U74F2_ARATH
ID U74F2_ARATH Reviewed; 449 AA.
AC O22822;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=UDP-glycosyltransferase 74F2;
DE EC=2.4.1.-;
DE AltName: Full=AtSGT1;
DE AltName: Full=Salicylic acid glucosyltransferase 1;
GN Name=UGT74F2; Synonyms=GT, SAGT1, SGT1; OrderedLocusNames=At2g43820;
GN ORFNames=F18O19.7;
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], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP INDUCTION.
RX PubMed=17085977;
RA Song J.T.;
RT "Induction of a salicylic acid glucosyltransferase, AtSGT1, is an early
RT disease response in Arabidopsis thaliana.";
RL Mol. Cells 22:233-238(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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=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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) 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.
RX PubMed=11641410; DOI=10.1074/jbc.m109287200;
RA Lim E.K., Doucet C.J., Li Y., Elias L., Worrall D., Spencer S.P., Ross J.,
RA Bowles D.J.;
RT "The activity of Arabidopsis glycosyltransferases toward salicylic acid, 4-
RT hydroxybenzoic acid, and other benzoates.";
RL J. Biol. Chem. 277:586-592(2002).
RN [8]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12475971; DOI=10.1074/jbc.m211822200;
RA Quiel J.A., Bender J.;
RT "Glucose conjugation of anthranilate by the Arabidopsis UGT74F2
RT glucosyltransferase is required for tryptophan mutant blue fluorescence.";
RL J. Biol. Chem. 278:6275-6281(2003).
RN [9]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=18385129; DOI=10.1074/jbc.m709591200;
RA Eudes A., Bozzo G.G., Waller J.C., Naponelli V., Lim E.K., Bowles D.J.,
RA Gregory J.F. III, Hanson A.D.;
RT "Metabolism of the folate precursor p-aminobenzoate in plants: glucose
RT ester formation and vacuolar storage.";
RL J. Biol. Chem. 283:15451-15459(2008).
RN [10]
RP FUNCTION.
RX PubMed=18226820; DOI=10.1016/j.phytochem.2007.12.010;
RA Song J.T., Koo Y.J., Seo H.S., Kim M.C., Choi Y.D., Kim J.H.;
RT "Overexpression of AtSGT1, an Arabidopsis salicylic acid
RT glucosyltransferase, leads to increased susceptibility to Pseudomonas
RT syringae.";
RL Phytochemistry 69:1128-1134(2008).
RN [11]
RP INDUCTION.
RX PubMed=19669626; DOI=10.1007/s10059-009-0108-x;
RA Song J.T., Koo Y.J., Park J.B., Seo Y.J., Cho Y.J., Seo H.S., Choi Y.D.;
RT "The expression patterns of AtBSMT1 and AtSAGT1 encoding a salicylic acid
RT (SA) methyltransferase and a SA glucosyltransferase, respectively, in
RT Arabidopsis plants with altered defense responses.";
RL Mol. Cells 28:105-109(2009).
CC -!- FUNCTION: Glycosyltransferase that glucosylates benzoic acid and
CC derivatives. Substrate preference is benzoic acid > salicylic acid (SA)
CC > 3-hydroxybenzoic acid > 4-hydroxybenzoic acid. Catalyzes the
CC formation of both SA 2-O-beta-D-glucoside (SAG) and SA glucose ester
CC (SGE). Has high affinity for the tryptophan precursor anthranilate.
CC Catalyzes the formation of anthranilate glucose ester. Is the major
CC source of this activity in the plant. {ECO:0000269|PubMed:11641410,
CC ECO:0000269|PubMed:12475971, ECO:0000269|PubMed:17085977,
CC ECO:0000269|PubMed:18226820, ECO:0000269|PubMed:18385129}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=80 uM for anthranilate {ECO:0000269|PubMed:12475971,
CC ECO:0000269|PubMed:17085977, ECO:0000269|PubMed:18385129};
CC KM=190 uM for salicylate {ECO:0000269|PubMed:12475971,
CC ECO:0000269|PubMed:17085977, ECO:0000269|PubMed:18385129};
CC KM=540 uM for benzoate {ECO:0000269|PubMed:12475971,
CC ECO:0000269|PubMed:17085977, ECO:0000269|PubMed:18385129};
CC KM=920 uM for 4-aminobenzoate {ECO:0000269|PubMed:12475971,
CC ECO:0000269|PubMed:17085977, ECO:0000269|PubMed:18385129};
CC -!- TISSUE SPECIFICITY: Expressed in seedlings.
CC {ECO:0000269|PubMed:12475971}.
CC -!- INDUCTION: By auxin, abscisic acid, salicylic acid and the bacterial
CC pathogen P.syringae. {ECO:0000269|PubMed:12475971,
CC ECO:0000269|PubMed:17085977, ECO:0000269|PubMed:19669626}.
CC -!- MISCELLANEOUS: Plants overexpressing UGT74F2 show increased
CC susceptibility to the bacterial pathogen P.syringae and reduced
CC accumulation of free SA upon infection.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; DQ407524; ABD66577.1; -; mRNA.
DR EMBL; AC002333; AAB64024.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10331.1; -; Genomic_DNA.
DR EMBL; AY062483; AAL32561.1; -; mRNA.
DR EMBL; BT010327; AAQ55278.1; -; mRNA.
DR EMBL; AY087340; AAM64890.1; -; mRNA.
DR PIR; H84870; H84870.
DR RefSeq; NP_181910.1; NM_129944.3.
DR PDB; 5U6M; X-ray; 2.57 A; A/B=1-449.
DR PDB; 5U6N; X-ray; 2.00 A; A/B=1-449.
DR PDB; 5U6S; X-ray; 2.00 A; A/B=1-449.
DR PDB; 5V2J; X-ray; 1.80 A; A/B=1-449.
DR PDB; 5V2K; X-ray; 2.00 A; A/B=1-449.
DR PDBsum; 5U6M; -.
DR PDBsum; 5U6N; -.
DR PDBsum; 5U6S; -.
DR PDBsum; 5V2J; -.
DR PDBsum; 5V2K; -.
DR AlphaFoldDB; O22822; -.
DR SMR; O22822; -.
DR STRING; 3702.AT2G43820.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PaxDb; O22822; -.
DR PRIDE; O22822; -.
DR ProteomicsDB; 242809; -.
DR EnsemblPlants; AT2G43820.1; AT2G43820.1; AT2G43820.
DR GeneID; 818986; -.
DR Gramene; AT2G43820.1; AT2G43820.1; AT2G43820.
DR KEGG; ath:AT2G43820; -.
DR Araport; AT2G43820; -.
DR TAIR; locus:2043949; AT2G43820.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_0_1_1; -.
DR InParanoid; O22822; -.
DR OMA; YIYYYVH; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; O22822; -.
DR BioCyc; ARA:AT2G43820-MON; -.
DR BioCyc; MetaCyc:AT2G43820-MON; -.
DR PRO; PR:O22822; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22822; baseline and differential.
DR Genevisible; O22822; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0052641; F:benzoic acid glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0090704; F:nicotinate-O-glucosyltransferase activity; IDA: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:0052639; F:salicylic acid glucosyltransferase (ester-forming) activity; IDA:TAIR.
DR GO; GO:0052640; F:salicylic acid glucosyltransferase (glucoside-forming) activity; IDA:TAIR.
DR GO; GO:0080002; F:UDP-glucose:4-aminobenzoate acylglucosyltransferase activity; IDA:TAIR.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0018874; P:benzoate metabolic process; IDA:TAIR.
DR GO; GO:0046482; P:para-aminobenzoic acid metabolic process; IDA:TAIR.
DR GO; GO:0010030; P:positive regulation of seed germination; IMP:TAIR.
DR GO; GO:0009696; P:salicylic acid metabolic 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 3D-structure; Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..449
FT /note="UDP-glycosyltransferase 74F2"
FT /id="PRO_0000409104"
FT BINDING 273
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 325..327
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 342..350
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 364..367
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:5V2J"
FT HELIX 16..31
FT /evidence="ECO:0007829|PDB:5V2J"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:5V2J"
FT HELIX 42..48
FT /evidence="ECO:0007829|PDB:5V2J"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:5V2J"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:5V2J"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:5V2J"
FT HELIX 76..97
FT /evidence="ECO:0007829|PDB:5V2J"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:5V2J"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:5V2J"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:5V2J"
FT HELIX 116..123
FT /evidence="ECO:0007829|PDB:5V2J"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:5V2J"
FT HELIX 136..147
FT /evidence="ECO:0007829|PDB:5V2J"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:5V2J"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:5U6S"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:5V2J"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:5V2J"
FT HELIX 178..185
FT /evidence="ECO:0007829|PDB:5V2J"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:5V2J"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:5V2J"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:5V2J"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:5V2J"
FT HELIX 207..216
FT /evidence="ECO:0007829|PDB:5V2J"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:5U6S"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:5V2J"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:5U6M"
FT HELIX 253..259
FT /evidence="ECO:0007829|PDB:5V2J"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:5V2J"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:5V2J"
FT HELIX 279..289
FT /evidence="ECO:0007829|PDB:5V2J"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:5V2J"
FT HELIX 300..305
FT /evidence="ECO:0007829|PDB:5V2J"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:5V2J"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:5V2J"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:5V2J"
FT HELIX 327..332
FT /evidence="ECO:0007829|PDB:5V2J"
FT STRAND 336..341
FT /evidence="ECO:0007829|PDB:5V2J"
FT HELIX 345..354
FT /evidence="ECO:0007829|PDB:5V2J"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:5V2J"
FT HELIX 367..376
FT /evidence="ECO:0007829|PDB:5V2J"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:5V2J"
FT TURN 388..390
FT /evidence="ECO:0007829|PDB:5V2J"
FT HELIX 395..406
FT /evidence="ECO:0007829|PDB:5V2J"
FT HELIX 409..418
FT /evidence="ECO:0007829|PDB:5V2J"
FT HELIX 420..429
FT /evidence="ECO:0007829|PDB:5V2J"
FT HELIX 434..446
FT /evidence="ECO:0007829|PDB:5V2J"
SQ SEQUENCE 449 AA; 50772 MW; B7485B1EFFC7102F CRC64;
MEHKRGHVLA VPYPTQGHIT PFRQFCKRLH FKGLKTTLAL TTFVFNSINP DLSGPISIAT
ISDGYDHGGF ETADSIDDYL KDFKTSGSKT IADIIQKHQT SDNPITCIVY DAFLPWALDV
AREFGLVATP FFTQPCAVNY VYYLSYINNG SLQLPIEELP FLELQDLPSF FSVSGSYPAY
FEMVLQQFIN FEKADFVLVN SFQELELHEN ELWSKACPVL TIGPTIPSIY LDQRIKSDTG
YDLNLFESKD DSFCINWLDT RPQGSVVYVA FGSMAQLTNV QMEELASAVS NFSFLWVVRS
SEEEKLPSGF LETVNKEKSL VLKWSPQLQV LSNKAIGCFL THCGWNSTME ALTFGVPMVA
MPQWTDQPMN AKYIQDVWKA GVRVKTEKES GIAKREEIEF SIKEVMEGER SKEMKKNVKK
WRDLAVKSLN EGGSTDTNID TFVSRVQSK
