SOT15_ARATH
ID SOT15_ARATH Reviewed; 359 AA.
AC Q8L5A7; Q940P4; Q9FL45;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Cytosolic sulfotransferase 15;
DE Short=AtSOT15;
DE EC=2.8.2.39 {ECO:0000269|PubMed:12637544};
DE AltName: Full=Sulfotransferase 2a;
DE Short=AtST2a;
GN Name=SOT15; Synonyms=ST2A; OrderedLocusNames=At5g07010; ORFNames=MOJ9.18;
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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 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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND
RP TISSUE SPECIFICITY.
RX PubMed=12637544; DOI=10.1074/jbc.m211943200;
RA Gidda S.K., Miersch O., Levitin A., Schmidt J., Wasternack C., Varin L.;
RT "Biochemical and molecular characterization of a hydroxyjasmonate
RT sulfotransferase from Arabidopsis thaliana.";
RL J. Biol. Chem. 278:17895-17900(2003).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to specifically catalyze the sulfate
CC conjugation of hydroxyjasmonates, with a preference for 12-
CC hydroxyjasmonate over 11-hydroxyjasmonate. No activity with 12-
CC hydroxyjasmonic acid methyl ester, cucurbic acid, 7-iso-cucurbic acid,
CC 6-epi-cucurbic acid, 6-epi-7-iso-cucurbic acid and their methyl esters,
CC prostaglandin E2, arachidonyl alcohol and 11-eicosenol.
CC {ECO:0000269|PubMed:12637544}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + a 12-hydroxyjasmonate = a 12-
CC sulfojasmonate + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:52728, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:136810, ChEBI:CHEBI:136811;
CC EC=2.8.2.39; Evidence={ECO:0000269|PubMed:12637544};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 uM for 11-hydroxyjasmonate {ECO:0000269|PubMed:12637544};
CC KM=10 uM for 12-hydroxyjasmonate {ECO:0000269|PubMed:12637544};
CC KM=1 uM for 3'-phospho-5'-adenylyl sulfate
CC {ECO:0000269|PubMed:12637544};
CC Vmax=37.5 pmol/sec/mg enzyme with 12-hydroxyjasmonate as substrate
CC {ECO:0000269|PubMed:12637544};
CC pH dependence:
CC Optimum pH is 7.5. Active in a broad range pH.
CC {ECO:0000269|PubMed:12637544};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|PubMed:12637544}.
CC -!- INDUCTION: Up-regulated by methyljasmonate, 12 hydroxyjasmonate and 12-
CC oxo-phytodienoic acid, but not by hormones.
CC {ECO:0000269|PubMed:12637544}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11159.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB010697; BAB11159.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED91098.1; -; Genomic_DNA.
DR EMBL; AY099809; AAM20660.1; -; mRNA.
DR EMBL; AY054219; AAL06879.1; -; mRNA.
DR EMBL; AY084999; AAM61557.1; -; mRNA.
DR EMBL; BT008847; AAP68286.1; -; mRNA.
DR RefSeq; NP_568177.1; NM_120783.4.
DR AlphaFoldDB; Q8L5A7; -.
DR SMR; Q8L5A7; -.
DR BioGRID; 15871; 1.
DR IntAct; Q8L5A7; 2.
DR STRING; 3702.AT5G07010.1; -.
DR PaxDb; Q8L5A7; -.
DR PRIDE; Q8L5A7; -.
DR ProteomicsDB; 232610; -.
DR EnsemblPlants; AT5G07010.1; AT5G07010.1; AT5G07010.
DR GeneID; 830592; -.
DR Gramene; AT5G07010.1; AT5G07010.1; AT5G07010.
DR KEGG; ath:AT5G07010; -.
DR Araport; AT5G07010; -.
DR TAIR; locus:2169344; AT5G07010.
DR eggNOG; KOG1584; Eukaryota.
DR HOGENOM; CLU_027239_0_1_1; -.
DR InParanoid; Q8L5A7; -.
DR OMA; HLFFTYQ; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; Q8L5A7; -.
DR BioCyc; ARA:AT5G07010-MON; -.
DR BRENDA; 2.8.2.39; 399.
DR PRO; PR:Q8L5A7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8L5A7; baseline and differential.
DR Genevisible; Q8L5A7; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0102056; F:11-hydroxyjasmonate sulfotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102055; F:12-hydroxyjasmonate sulfotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0080131; F:hydroxyjasmonate sulfotransferase activity; IDA:TAIR.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0009694; P:jasmonic acid metabolic process; IDA:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; 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..359
FT /note="Cytosolic sulfotransferase 15"
FT /id="PRO_0000417062"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 101..106
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 322..324
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CONFLICT 231
FT /note="G -> A (in Ref. 3; AAL06879)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 41364 MW; 04244AD987C3F104 CRC64;
MATSSMKSIP MAIPSFSMCH KLELLKEGKT RDVPKAEEDE GLSCEFQEML DSLPKERGWR
TRYLYLFQGF WCQAKEIQAI MSFQKHFQSL ENDVVLATIP KSGTTWLKAL TFTILNRHRF
DPVASSTNHP LFTSNPHDLV PFFEYKLYAN GDVPDLSGLA SPRTFATHLP FGSLKETIEK
PGVKVVYLCR NPFDTFISSW HYTNNIKSES VSPVLLDQAF DLYCRGVIGF GPFWEHMLGY
WRESLKRPEK VFFLRYEDLK DDIETNLKRL ATFLELPFTE EEERKGVVKA IAELCSFENL
KKLEVNKSNK SIKNFENRFL FRKGEVSDWV NYLSPSQVER LSALVDDKLG GSGLTFRLS
