ID   F3ST_FLABI              Reviewed;         312 AA.
AC   P52835;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Flavonol 3-sulfotransferase;
DE            Short=F3-ST;
DE            EC=2.8.2.-;
OS   Flaveria bidentis (Coastal plain yellowtops) (Ethulia bidentis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Tageteae; Flaveria.
OX   NCBI_TaxID=4224;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7991681; DOI=10.1104/pp.106.2.485;
RA   Ananvoranich S., Varin L., Gulick P., Ibrahim R.;
RT   "Cloning and regulation of flavonol 3-sulfotransferase in cell-suspension
RT   cultures of Flaveria bidentis.";
RL   Plant Physiol. 106:485-491(1994).
CC   -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC       (PAPS) as sulfonate donor to catalyze the sulfate conjugation of
CC       quercetin, rhamnetin and isorhamnetin but not kaempferol. O-sulfation
CC       of position 3 of flavonol. May play a role in auxin transport.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Highest in shoot tips and lowest in mature leaves
CC       and roots.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR   EMBL; U10275; AAA61638.1; -; mRNA.
DR   AlphaFoldDB; P52835; -.
DR   SMR; P52835; -.
DR   KEGG; ag:AAA61638; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008146; F:sulfotransferase activity; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cytoplasm; Transferase.
FT   CHAIN           1..312
FT                   /note="Flavonol 3-sulfotransferase"
FT                   /id="PRO_0000085177"
FT   ACT_SITE        119
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         59..64
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         141
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         207
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         277..279
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   312 AA;  36457 MW;  29D174E8CB663FC2 CRC64;
     MEDIIKTLPQ HTCSFLKQRF TLYKYQDVWN HQEFLEGRML SEQTFKAHPN DVFLASYPKS
     GTTWLKALAF AIITREKFDD STSPLLTTMP HDCIPLLEKD LEKIQENQRN SLYTPISTHF
     HYKSLPESAR TSNCKIVYIY RNMKDVIVSY YHFLRQIVKL SVEEAPFEEA VDEFCQGISS
     CGPYWEHILG YWKASLEKPE IFLFLKYEDM KKDPVPSVKK LADFIGHPFT PKEEEAGVIE
     NIIKLCSFEK LSSLEVNKSG MHRPEEAHSI ENRLYFRKGK DGDWKNYFTD EMIEKIDKLI
     DEKLGATGLV LK