ID U74E2_ARATH Reviewed; 453 AA.
AC Q9SYK9;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=UDP-glycosyltransferase 74E2;
DE EC=2.4.1.- {ECO:0000269|PubMed:20798329};
GN Name=UGT74E2; OrderedLocusNames=At1g05680; ORFNames=F3F20.13;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF Clone.";
RL Submitted (OCT-2006) 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, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20798329; DOI=10.1105/tpc.109.071316;
RA Tognetti V.B., Van Aken O., Morreel K., Vandenbroucke K., van de Cotte B.,
RA De Clercq I., Chiwocha S., Fenske R., Prinsen E., Boerjan W., Genty B.,
RA Stubbs K.A., Inze D., Van Breusegem F.;
RT "Perturbation of indole-3-butyric acid homeostasis by the UDP-
RT glucosyltransferase UGT74E2 modulates Arabidopsis architecture and water
RT stress tolerance.";
RL Plant Cell 22:2660-2679(2010).
CC -!- FUNCTION: Glucosyltransferase that acts on the auxin indole-3-butyric
CC acid (IBA). Mediates abiotic stress responses and stress-induced
CC morphological adaptations by regulating auxin homeostasis. Possesses
CC low activity in vitro on jasmonate (JA) and the synthetic auxin analog
CC naphthaleneacetic acid (NAA). {ECO:0000269|PubMed:20798329}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(indol-3-yl)butanoate + UDP-alpha-D-glucose = 4-(indol-3-
CC yl)butanoyl-beta-D-glucose + UDP; Xref=Rhea:RHEA:62708,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:143274,
CC ChEBI:CHEBI:145927; Evidence={ECO:0000269|PubMed:20798329};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.39 uM for indole-3-butyric acid {ECO:0000269|PubMed:20798329};
CC -!- TISSUE SPECIFICITY: Expressed in roots, cotyledons and leaf hydathodes.
CC {ECO:0000269|PubMed:20798329}.
CC -!- INDUCTION: By H(2)O(2) and abiotic stresses.
CC {ECO:0000269|PubMed:20798329}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC condition. {ECO:0000269|PubMed:20798329}.
CC -!- MISCELLANEOUS: Plants overexpressing UGT74E2 develop more compact
CC rosette structure with shorter petioles, dark-green leaves and a shoot
CC branching phenotype after inflorescence emergence. Mature plants are
CC shorter than wild-type. Over-expression of UGT74E2 increases plant
CC tolerance to osmotic stress.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AC007153; AAD30627.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27876.1; -; Genomic_DNA.
DR EMBL; BT022019; AAY25431.1; -; mRNA.
DR EMBL; BT029189; ABJ17124.1; -; mRNA.
DR PIR; A86191; A86191.
DR RefSeq; NP_172059.1; NM_100448.4.
DR AlphaFoldDB; Q9SYK9; -.
DR SMR; Q9SYK9; -.
DR BioGRID; 22317; 1.
DR IntAct; Q9SYK9; 1.
DR STRING; 3702.Q9SYK9; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PaxDb; 3702-AT1G05680-1; -.
DR ProteomicsDB; 228562; -.
DR EnsemblPlants; AT1G05680.1; AT1G05680.1; AT1G05680.
DR GeneID; 837075; -.
DR Gramene; AT1G05680.1; AT1G05680.1; AT1G05680.
DR KEGG; ath:AT1G05680; -.
DR Araport; AT1G05680; -.
DR TAIR; AT1G05680; UGT74E2.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_0_1_1; -.
DR InParanoid; Q9SYK9; -.
DR OMA; WVQSLWP; -.
DR OrthoDB; 382054at2759; -.
DR PhylomeDB; Q9SYK9; -.
DR BioCyc; ARA:AT1G05680-MONOMER; -.
DR BioCyc; MetaCyc:AT1G05680-MONOMER; -.
DR PRO; PR:Q9SYK9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SYK9; baseline and differential.
DR Genevisible; Q9SYK9; AT.
DR GO; GO:0052638; F:indole-3-butyrate beta-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0071475; P:cellular hyperosmotic salinity response; IEP:TAIR.
DR GO; GO:0071215; P:cellular response to abscisic acid stimulus; IMP:TAIR.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:TAIR.
DR GO; GO:0042631; P:cellular response to water deprivation; IEP:TAIR.
DR GO; GO:0080024; P:indolebutyric acid metabolic process; IMP:TAIR.
DR GO; GO:0010016; P:shoot system morphogenesis; IMP:TAIR.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR002213; UDP_glucos_trans.
DR InterPro; IPR035595; UDP_glycos_trans_CS.
DR PANTHER; PTHR11926; GLUCOSYL/GLUCURONOSYL TRANSFERASES; 1.
DR PANTHER; PTHR11926:SF1539; UDP-GLYCOSYLTRANSFERASE 74E1-RELATED; 1.
DR Pfam; PF00201; UDPGT; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS00375; UDPGT; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Reference proteome; Stress response; Transferase.
FT CHAIN 1..453
FT /note="UDP-glycosyltransferase 74E2"
FT /id="PRO_0000409102"
FT ACT_SITE 17
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT ACT_SITE 109
FT /note="Charge relay"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 17
FT /ligand="an anthocyanidin"
FT /ligand_id="ChEBI:CHEBI:143576"
FT /evidence="ECO:0000250|UniProtKB:P51094"
FT BINDING 131
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 334
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 349
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 352
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 353
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 354
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 357
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 373
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 374
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
SQ SEQUENCE 453 AA; 51051 MW; 4D7ABF3D36C4FAD0 CRC64;
MREGSHLIVL PFPGQGHITP MSQFCKRLAS KGLKLTLVLV SDKPSPPYKT EHDSITVFPI
SNGFQEGEEP LQDLDDYMER VETSIKNTLP KLVEDMKLSG NPPRAIVYDS TMPWLLDVAH
SYGLSGAVFF TQPWLVTAIY YHVFKGSFSV PSTKYGHSTL ASFPSFPMLT ANDLPSFLCE
SSSYPNILRI VVDQLSNIDR VDIVLCNTFD KLEEKLLKWV QSLWPVLNIG PTVPSMYLDK
RLSEDKNYGF SLFNAKVAEC MEWLNSKEPN SVVYLSFGSL VILKEDQMLE LAAGLKQSGR
FFLWVVRETE THKLPRNYVE EIGEKGLIVS WSPQLDVLAH KSIGCFLTHC GWNSTLEGLS
LGVPMIGMPH WTDQPTNAKF MQDVWKVGVR VKAEGDGFVR REEIMRSVEE VMEGEKGKEI
RKNAEKWKVL AQEAVSEGGS SDKSINEFVS MFC
//
