SOT17_ARATH
ID SOT17_ARATH Reviewed; 346 AA.
AC Q9FZ80;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Cytosolic sulfotransferase 17;
DE Short=AtSOT17;
DE EC=2.8.2.38 {ECO:0000269|PubMed:15358770, ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143};
DE AltName: Full=Desulfoglucosinolate sulfotransferase C;
DE Short=AtST5c;
GN Name=SOT17; Synonyms=ST5C; OrderedLocusNames=At1g18590;
GN ORFNames=F25I16.7, F25I16_11;
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;
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 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 FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX PubMed=15358770; DOI=10.1074/jbc.m407681200;
RA Piotrowski M., Schemenewitz A., Lopukhina A., Mueller A., Janowitz T.,
RA Weiler E.W., Oecking C.;
RT "Desulfoglucosinolate sulfotransferases from Arabidopsis thaliana catalyze
RT the final step in the biosynthesis of the glucosinolate core structure.";
RL J. Biol. Chem. 279:50717-50725(2004).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15234990; DOI=10.1093/jxb/erh183;
RA Klein M., Papenbrock J.;
RT "The multi-protein family of Arabidopsis sulphotransferases and their
RT relatives in other plant species.";
RL J. Exp. Bot. 55:1809-1820(2004).
RN [7]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=15866872; DOI=10.1074/jbc.m502332200;
RA Hirai M.Y., Klein M., Fujikawa Y., Yano M., Goodenowe D.B., Yamazaki Y.,
RA Kanaya S., Nakamura Y., Kitayama M., Suzuki H., Sakurai N., Shibata D.,
RA Tokuhisa J., Reichelt M., Gershenzon J., Papenbrock J., Saito K.;
RT "Elucidation of gene-to-gene and metabolite-to-gene networks in Arabidopsis
RT by integration of metabolomics and transcriptomics.";
RL J. Biol. Chem. 280:25590-25595(2005).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, INDUCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND VARIANTS
RP ARG-183 AND THR-344.
RC STRAIN=cv. C24;
RX PubMed=16367753; DOI=10.1111/j.1742-4658.2005.05048.x;
RA Klein M., Reichelt M., Gershenzon J., Papenbrock J.;
RT "The three desulfoglucosinolate sulfotransferase proteins in Arabidopsis
RT have different substrate specificities and are differentially expressed.";
RL FEBS J. 273:122-136(2006).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. C24;
RX PubMed=19077143; DOI=10.1111/j.1399-3054.2008.01182.x;
RA Klein M., Papenbrock J.;
RT "Kinetics and substrate specificities of desulfo-glucosinolate
RT sulfotransferases in Arabidopsis thaliana.";
RL Physiol. Plantarum 135:140-149(2009).
RN [10]
RP FUNCTION.
RX PubMed=21281472; DOI=10.1186/1472-6750-11-12;
RA Moeldrup M.E., Geu-Flores F., Olsen C.E., Halkier B.A.;
RT "Modulation of sulfur metabolism enables efficient glucosinolate
RT engineering.";
RL BMC Biotechnol. 11:12-12(2011).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the sulfate conjugation of
CC desulfo-glucosinolates (dsGSs), the final step in the biosynthesis of
CC the glucosinolate core structure. Substrate preference is desulfo-
CC benzyl glucosinolate > desulfo-6-methylthiohexyl glucosinolate.
CC Increased specific activity with increasing chain length of desulfo-
CC glucosinolate derived from methionine. Preferred substrate is desulfo-
CC 8-methylthiooctyl glucosinolate. {ECO:0000269|PubMed:15358770,
CC ECO:0000269|PubMed:15866872, ECO:0000269|PubMed:16367753,
CC ECO:0000269|PubMed:19077143, ECO:0000269|PubMed:21281472}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + an aliphatic (Z)-desulfo-
CC glucosinolate = a (Z)-omega-(methylsulfanyl)-N-sulfo-alkylhydroximate
CC S-glucoside + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:52724, Rhea:RHEA-COMP:13191, Rhea:RHEA-COMP:13194,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:136425, ChEBI:CHEBI:136434; EC=2.8.2.38;
CC Evidence={ECO:0000269|PubMed:15358770, ECO:0000269|PubMed:16367753,
CC ECO:0000269|PubMed:19077143};
CC -!- ACTIVITY REGULATION: Inhibited by phosphoadenosine 5'-phosphate (PAP).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=100 uM for desulfo-benzyl glucosinolate
CC {ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143};
CC KM=25 uM for 3'-phospho-5'-adenylyl sulfate
CC {ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143};
CC KM=88 uM for desulfo-3-methylthiopropyl glucosinolate
CC {ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143};
CC KM=65 uM for desulfo-4-methylthiobutyl glucosinolate
CC {ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143};
CC Vmax=125 pmol/sec/mg enzyme with desulfo-benzyl glucosinolate as
CC substrate {ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143};
CC Vmax=142 pmol/sec/mg enzyme with 3'-phospho-5'-adenylyl sulfate as
CC substrate {ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143};
CC Vmax=439 pmol/sec/mg enzyme with desulfo-3-methylthiopropyl
CC glucosinolate as substrate {ECO:0000269|PubMed:16367753,
CC ECO:0000269|PubMed:19077143};
CC Vmax=575 pmol/sec/mg enzyme with desulfo-4-methylthiobutyl
CC glucosinolate as substrate {ECO:0000269|PubMed:16367753,
CC ECO:0000269|PubMed:19077143};
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:16367753,
CC ECO:0000269|PubMed:19077143};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16367753}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots, stems and mature leaves.
CC Low expression in young leaves and flowers. Barely detected in
CC siliques. {ECO:0000269|PubMed:16367753}.
CC -!- DEVELOPMENTAL STAGE: Expression reaching a maximum in 2-week-old plants
CC and a minimum in flowering plants. {ECO:0000269|PubMed:16367753}.
CC -!- INDUCTION: Induced by coronatine, but not by methyl jasmonate or high
CC sulfate concentration. {ECO:0000269|PubMed:15358770,
CC ECO:0000269|PubMed:16367753}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; AC026238; AAF98415.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29732.1; -; Genomic_DNA.
DR EMBL; BT005398; AAO63818.1; -; mRNA.
DR EMBL; AK117408; BAC42075.1; -; mRNA.
DR PIR; E86319; E86319.
DR RefSeq; NP_173294.1; NM_101717.3.
DR AlphaFoldDB; Q9FZ80; -.
DR SMR; Q9FZ80; -.
DR STRING; 3702.AT1G18590.1; -.
DR iPTMnet; Q9FZ80; -.
DR PaxDb; Q9FZ80; -.
DR PRIDE; Q9FZ80; -.
DR ProteomicsDB; 232628; -.
DR EnsemblPlants; AT1G18590.1; AT1G18590.1; AT1G18590.
DR GeneID; 838440; -.
DR Gramene; AT1G18590.1; AT1G18590.1; AT1G18590.
DR KEGG; ath:AT1G18590; -.
DR Araport; AT1G18590; -.
DR TAIR; locus:2027458; AT1G18590.
DR eggNOG; KOG1584; Eukaryota.
DR HOGENOM; CLU_027239_0_3_1; -.
DR InParanoid; Q9FZ80; -.
DR OMA; PNMGFRS; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; Q9FZ80; -.
DR BioCyc; MetaCyc:AT1G18590-MON; -.
DR BRENDA; 2.8.2.38; 399.
DR PRO; PR:Q9FZ80; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZ80; baseline and differential.
DR Genevisible; Q9FZ80; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0047364; F:desulfoglucosinolate sulfotransferase activity; IDA:TAIR.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0019761; P:glucosinolate biosynthetic process; IDA:TAIR.
DR GO; GO:0051923; P:sulfation; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..346
FT /note="Cytosolic sulfotransferase 17"
FT /id="PRO_0000315846"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 89..94
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 309..311
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT VARIANT 183
FT /note="W -> R (in strain: cv. C24)"
FT /evidence="ECO:0000269|PubMed:16367753"
FT VARIANT 344
FT /note="S -> T (in strain: cv. C24)"
FT /evidence="ECO:0000269|PubMed:16367753"
SQ SEQUENCE 346 AA; 39912 MW; 84208C67260FD6B8 CRC64;
MESKTINDVV VSESNHELAS SSPSEFEKNQ KHYQEIIATL PHKDGWRPKD PFVEYGGHWW
LQPLLEGLLH AQKFFKARPN DFFVCSYPKT GTTWLKALTF AIANRSKFDV STNPLLKRNP
HEFVPYIEID FPFFPSVDVL KDEGNTLFST HIPYDLLPES VVKSGCKIVY IWRDPKDTFV
SMWTFAHKER SQQGPVVSIE EAFDKYCQGL SAYGPYLDHV LGYWKAYQAN PDQILFLKYE
TMRADPLPYV KRLAEFMGYG FTKEEEEGNV VEKVVKLCSF ETLKNLEANK GEKDREDRPA
VYANSAYFRK GKVGDWQNYL TPEMVARIDG LMEEKFKGTG FLSSKS
