SOT16_ARATH
ID SOT16_ARATH Reviewed; 338 AA.
AC Q9C9D0; Q8LB09;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Cytosolic sulfotransferase 16;
DE Short=AtSOT16;
DE EC=2.8.2.24 {ECO:0000269|PubMed:19077143};
DE AltName: Full=Aromatic desulfoglucosinolate sulfotransferase {ECO:0000305};
DE AltName: Full=Desulfoglucosinolate sulfotransferase A;
DE Short=AtST5a;
DE AltName: Full=Protein CORONATINE INDUCED 7;
GN Name=SOT16; Synonyms=CORI-7, ST5A; OrderedLocusNames=At1g74100;
GN ORFNames=F2P9.3;
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].
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 [5]
RP FUNCTION, 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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INDUCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND VARIANT LEU-324.
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-2-
CC phenylethyl glucosinolate > desulfo-indol-3-yl methyl glucosinolate >
CC desulfo-benzyl glucosinolate > desulfo-6-methylthiohexyl glucosinolate
CC > desulfo-4-methylthiobutyl glucosinolate > desulfo-3-methylthiopropyl
CC glucosinolate > desulfo-singrin > desulfo-3-butenyl glucosinolate.
CC {ECO:0000269|PubMed:15358770, ECO:0000269|PubMed:15866872,
CC ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143,
CC ECO:0000269|PubMed:21281472}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(Z)-desulfoglucotropeolin + 3'-phosphoadenylyl sulfate = (Z)-
CC glucotropeolin + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:20281, ChEBI:CHEBI:15378, ChEBI:CHEBI:58021,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136422;
CC EC=2.8.2.24; Evidence={ECO:0000269|PubMed:19077143};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(Z)-indolylmethyl desulfoglucosinolate + 3'-phosphoadenylyl
CC sulfate = (Z)-glucobrassicin + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:52736, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:136527, ChEBI:CHEBI:187898;
CC EC=2.8.2.24; Evidence={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=100 uM for 3'-phospho-5'-adenylyl sulfate
CC {ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143};
CC KM=70 uM for desulfo-3-methylthiopropyl glucosinolate
CC {ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143};
CC KM=80 uM for desulfo-4-methylthiobutyl glucosinolate
CC {ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143};
CC Vmax=1100 pmol/sec/mg enzyme with desulfo-benzyl glucosinolate as
CC substrate {ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143};
CC Vmax=692 pmol/sec/mg enzyme with 3'-phospho-5'-adenylyl sulfate as
CC substrate {ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143};
CC Vmax=623 pmol/sec/mg enzyme with desulfo-3-methylthiopropyl
CC glucosinolate as substrate {ECO:0000269|PubMed:16367753,
CC ECO:0000269|PubMed:19077143};
CC Vmax=496 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: By wounding, 12-oxophytodienoic acid, jasmonic acid,
CC ethylene, UV-C and coronatine treatments. Not induced by abscisic acid,
CC 2,4-dichlorophenoxyacetic acid, gibberellin, kinetin, salicylic acid,
CC yeast elicitor or high sulfate concentration.
CC {ECO:0000269|PubMed:15358770, ECO:0000269|PubMed:16367753}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; AC016662; AAG52512.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35550.1; -; Genomic_DNA.
DR EMBL; AY042887; AAK68827.1; -; mRNA.
DR EMBL; AY081540; AAM10102.1; -; mRNA.
DR EMBL; AY087493; AAM65036.1; -; mRNA.
DR PIR; A96769; A96769.
DR RefSeq; NP_177550.1; NM_106070.2.
DR AlphaFoldDB; Q9C9D0; -.
DR SMR; Q9C9D0; -.
DR STRING; 3702.AT1G74100.1; -.
DR PaxDb; Q9C9D0; -.
DR PRIDE; Q9C9D0; -.
DR ProteomicsDB; 232611; -.
DR EnsemblPlants; AT1G74100.1; AT1G74100.1; AT1G74100.
DR GeneID; 843750; -.
DR Gramene; AT1G74100.1; AT1G74100.1; AT1G74100.
DR KEGG; ath:AT1G74100; -.
DR Araport; AT1G74100; -.
DR TAIR; locus:2031501; AT1G74100.
DR eggNOG; KOG1584; Eukaryota.
DR HOGENOM; CLU_027239_0_3_1; -.
DR InParanoid; Q9C9D0; -.
DR OMA; DPYEKNI; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; Q9C9D0; -.
DR BioCyc; MetaCyc:AT1G74100-MON; -.
DR BRENDA; 2.8.2.24; 399.
DR BRENDA; 2.8.2.38; 399.
DR PRO; PR:Q9C9D0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9D0; baseline and differential.
DR Genevisible; Q9C9D0; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; 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:0032260; P:response to jasmonic acid stimulus involved in jasmonic acid and ethylene-dependent systemic resistance; IEP: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..338
FT /note="Cytosolic sulfotransferase 16"
FT /id="PRO_0000315845"
FT ACT_SITE 143
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 81..86
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 165
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 231
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 301..303
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT VARIANT 324
FT /note="V -> L (in strain: cv. C24)"
FT /evidence="ECO:0000269|PubMed:16367753"
SQ SEQUENCE 338 AA; 39219 MW; ED8A7E0E90687A01 CRC64;
MESKTTQNGS EVVELTEFEK TQKKYQDFIA TLPKSKGWRP DEILTQYGGH WWQECLLEGL
FHAKDHFEAR PTDFLVCSYP KTGTTWLKAL TYAIVNRSRY DDAANPLLKR NPHEFVPYVE
IDFAFYPTVD VLQDRKNPLF STHIPNGLLP DSIVNSGCKM VYIWRDPKDT FISMWTFLHK
EKSQEGQLAS LEDSFDMFCK GLSVYGPYLD HVLGYWKAYQ ENPDRILFLR YETMRANPLP
FVKRLAEFMG YGFTDEEEEN GVAEKVVKLC SFETLKNLEA NKGDKEREDR PAVYANSAYF
RKGKVGDWAN YLTPEMAARI DGLVEEKFKD TGLLQHDN
