ID   U76B1_ARATH             Reviewed;         447 AA.
AC   Q9C768; Q8GWA0; Q9CAY9;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=UDP-glycosyltransferase 76B1 {ECO:0000305};
DE            EC=2.4.1.- {ECO:0000305};
GN   Name=UGT76B1 {ECO:0000303|PubMed:22080599};
GN   OrderedLocusNames=At3g11340 {ECO:0000312|Araport:AT3G11340,
GN   ECO:0000312|EMBL:AEE75032.1};
GN   ORFNames=F11B9.23 {ECO:0000312|EMBL:AAG50970.1},
GN   F24K9.1 {ECO:0000312|EMBL:AAG51429.1};
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].
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;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF Clones.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=22080599; DOI=10.1105/tpc.111.088443;
RA   von Saint Paul V., Zhang W., Kanawati B., Geist B., Faus-Kessler T.,
RA   Schmitt-Kopplin P., Schaeffner A.R.;
RT   "The Arabidopsis glucosyltransferase UGT76B1 conjugates isoleucic acid and
RT   modulates plant defense and senescence.";
RL   Plant Cell 23:4124-4145(2011).
CC   -!- FUNCTION: Glycosylates the amino acid-related molecules isoleucic acid
CC       (2-hydroxy-3-methylpentanoic acid) and valic acid (2-hydroxy-3-
CC       methylbutyric acid). Acts as a negative regulator of salicylic acid
CC       (SA)-dependent plant defense in the absence of pathogens and promotes
CC       the jasmonate (JA) response. Negatively influences the onset of
CC       senescence. {ECO:0000269|PubMed:22080599}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, hydathodes, sepals and
CC       style. {ECO:0000269|PubMed:22080599}.
CC   -!- INDUCTION: Induced by wounding and the bacterial pathogen Pseudomonas
CC       syringae pv. tomato (avirulent avrRpm1 strain).
CC       {ECO:0000269|PubMed:22080599}.
CC   -!- DISRUPTION PHENOTYPE: Reduced rosette size, early leaf senescence,
CC       enhanced resistance to the biotrophic pathogen Pseudomonas syringae,
CC       increased susceptibility toward necrotrophic Alternaria brassicicola
CC       and constitutively elevated salicylic acid (SA) levels.
CC       {ECO:0000269|PubMed:22080599}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; KJ138830; AHL38770.1; -; mRNA.
DR   EMBL; AC008153; AAG51429.1; -; Genomic_DNA.
DR   EMBL; AC073395; AAG50970.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75032.1; -; Genomic_DNA.
DR   EMBL; AK118988; BAC43564.1; -; mRNA.
DR   EMBL; BT026457; ABH04564.1; -; mRNA.
DR   RefSeq; NP_187742.1; NM_111968.4.
DR   AlphaFoldDB; Q9C768; -.
DR   SMR; Q9C768; -.
DR   STRING; 3702.AT3G11340.1; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   SwissPalm; Q9C768; -.
DR   PaxDb; Q9C768; -.
DR   PRIDE; Q9C768; -.
DR   ProteomicsDB; 228646; -.
DR   EnsemblPlants; AT3G11340.1; AT3G11340.1; AT3G11340.
DR   GeneID; 820307; -.
DR   Gramene; AT3G11340.1; AT3G11340.1; AT3G11340.
DR   KEGG; ath:AT3G11340; -.
DR   Araport; AT3G11340; -.
DR   TAIR; locus:2074738; AT3G11340.
DR   eggNOG; KOG1192; Eukaryota.
DR   HOGENOM; CLU_001724_0_0_1; -.
DR   InParanoid; Q9C768; -.
DR   OMA; FVEIAWG; -.
DR   OrthoDB; 508327at2759; -.
DR   PhylomeDB; Q9C768; -.
DR   BioCyc; ARA:AT3G11340-MON; -.
DR   PRO; PR:Q9C768; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9C768; baseline and differential.
DR   GO; GO:0046527; F:glucosyltransferase activity; IMP:TAIR.
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:0052640; F:salicylic acid glucosyltransferase (glucoside-forming) activity; IDA:TAIR.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IDA:TAIR.
DR   GO; GO:0006952; P:defense response; IMP:TAIR.
DR   GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR   GO; GO:0002239; P:response to oomycetes; IEP: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   2: Evidence at transcript level;
KW   Glycosyltransferase; Plant defense; Reference proteome; Transferase.
FT   CHAIN           1..447
FT                   /note="UDP-glycosyltransferase 76B1"
FT                   /id="PRO_0000440610"
FT   BINDING         269
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         327..328
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         345..353
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         367..370
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   CONFLICT        120
FT                   /note="E -> G (in Ref. 4; BAC43564)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   447 AA;  50705 MW;  93B060914E646F1D CRC64;
     METRETKPVI FLFPFPLQGH LNPMFQLANI FFNRGFSITV IHTEFNSPNS SNFPHFTFVS
     IPDSLSEPES YPDVIEILHD LNSKCVAPFG DCLKKLISEE PTAACVIVDA LWYFTHDLTE
     KFNFPRIVLR TVNLSAFVAF SKFHVLREKG YLSLQETKAD SPVPELPYLR MKDLPWFQTE
     DPRSGDKLQI GVMKSLKSSS GIIFNAIEDL ETDQLDEARI EFPVPLFCIG PFHRYVSASS
     SSLLAHDMTC LSWLDKQATN SVIYASLGSI ASIDESEFLE IAWGLRNSNQ PFLWVVRPGL
     IHGKEWIEIL PKGFIENLEG RGKIVKWAPQ PEVLAHRATG GFLTHCGWNS TLEGICEAIP
     MICRPSFGDQ RVNARYINDV WKIGLHLENK VERLVIENAV RTLMTSSEGE EIRKRIMPMK
     ETVEQCLKLG GSSFRNLENL IAYILSF