProteomicsDB; 228590; -.
DR   EnsemblPlants; AT5G26310.1; AT5G26310.1; AT5G26310.
DR   GeneID; 832700; -.
DR   Gramene; AT5G26310.1; AT5G26310.1; AT5G26310.
DR   KEGG; ath:AT5G26310; -.
DR   Araport; AT5G26310; -.
DR   TAIR; locus:2151059; AT5G26310.
DR   eggNOG; KOG1192; Eukaryota.
DR   HOGENOM; CLU_001724_3_0_1; -.
DR   InParanoid; O81498; -.
DR   OMA; SANHGFH; -.
DR   OrthoDB; 508327at2759; -.
DR   PhylomeDB; O81498; -.
DR   BioCyc; ARA:AT5G26310-MON; -.
DR   BioCyc; MetaCyc:AT5G26310-MON; -.
DR   SABIO-RK; O81498; -.
DR   PRO; PR:O81498; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; O81498; baseline and differential.
DR   Genevisible; O81498; 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   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 72E3"
FT                   /id="PRO_0000409075"
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"
SQ   SEQUENCE   481 AA;  52904 MW;  5766E0877F0A1583 CRC64;
     MHITKPHAAM FSSPGMGHVL PVIELAKRLS ANHGFHVTVF VLETDAASVQ SKLLNSTGVD
     IVNLPSPDIS GLVDPNAHVV TKIGVIMREA VPTLRSKIVA MHQNPTALII DLFGTDALCL
     AAELNMLTYV FIASNARYLG VSIYYPTLDE VIKEEHTVQR KPLTIPGCEP VRFEDIMDAY
     LVPDEPVYHD LVRHCLAYPK ADGILVNTWE EMEPKSLKSL QDPKLLGRVA RVPVYPVGPL
     CRPIQSSTTD HPVFDWLNKQ PNESVLYISF GSGGSLTAQQ LTELAWGLEE SQQRFIWVVR
     PPVDGSSCSD YFSAKGGVTK DNTPEYLPEG FVTRTCDRGF MIPSWAPQAE ILAHQAVGGF
     LTHCGWSSTL ESVLCGVPMI AWPLFAEQNM NAALLSDELG ISVRVDDPKE AISRSKIEAM
     VRKVMAEDEG EEMRRKVKKL RDTAEMSLSI HGGGSAHESL CRVTKECQRF LECVGDLGRG
     A
 
 
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