ID   U71B2_ARATH             Reviewed;         485 AA.
AC   Q9LSY8;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=UDP-glycosyltransferase 71B2;
DE            EC=2.4.1.-;
DE   AltName: Full=Protein HYPOSTATIN RESISTANCE 1;
GN   Name=UGT71B2; Synonyms=HYR1; OrderedLocusNames=At3g21760;
GN   ORFNames=MSD21.7, MSD21.9;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(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   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, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-26.
RX   PubMed=17891152; DOI=10.1038/nchembio.2007.32;
RA   Zhao Y., Chow T.F., Puckrin R.S., Alfred S.E., Korir A.K., Larive C.K.,
RA   Cutler S.R.;
RT   "Chemical genetic interrogation of natural variation uncovers a molecule
RT   that is glycoactivated.";
RL   Nat. Chem. Biol. 3:716-721(2007).
CC   -!- FUNCTION: Glucosyltransferase that glucosylates the cell wall inhibitor
CC       hypostatin in vivo to form a bioactive glucoside.
CC       {ECO:0000269|PubMed:17891152}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       condition, but resistance to hypostatin treatment.
CC       {ECO:0000269|PubMed:17891152}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AB025634; BAB02838.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76549.1; -; Genomic_DNA.
DR   EMBL; AF372973; AAK50110.1; -; mRNA.
DR   EMBL; AF428321; AAL16251.1; -; mRNA.
DR   EMBL; AY140044; AAM98185.1; -; mRNA.
DR   EMBL; AY143906; AAN28845.1; -; mRNA.
DR   RefSeq; NP_188813.1; NM_113071.2.
DR   AlphaFoldDB; Q9LSY8; -.
DR   SMR; Q9LSY8; -.
DR   STRING; 3702.AT3G21760.1; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   PaxDb; Q9LSY8; -.
DR   PRIDE; Q9LSY8; -.
DR   ProteomicsDB; 228559; -.
DR   EnsemblPlants; AT3G21760.1; AT3G21760.1; AT3G21760.
DR   GeneID; 821730; -.
DR   Gramene; AT3G21760.1; AT3G21760.1; AT3G21760.
DR   KEGG; ath:AT3G21760; -.
DR   Araport; AT3G21760; -.
DR   TAIR; locus:2093089; AT3G21760.
DR   eggNOG; KOG1192; Eukaryota.
DR   HOGENOM; CLU_001724_3_2_1; -.
DR   InParanoid; Q9LSY8; -.
DR   OMA; VPSYMFY; -.
DR   OrthoDB; 508327at2759; -.
DR   PhylomeDB; Q9LSY8; -.
DR   BioCyc; ARA:AT3G21760-MON; -.
DR   PRO; PR:Q9LSY8; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LSY8; differential.
DR   Genevisible; Q9LSY8; AT.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IDA: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..485
FT                   /note="UDP-glycosyltransferase 71B2"
FT                   /id="PRO_0000409048"
FT   BINDING         287
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         354..356
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         371..379
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         393..396
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         26
FT                   /note="H->L: In hyr1; resistance to hypostatin."
FT                   /evidence="ECO:0000269|PubMed:17891152"
SQ   SEQUENCE   485 AA;  54342 MW;  1BBB3D04C5A1408D CRC64;
     MKLELVFIPS PGDGHLRPLV EVAKLHVDRD DHLSITIIII PQMHGFSSSN SSSYIASLSS
     DSEERLSYNV LSVPDKPDSD DTKPHFFDYI DNFKPQVKAT VEKLTDPGPP DSPSRLAGFV
     VDMFCMMMID VANEFGVPSY MFYTSNATFL GLQVHVEYLY DVKNYDVSDL KDSDTTELEV
     PCLTRPLPVK CFPSVLLTKE WLPVMFRQTR RFRETKGILV NTFAELEPQA MKFFSGVDSP
     LPTVYTVGPV MNLKINGPNS SDDKQSEILR WLDEQPRKSV VFLCFGSMGG FREGQAKEIA
     IALERSGHRF VWSLRRAQPK GSIGPPEEFT NLEEILPEGF LERTAEIGKI VGWAPQSAIL
     ANPAIGGFVS HCGWNSTLES LWFGVPMATW PLYAEQQVNA FEMVEELGLA VEVRNSFRGD
     FMAADDELMT AEEIERGIRC LMEQDSDVRS RVKEMSEKSH VALMDGGSSH VALLKFIQDV
     TKNIS