ID   F4ST_FLACH              Reviewed;         320 AA.
AC   P52837;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Flavonol 4'-sulfotransferase;
DE            Short=F4-ST;
DE            EC=2.8.2.27;
OS   Flaveria chlorifolia (Clasping yellowtops).
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=4228;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1741382; DOI=10.1073/pnas.89.4.1286;
RA   Varin L., Deluca V., Ibrahim R.K., Brisson N.;
RT   "Molecular characterization of two plant flavonol sulfotransferases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:1286-1290(1992).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP   REGULATION.
RX   PubMed=16666908; DOI=10.1104/pp.90.3.977;
RA   Varin L., Ibrahim R.K.;
RT   "Partial purification and characterization of three flavonol-specific
RT   sulfotransferases from Flaveria chloraefolia.";
RL   Plant Physiol. 90:977-981(1989).
RN   [3]
RP   PAPS-BINDING SITE.
RX   PubMed=7759495; DOI=10.1074/jbc.270.21.12498;
RA   Varin L., Marsolais F., Brisson N.;
RT   "Chimeric flavonol sulfotransferases define a domain responsible for
RT   substrate and position specificities.";
RL   J. Biol. Chem. 270:12498-12502(1995).
CC   -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC       (PAPS) as sulfonate donor to catalyze the sulfate conjugation of
CC       quercetin 3-sulfate > kaempferol 3-sulfate > isorhamnetin 3-sulfate >
CC       patuletin 3-sulfate, but not tamarixetin 3-sulfate. O-sulfation of
CC       position 4' of flavonol. May play a role in auxin transport.
CC       {ECO:0000269|PubMed:16666908}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + quercetin 3-sulfate = adenosine
CC         3',5'-bisphosphate + H(+) + quercetin 3,4'-bissulfate;
CC         Xref=Rhea:RHEA:17205, ChEBI:CHEBI:15378, ChEBI:CHEBI:58254,
CC         ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:58353; EC=2.8.2.27;
CC         Evidence={ECO:0000269|PubMed:16666908};
CC   -!- ACTIVITY REGULATION: No requirement for divalent cations and
CC       insensitive to p-chloromercuribenzoate, iodoacetate, or iodoacetamide.
CC       {ECO:0000269|PubMed:16666908}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.36 uM for quercetin 3-sulfate {ECO:0000269|PubMed:16666908};
CC         KM=0.38 uM for 3'-phosphoadenosine 5'-phosphosulfate
CC         {ECO:0000269|PubMed:16666908};
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:16666908};
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; M84136; AAA33343.1; -; mRNA.
DR   PIR; A40216; A40216.
DR   AlphaFoldDB; P52837; -.
DR   SMR; P52837; -.
DR   KEGG; ag:AAA33343; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0047366; F:quercetin-3-sulfate 4'-sulfotransferase activity; IEA:UniProtKB-EC.
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; Transferase.
FT   CHAIN           1..320
FT                   /note="Flavonol 4'-sulfotransferase"
FT                   /id="PRO_0000085179"
FT   ACT_SITE        129
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         151
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         285..287
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   320 AA;  37255 MW;  6B263659F6CCBCC0 CRC64;
     METTKTQFES MAEMIKKLPQ HTCSSLKGRI TLYKYQDFWG LQNNIEGAIL AQQSFKARPD
     DVFLCSYPKS GTTWLKALAY AIVTREKFDE FTSPLLTNIP HNCIPYIEKD LKKIVENQNN
     SCFTPMATHM PYHVLPKSIL ALNCKMVYIY RNIKDVIVSF YHFGREITKL PLEDAPFEEA
     FDEFYHGISQ FGPYWDHLLG YWKASLERPE VILFLKYEDV KKDPTSNVKR LAEFIGYPFT
     FEEEKEGVIE SIIKLCSFEN LSNLEVNKSG NSKGFLPIEN RLYFRKAKDG DWKNYFTDEM
     TEKIDKLIDE KLSATGLVLK