SOT5_ARATH
ID SOT5_ARATH Reviewed; 323 AA.
AC Q9M1V2;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Cytosolic sulfotransferase 5;
DE Short=AtSOT5;
DE EC=2.8.2.-;
DE AltName: Full=Flavonoid 7-sulfotransferase 3a;
DE Short=AtST3a;
GN Name=SOT5; Synonyms=ST3A; OrderedLocusNames=At3g45070; ORFNames=T14D3.10;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
RA Cheuk R., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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, DEVELOPMENTAL
RP STAGE, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=17095238; DOI=10.1016/j.plaphy.2006.10.004;
RA Gidda S.K., Varin L.;
RT "Biochemical and molecular characterization of flavonoid 7-sulfotransferase
RT from Arabidopsis thaliana.";
RL Plant Physiol. Biochem. 44:628-636(2006).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to specifically catalyze the sulfate
CC conjugation of flavones and flavonols. Strictly specific for the
CC position 7. Substrate preference is kaempferol 3-sulfate > isorhamnetin
CC > kaempferol. {ECO:0000269|PubMed:17095238}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2 uM for kaempferol 3-sulfate {ECO:0000269|PubMed:17095238};
CC KM=6 uM for isorhamnetin {ECO:0000269|PubMed:17095238};
CC KM=3.2 uM for kaempferol {ECO:0000269|PubMed:17095238};
CC KM=11 uM for galangin {ECO:0000269|PubMed:17095238};
CC KM=1.5 uM for quercetin {ECO:0000269|PubMed:17095238};
CC KM=5.1 uM for apigenin 4'-sulfate {ECO:0000269|PubMed:17095238};
CC KM=51 uM for apigenin {ECO:0000269|PubMed:17095238};
CC KM=40.6 uM for chrysin {ECO:0000269|PubMed:17095238};
CC KM=26 uM for 7-hydroxyflavone {ECO:0000269|PubMed:17095238};
CC KM=1 uM for 3'-phospho-5'-adenylyl sulfate
CC {ECO:0000269|PubMed:17095238};
CC Vmax=286 pmol/sec/mg enzyme with kaempferol 3-sulfate as substrate
CC {ECO:0000269|PubMed:17095238};
CC Vmax=232 pmol/sec/mg enzyme with isorhamnetin as substrate
CC {ECO:0000269|PubMed:17095238};
CC Vmax=116 pmol/sec/mg enzyme with kaempferol as substrate
CC {ECO:0000269|PubMed:17095238};
CC Vmax=270 pmol/sec/mg enzyme with galangin as substrate
CC {ECO:0000269|PubMed:17095238};
CC Vmax=24 pmol/sec/mg enzyme with quercetin as substrate
CC {ECO:0000269|PubMed:17095238};
CC Vmax=45 pmol/sec/mg enzyme with apigenin 4'-sulfate as substrate
CC {ECO:0000269|PubMed:17095238};
CC Vmax=370 pmol/sec/mg enzyme with apigenin as substrate
CC {ECO:0000269|PubMed:17095238};
CC Vmax=156 pmol/sec/mg enzyme with chrysin as substrate
CC {ECO:0000269|PubMed:17095238};
CC Vmax=91 pmol/sec/mg enzyme with 7-hydroxyflavone as substrate
CC {ECO:0000269|PubMed:17095238};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:17095238};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in inflorescence stems, roots and
CC siliques. {ECO:0000269|PubMed:17095238}.
CC -!- DEVELOPMENTAL STAGE: Expressed mostly in 5-day old seedlings, at
CC developmental stage 1. {ECO:0000269|PubMed:17095238}.
CC -!- INDUCTION: Up-regulated by trans-zeatin, but not by cold, heat,
CC hypoxia, salt stress, auxins, gibberellins, wounding, etiolation and
CC salicylic acid or methyl jasmonate treatments.
CC {ECO:0000269|PubMed:17095238}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; AL138649; CAB72145.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77988.1; -; Genomic_DNA.
DR EMBL; BT011733; AAS49096.1; -; mRNA.
DR PIR; T47447; T47447.
DR RefSeq; NP_190093.1; NM_114376.2.
DR AlphaFoldDB; Q9M1V2; -.
DR SMR; Q9M1V2; -.
DR STRING; 3702.AT3G45070.1; -.
DR PaxDb; Q9M1V2; -.
DR PRIDE; Q9M1V2; -.
DR ProteomicsDB; 232516; -.
DR EnsemblPlants; AT3G45070.1; AT3G45070.1; AT3G45070.
DR GeneID; 823642; -.
DR Gramene; AT3G45070.1; AT3G45070.1; AT3G45070.
DR KEGG; ath:AT3G45070; -.
DR Araport; AT3G45070; -.
DR TAIR; locus:2096845; AT3G45070.
DR eggNOG; KOG1584; Eukaryota.
DR HOGENOM; CLU_027239_0_1_1; -.
DR InParanoid; Q9M1V2; -.
DR OMA; GWWALRD; -.
DR PhylomeDB; Q9M1V2; -.
DR BioCyc; ARA:AT3G45070-MON; -.
DR PRO; PR:Q9M1V2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M1V2; baseline and differential.
DR Genevisible; Q9M1V2; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:1990135; F:flavonoid sulfotransferase activity; IDA:TAIR.
DR GO; GO:0008146; F:sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0009812; P:flavonoid metabolic process; IDA:UniProtKB.
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..323
FT /note="Cytosolic sulfotransferase 5"
FT /id="PRO_0000417053"
FT ACT_SITE 135
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 69..74
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 157
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 289..291
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
SQ SEQUENCE 323 AA; 37502 MW; 00F9259E9CCF6E89 CRC64;
MEMNLRIEDL NEETKTLISS LPSDKDFTGK TICKYQGCWY THNVLQAVLN FQKSFKPQDT
DIIVASFPKC GTTWLKALTF ALLHRSKQPS HDDDHPLLSN NPHVLVPYFE IDLYLRSENP
DLTKFSSSPR LFSTHVPSHT LQEGLKGSTC KIVYISRNVK DTLVSYWHFF TKKQTDEKII
SSFEDTFEMF CRGVSIFGPF WDHVLSYWRG SLEDPNHVLF MKFEEMKAEP RDQIKKFAEF
LGCPFTKEEE ESGSVDEIID LCSLRNLSSL EINKTGKLNS GRENKMFFRK GEVGDWKNYL
TPEMENKIDM IIQEKLQNSG LKF
