U72E1_ARATH
ID U72E1_ARATH Reviewed; 487 AA.
AC Q94A84; Q9S7R8; W8Q6P4;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=UDP-glycosyltransferase 72E1 {ECO:0000303|PubMed:11042215};
DE EC=2.4.1.- {ECO:0000269|PubMed:15907484};
GN Name=UGT72E1 {ECO:0000303|PubMed:11042215};
GN OrderedLocusNames=At3g50740 {ECO:0000312|Araport:AT3G50740};
GN ORFNames=F18B3.20 {ECO:0000312|EMBL:CAB42903.1};
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 [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=24905498; DOI=10.1111/tpj.12577;
RA Lao J., Oikawa A., Bromley J.R., McInerney P., Suttangkakul A.,
RA Smith-Moritz A.M., Plahar H., Chiu T.-Y., Gonzalez Fernandez-Nino S.M.G.,
RA Ebert B., Yang F., Christiansen K.M., Hansen S.F., Stonebloom S.,
RA Adams P.D., Ronald P.C., Hillson N.J., Hadi M.Z., Vega-Sanchez M.E.,
RA Loque D., Scheller H.V., Heazlewood J.L.;
RT "The plant glycosyltransferase clone collection for functional genomics.";
RL Plant J. 79:517-529(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) 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=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 INTERACTION WITH SIS8, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=24320620; DOI=10.1111/tpj.12404;
RA Huang Y., Li C.Y., Qi Y., Park S., Gibson S.I.;
RT "SIS8, a putative mitogen-activated protein kinase kinase kinase, regulates
RT sugar-resistant seedling development in Arabidopsis.";
RL Plant J. 77:577-588(2014).
CC -!- FUNCTION: UDP-glycosyltransferase that glucosylates coniferyl aldehyde
CC to form coniferyl aldehyde 4-O-glucoside (PubMed:15907484).
CC Glucosylates sinapyl aldehyde to form sinapyl aldehyde 4-O-glucoside
CC (PubMed:15907484). Is not active in presence of coniferyl alcohol or
CC sinapyl alcohol (PubMed:15907484). Can glucosylate the phytotoxic
CC xenobiotic compound 2,4,5-trichlorophenol (TCP) (PubMed:15907484).
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=0.27 mM for coniferyl aldehyde {ECO:0000269|PubMed:15907484};
CC KM=0.46 mM for sinapyl aldehyde {ECO:0000269|PubMed:15907484};
CC -!- SUBUNIT: Interacts with SIS8. {ECO:0000269|PubMed:24320620}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24320620}.
CC Note=Colocalizes with SIS8 in the nucleus.
CC {ECO:0000269|PubMed:24320620}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots and leaves.
CC {ECO:0000269|PubMed:16995900}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants display a sugar-resistant seedling
CC development phenotype. {ECO:0000269|PubMed:24320620}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB42903.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB62443.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; KJ138794; AHL38734.1; -; mRNA.
DR EMBL; AL049862; CAB42903.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL132979; CAB62443.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE78703.1; -; Genomic_DNA.
DR EMBL; AY049277; AAK83619.1; -; mRNA.
DR EMBL; BT015770; AAU90060.1; -; mRNA.
DR PIR; T08395; T08395.
DR RefSeq; NP_566938.1; NM_114934.2.
DR AlphaFoldDB; Q94A84; -.
DR SMR; Q94A84; -.
DR BioGRID; 9556; 1.
DR STRING; 3702.AT3G50740.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PaxDb; Q94A84; -.
DR PRIDE; Q94A84; -.
DR ProteomicsDB; 228620; -.
DR EnsemblPlants; AT3G50740.1; AT3G50740.1; AT3G50740.
DR GeneID; 824238; -.
DR Gramene; AT3G50740.1; AT3G50740.1; AT3G50740.
DR KEGG; ath:AT3G50740; -.
DR Araport; AT3G50740; -.
DR TAIR; locus:2101709; AT3G50740.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_3_2_1; -.
DR InParanoid; Q94A84; -.
DR OMA; VALYFPT; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q94A84; -.
DR BioCyc; ARA:AT3G50740-MON; -.
DR BioCyc; MetaCyc:AT3G50740-MON; -.
DR PRO; PR:Q94A84; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q94A84; baseline and differential.
DR Genevisible; Q94A84; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0047209; F:coniferyl-alcohol glucosyltransferase activity; IDA:TAIR.
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 GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
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 Detoxification; Glycosyltransferase; Nucleus; Reference proteome;
KW Transferase.
FT CHAIN 1..487
FT /note="UDP-glycosyltransferase 72E1"
FT /id="PRO_0000409073"
FT BINDING 277
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 351..353
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 368..376
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 390..393
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
SQ SEQUENCE 487 AA; 53363 MW; 060F98CA674D5CF5 CRC64;
MKITKPHVAM FASPGMGHII PVIELGKRLA GSHGFDVTIF VLETDAASAQ SQFLNSPGCD
AALVDIVGLP TPDISGLVDP SAFFGIKLLV MMRETIPTIR SKIEEMQHKP TALIVDLFGL
DAIPLGGEFN MLTYIFIASN ARFLAVALFF PTLDKDMEEE HIIKKQPMVM PGCEPVRFED
TLETFLDPNS QLYREFVPFG SVFPTCDGII VNTWDDMEPK TLKSLQDPKL LGRIAGVPVY
PIGPLSRPVD PSKTNHPVLD WLNKQPDESV LYISFGSGGS LSAKQLTELA WGLEMSQQRF
VWVVRPPVDG SACSAYLSAN SGKIRDGTPD YLPEGFVSRT HERGFMVSSW APQAEILAHQ
AVGGFLTHCG WNSILESVVG GVPMIAWPLF AEQMMNATLL NEELGVAVRS KKLPSEGVIT
RAEIEALVRK IMVEEEGAEM RKKIKKLKET AAESLSCDGG VAHESLSRIA DESEHLLERV
RCMARGA
