F3ST_FLACH
ID F3ST_FLACH Reviewed; 312 AA.
AC P52836;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Flavonol 3-sulfotransferase;
DE Short=F3-ST;
DE EC=2.8.2.25;
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], AND FUNCTION.
RC TISSUE=Leaf;
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 SEQUENCE REVISION TO 68-70.
RA Varin L.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 25-38 AND 160-191, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=1309801; DOI=10.1016/s0021-9258(18)46026-7;
RA Varin L., Ibrahim R.K.;
RT "Novel flavonol 3-sulfotransferase. Purification, kinetic properties, and
RT partial amino acid sequence.";
RL J. Biol. Chem. 267:1858-1863(1992).
RN [4]
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 [5]
RP MUTAGENESIS OF LYS-59; GLU-102; ARG-277; GLY-282 AND LYS-285.
RX PubMed=8530475; DOI=10.1074/jbc.270.51.30458;
RA Marsolais F., Varin L.;
RT "Identification of amino acid residues critical for catalysis and
RT cosubstrate binding in the flavonol 3-sulfotransferase.";
RL J. Biol. Chem. 270:30458-30463(1995).
RN [6]
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 rhamnetin > isorhamnetin > quercetin > patuletin > kaempferol >ombuin >
CC tamarixetin, but not quercertagetin, gossypetin or myricetin. O-
CC sulfonation of position 3 of flavonol. May play a role in auxin
CC transport. {ECO:0000269|PubMed:1309801, ECO:0000269|PubMed:16666908,
CC ECO:0000269|PubMed:1741382}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + quercetin = adenosine 3',5'-
CC bisphosphate + H(+) + quercetin 3-sulfate; Xref=Rhea:RHEA:13453,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57694, ChEBI:CHEBI:58254,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343; EC=2.8.2.25;
CC Evidence={ECO:0000269|PubMed:1309801, 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=0.18 uM for rhamnetin {ECO:0000269|PubMed:1309801,
CC ECO:0000269|PubMed:16666908};
CC KM=0.18 uM for isorhamnetin {ECO:0000269|PubMed:1309801,
CC ECO:0000269|PubMed:16666908};
CC KM=0.20 uM for quercetin {ECO:0000269|PubMed:1309801,
CC ECO:0000269|PubMed:16666908};
CC KM=0.25 uM for patuletin {ECO:0000269|PubMed:1309801,
CC ECO:0000269|PubMed:16666908};
CC KM=0.27 uM for kaempferol {ECO:0000269|PubMed:1309801,
CC ECO:0000269|PubMed:16666908};
CC KM=0.20 uM for 3'-phosphoadenosine 5'-phosphosulfate
CC {ECO:0000269|PubMed:1309801, ECO:0000269|PubMed:16666908};
CC Vmax=1.68 nmol/sec/mg enzyme with rhamnetin as substrate
CC {ECO:0000269|PubMed:1309801, ECO:0000269|PubMed:16666908};
CC Vmax=1.58 nmol/sec/mg enzyme with isorhamnetin as substrate
CC {ECO:0000269|PubMed:1309801, ECO:0000269|PubMed:16666908};
CC Vmax=1.36 nmol/sec/mg enzyme with quercetin as substrate
CC {ECO:0000269|PubMed:1309801, ECO:0000269|PubMed:16666908};
CC Vmax=1.35 nmol/sec/mg enzyme with patuletin as substrate
CC {ECO:0000269|PubMed:1309801, ECO:0000269|PubMed:16666908};
CC Vmax=0.70 nmol/sec/mg enzyme with kaempferol as substrate
CC {ECO:0000269|PubMed:1309801, ECO:0000269|PubMed:16666908};
CC pH dependence:
CC Optimum pH is 6.0-8.5. {ECO:0000269|PubMed:1309801,
CC ECO:0000269|PubMed:16666908};
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M84135; AAA33342.2; -; mRNA.
DR PIR; B40216; B40216.
DR AlphaFoldDB; P52836; -.
DR SMR; P52836; -.
DR KEGG; ag:AAA33342; -.
DR SABIO-RK; P52836; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0047894; F:flavonol 3-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; Direct protein sequencing; Transferase.
FT CHAIN 1..312
FT /note="Flavonol 3-sulfotransferase"
FT /id="PRO_0000085178"
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"
FT MUTAGEN 59
FT /note="K->A: Reduction of activity."
FT /evidence="ECO:0000269|PubMed:8530475"
FT MUTAGEN 102
FT /note="E->K: No effect."
FT /evidence="ECO:0000269|PubMed:8530475"
FT MUTAGEN 277
FT /note="R->A,E,K: Reduction of activity."
FT /evidence="ECO:0000269|PubMed:8530475"
FT MUTAGEN 282
FT /note="G->A: Reduction of activity."
FT /evidence="ECO:0000269|PubMed:8530475"
FT MUTAGEN 285
FT /note="K->G: Reduction of activity."
FT /evidence="ECO:0000269|PubMed:8530475"
SQ SEQUENCE 312 AA; 36484 MW; 057A32C325DF86B5 CRC64;
MEDIIKTLPQ HTCSFLKHRF TLYKYKDAWN HQEFLEGRIL SEQKFKAHPN DVFLASYPKS
GTTWLKALAF AIITREKFDD STSPLLTTMP HDCIPLLEKD LEKIQENQRN SLYTPISTHF
HYKSLPESAR TSNCKIVYIY RNMKDVIVSY YHFLRQIVKL SVEEAPFEEA FDEFCQGISS
CGPYWEHIKG YWKASLEKPE IFLFLKYEDM KKDPVPSVKK LADFIGHPFT PKEEEAGVIE
DIVKLCSFEK LSSLEVNKSG MHRPEEAHSI ENRLYFRKGK DGDWKNYFTD EMTQKIDKLI
DEKLGATGLV LK
