U74B1_ARATH
ID U74B1_ARATH Reviewed; 460 AA.
AC O48676; Q0WLE1; W8PVB1;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=UDP-glycosyltransferase 74B1;
DE AltName: Full=N-hydroxythioamide S-beta-glucosyltransferase;
DE EC=2.4.1.195 {ECO:0000269|PubMed:15584955};
DE AltName: Full=Thiohydroximate S-glucosyltransferase;
GN Name=UGT74B1; OrderedLocusNames=At1g24100; ORFNames=F3I6.2;
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=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 [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] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INDUCTION BY IAA,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION PHENOTYPE.
RX PubMed=15584955; DOI=10.1111/j.1365-313x.2004.02261.x;
RA Grubb C.D., Zipp B.J., Ludwig-Mueller J., Masuno M.N., Molinski T.F.,
RA Abel S.;
RT "Arabidopsis glucosyltransferase UGT74B1 functions in glucosinolate
RT biosynthesis and auxin homeostasis.";
RL Plant J. 40:893-908(2004).
CC -!- FUNCTION: Involved in the biosynthesis of glucosinolate. In in vitro
CC assay, may use phenylacetothiohydroximate (PATH), but not phenylacetic
CC acid (PAA), indole-3-acetic acid (IAA) or salicylic acid (SA) as
CC substrate. Specific for the thiohydroximate functional group and does
CC not glucosylate the carboxylate group or a hydroxyl group.
CC {ECO:0000269|PubMed:15584955}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(Z)-2-phenyl-1-thioacetohydroximate + UDP-alpha-D-glucose =
CC (Z)-desulfoglucotropeolin + UDP; Xref=Rhea:RHEA:13757,
CC ChEBI:CHEBI:58176, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:136422; EC=2.4.1.195;
CC Evidence={ECO:0000269|PubMed:15584955};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (Z)-omega-(methylsulfanyl)alkyl-thiohydroximate + UDP-alpha-
CC D-glucose = an aliphatic (Z)-desulfo-glucosinolate + UDP;
CC Xref=Rhea:RHEA:52148, Rhea:RHEA-COMP:13191, Rhea:RHEA-COMP:17746,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:136425,
CC ChEBI:CHEBI:187900; EC=2.4.1.195;
CC Evidence={ECO:0000269|PubMed:15584955};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(Z)-2-(indol-3-yl)-1-thioacetohydroximate + UDP-alpha-D-
CC glucose = (Z)-indolylmethyl desulfoglucosinolate + UDP;
CC Xref=Rhea:RHEA:52152, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:136527, ChEBI:CHEBI:187899; EC=2.4.1.195;
CC Evidence={ECO:0000269|PubMed:15584955};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.8 uM for PATH {ECO:0000269|PubMed:15584955};
CC KM=48 uM for UDP-glucose {ECO:0000269|PubMed:15584955};
CC pH dependence:
CC Optimum pH is 6. Stable between pH 5-9.
CC {ECO:0000269|PubMed:15584955};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O48676-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O48676-2; Sequence=VSP_025589;
CC -!- TISSUE SPECIFICITY: Expressed in the vasculature, the apical meristems
CC of roots, shoots and inflorescence, and the junction of organ or
CC branches. {ECO:0000269|PubMed:15584955}.
CC -!- INDUCTION: By high IAA concentration. {ECO:0000269|PubMed:15584955}.
CC -!- DISRUPTION PHENOTYPE: Plants are severely dwarfed, partially sterile
CC and display decreased glucosinolate levels and increased IAA
CC concentrations. {ECO:0000269|PubMed:15584955}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; KJ138987; AHL38927.1; -; mRNA.
DR EMBL; AC002396; AAC00570.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30478.1; -; Genomic_DNA.
DR EMBL; BT001160; AAN65047.1; -; mRNA.
DR EMBL; AF387008; AAK62453.1; -; mRNA.
DR EMBL; AK230264; BAF02066.1; -; mRNA.
DR PIR; T00639; T00639.
DR RefSeq; NP_173820.1; NM_102256.3. [O48676-1]
DR AlphaFoldDB; O48676; -.
DR SMR; O48676; -.
DR STRING; 3702.AT1G24100.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR iPTMnet; O48676; -.
DR PaxDb; O48676; -.
DR PRIDE; O48676; -.
DR ProteomicsDB; 242609; -. [O48676-1]
DR EnsemblPlants; AT1G24100.1; AT1G24100.1; AT1G24100. [O48676-1]
DR GeneID; 839022; -.
DR Gramene; AT1G24100.1; AT1G24100.1; AT1G24100. [O48676-1]
DR KEGG; ath:AT1G24100; -.
DR Araport; AT1G24100; -.
DR TAIR; locus:2032387; AT1G24100.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_0_1_1; -.
DR InParanoid; O48676; -.
DR OMA; SIFCRIH; -.
DR PhylomeDB; O48676; -.
DR BioCyc; ARA:MON-6102; -.
DR BioCyc; MetaCyc:AT1G24100-MON; -.
DR PRO; PR:O48676; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O48676; baseline and differential.
DR Genevisible; O48676; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA: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:0047251; F:thiohydroximate beta-D-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0102659; F:UDP-glucose: 4-methylthiobutylhydroximate S-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0103100; F:UDP-glucose: 6-methylthiohexylhydroximate S-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0103103; F:UDP-glucose: 9-methylthiononylhydroximate S-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0103099; F:UDP-glucose:5-methylthiopentylhydroximate S-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0103101; F:UDP-glucose:7-methylthioheptylhydroximate S-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0103102; F:UDP-glucose:8-methylthiooctylhydroximate S-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0052544; P:defense response by callose deposition in cell wall; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0019761; P:glucosinolate biosynthetic process; IMP: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 Alternative splicing; Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..460
FT /note="UDP-glycosyltransferase 74B1"
FT /id="PRO_0000287670"
FT BINDING 284
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 337..339
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 354..362
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 376..379
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT VAR_SEQ 144..363
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_025589"
SQ SEQUENCE 460 AA; 51002 MW; D8C5A0C2DBA6883D CRC64;
MAETTPKVKG HVVILPYPVQ GHLNPMVQFA KRLVSKNVKV TIATTTYTAS SITTPSLSVE
PISDGFDFIP IGIPGFSVDT YSESFKLNGS ETLTLLIEKF KSTDSPIDCL IYDSFLPWGL
EVARSMELSA ASFFTNNLTV CSVLRKFSNG DFPLPADPNS APFRIRGLPS LSYDELPSFV
GRHWLTHPEH GRVLLNQFPN HENADWLFVN GFEGLEETQD CENGESDAMK ATLIGPMIPS
AYLDDRMEDD KDYGASLLKP ISKECMEWLE TKQAQSVAFV SFGSFGILFE KQLAEVAIAL
QESDLNFLWV IKEAHIAKLP EGFVESTKDR ALLVSWCNQL EVLAHESIGC FLTHCGWNST
LEGLSLGVPM VGVPQWSDQM NDAKFVEEVW KVGYRAKEEA GEVIVKSEEL VRCLKGVMEG
ESSVKIRESS KKWKDLAVKA MSEGGSSDRS INEFIESLGK
