SOT10_ARATH
ID SOT10_ARATH Reviewed; 333 AA.
AC O82330;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Cytosolic sulfotransferase 10;
DE Short=AtSOT10;
DE EC=2.8.2.-;
DE AltName: Full=Sulfotransferase 4a;
DE Short=AtST4a;
GN Name=SOT10; Synonyms=ST4A; OrderedLocusNames=At2g14920; ORFNames=T26I20;
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=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 [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 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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION BY
RP TRANS-ZEATIN, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=17039368; DOI=10.1007/s00425-006-0413-y;
RA Marsolais F., Boyd J., Paredes Y., Schinas A.M., Garcia M., Elzein S.,
RA Varin L.;
RT "Molecular and biochemical characterization of two brassinosteroid
RT sulfotransferases from Arabidopsis, AtST4a (At2g14920) and AtST1
RT (At2g03760).";
RL Planta 225:1233-1244(2007).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to specifically catalyze the sulfate
CC conjugation of brassinosteroids, including castasterone (CS),
CC brassinolide (BL), related 24-epimers, and the naturally occurring
CC (22R, 23R)-28-homobrassinosteroids. No activity on phenolic acids,
CC desulfo-glucosinolates, flavonoids, steroids, gibberellic acids,
CC cytokinins, phenylpropanoids, hydroxyjasmonates and coumarins.
CC {ECO:0000269|PubMed:17039368}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16 uM for brassinolide {ECO:0000269|PubMed:17039368};
CC KM=14 uM for castasterone {ECO:0000269|PubMed:17039368};
CC KM=43 uM for 24-epibrassinolide {ECO:0000269|PubMed:17039368};
CC KM=19 uM for (22R, 23R)-28-homobrassinolide
CC {ECO:0000269|PubMed:17039368};
CC KM=7 uM for (22R, 23R)-28-homocastasterone
CC {ECO:0000269|PubMed:17039368};
CC KM=0.4 uM for 3'-phospho-5'-adenylyl sulfate
CC {ECO:0000269|PubMed:17039368};
CC Vmax=5 pmol/sec/mg enzyme with brassinolide as substrate
CC {ECO:0000269|PubMed:17039368};
CC Vmax=3 pmol/sec/mg enzyme with castasterone as substrate
CC {ECO:0000269|PubMed:17039368};
CC Vmax=10 pmol/sec/mg enzyme with 24-epibrassinolide as substrate
CC {ECO:0000269|PubMed:17039368};
CC Vmax=34 pmol/sec/mg enzyme with (22R, 23R)-28-homobrassinolide as
CC substrate {ECO:0000269|PubMed:17039368};
CC Vmax=19 pmol/sec/mg enzyme with (22R, 23R)-28-homocastasterone as
CC substrate {ECO:0000269|PubMed:17039368};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in roots. {ECO:0000269|PubMed:17039368}.
CC -!- INDUCTION: Down-regulated by trans-zeatin.
CC {ECO:0000269|PubMed:17039368}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; AC005396; AAC61289.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06351.1; -; Genomic_DNA.
DR PIR; A84523; A84523.
DR RefSeq; NP_179098.1; NM_127056.1.
DR AlphaFoldDB; O82330; -.
DR SMR; O82330; -.
DR BioGRID; 1340; 1.
DR STRING; 3702.AT2G14920.1; -.
DR PaxDb; O82330; -.
DR PRIDE; O82330; -.
DR ProteomicsDB; 232547; -.
DR EnsemblPlants; AT2G14920.1; AT2G14920.1; AT2G14920.
DR GeneID; 815981; -.
DR Gramene; AT2G14920.1; AT2G14920.1; AT2G14920.
DR KEGG; ath:AT2G14920; -.
DR Araport; AT2G14920; -.
DR TAIR; locus:2060505; AT2G14920.
DR eggNOG; KOG1584; Eukaryota.
DR HOGENOM; CLU_027239_0_1_1; -.
DR InParanoid; O82330; -.
DR OMA; HEQIKRH; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; O82330; -.
DR BioCyc; ARA:AT2G14920-MON; -.
DR BioCyc; MetaCyc:AT2G14920-MON; -.
DR SABIO-RK; O82330; -.
DR PRO; PR:O82330; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82330; baseline and differential.
DR Genevisible; O82330; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0080118; F:brassinosteroid sulfotransferase activity; IDA:TAIR.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0016131; P:brassinosteroid metabolic process; IDA:TAIR.
DR GO; GO:0009735; P:response to cytokinin; 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..333
FT /note="Cytosolic sulfotransferase 10"
FT /id="PRO_0000417058"
FT ACT_SITE 146
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 76..81
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 299..301
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
SQ SEQUENCE 333 AA; 38924 MW; B13B671253C619CF CRC64;
MDEKDRPKNL REEEEKPSEE TKILISSLPW EIDYLGNKLF NYEGYWYSED ILQSIPNIHT
GFQPQETDII LASFYKSGTT WLKALTFALV QRSKHSLEDH QHPLLHHNPH EIVPNLELDL
YLKSSKPDLT KFLSSSSSSP RLFSTHMSLD PLQVPLKENL CKIVYVCRNV KDVMVSVWYF
RQSKKITRAE DYSLEAIFES FCNGVTLHGP FWDHALSYWR GSLEDPKHFL FMRYEDLKAE
PRTQVKRLAE FLDCPFTKEE EDSGSVDKIL ELCSLSNLRS VEINKTRTSS RVDFKSYFRK
GQVGDWKSYM TPEMVDKIDM IIEEKLKGSG LKF
