ID   ST1A1_MACFA             Reviewed;         295 AA.
AC   P52846;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=Sulfotransferase 1A1;
DE            Short=ST1A1;
DE            EC=2.8.2.1 {ECO:0000250|UniProtKB:P50225};
DE   AltName: Full=Aryl sulfotransferase;
DE   AltName: Full=Phenol sulfotransferase {ECO:0000303|Ref.1};
DE   AltName: Full=Phenol-sulfating phenol sulfotransferase;
DE            Short=P-PST;
GN   Name=SULT1A1; Synonyms=STP;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Ogura K., Satsukawa M., Okuda H., Watabe T.;
RT   "cDNA cloning and bacterial expression of monkey liver phenol
RT   sulfotransferase.";
RL   Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC       (PAPS) as sulfonate donor to catalyze the sulfate conjugation of a wide
CC       variety of acceptor molecules bearing a hydroxyl or an amine groupe.
CC       Sulfonation increases the water solubility of most compounds, and
CC       therefore their renal excretion, but it can also result in
CC       bioactivation to form active metabolites. Displays broad substrate
CC       specificity for small phenolic compounds. Plays an important role in
CC       the sulfonation of endogenous molecules such as steroid hormones and
CC       3,3'-diiodothyronin (By similarity). Mediates the sulfate conjugation
CC       of a variety of xenobiotics, including the drugs acetaminophen and
CC       minoxidil (By similarity). Mediates also the metabolic activation of
CC       carcinogenic N-hydroxyarylamines leading to highly reactive
CC       intermediates capable of forming DNA adducts, potentially resulting in
CC       mutagenesis (By similarity). May play a role in gut microbiota-host
CC       metabolic interaction. O-sulfonates 4-ethylphenol (4-EP), a dietary
CC       tyrosine-derived metabolite produced by gut bacteria. The product 4-EPS
CC       crosses the blood-brain barrier and may negatively regulate
CC       oligodendrocyte maturation and myelination, affecting the functional
CC       connectivity of different brain regions associated with the limbic
CC       system. {ECO:0000250|UniProtKB:P17988, ECO:0000250|UniProtKB:P50225}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-
CC         bisphosphate + an aryl sulfate + H(+); Xref=Rhea:RHEA:12164,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33853, ChEBI:CHEBI:58339,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:140317; EC=2.8.2.1;
CC         Evidence={ECO:0000250|UniProtKB:P50225};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12165;
CC         Evidence={ECO:0000250|UniProtKB:P50225};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17beta-estradiol + 3'-phosphoadenylyl sulfate = 17beta-
CC         estradiol 3-sulfate + adenosine 3',5'-bisphosphate + H(+);
CC         Xref=Rhea:RHEA:52372, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469,
CC         ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136582;
CC         Evidence={ECO:0000250|UniProtKB:P50225};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52373;
CC         Evidence={ECO:0000250|UniProtKB:P50225};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + 4-ethylphenol = 4-ethylphenyl
CC         sulfate + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:70607,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:49584, ChEBI:CHEBI:58339,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:133681;
CC         Evidence={ECO:0000250|UniProtKB:P50225};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70608;
CC         Evidence={ECO:0000250|UniProtKB:P50225};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P50225}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P17988}.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR   EMBL; D85514; BAA12822.1; -; mRNA.
DR   PIR; G02924; G02924.
DR   AlphaFoldDB; P52846; -.
DR   SMR; P52846; -.
DR   STRING; 9541.ENSMFAP00000042972; -.
DR   eggNOG; KOG1584; Eukaryota.
DR   BRENDA; 2.8.2.1; 1793.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0050656; F:3'-phosphoadenosine 5'-phosphosulfate binding; ISS:UniProtKB.
DR   GO; GO:0004062; F:aryl sulfotransferase activity; ISS:UniProtKB.
DR   GO; GO:0050294; F:steroid sulfotransferase activity; ISS:UniProtKB.
DR   GO; GO:0006584; P:catecholamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0008210; P:estrogen metabolic process; ISS:UniProtKB.
DR   GO; GO:0042403; P:thyroid hormone metabolic process; ISS:UniProtKB.
DR   GO; GO:0006805; P:xenobiotic metabolic process; ISS:UniProtKB.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000863; Sulfotransferase_dom.
DR   PANTHER; PTHR11783:SF324; SULFOTRANSFERASE 1A3-RELATED; 1.
DR   PANTHER; PTHR11783; SULFOTRANSFERASE SULT; 1.
DR   Pfam; PF00685; Sulfotransfer_1; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   2: Evidence at transcript level;
KW   Catecholamine metabolism; Cytoplasm; Lipid metabolism; Phosphoprotein;
KW   Reference proteome; Steroid metabolism; Transferase.
FT   CHAIN           1..295
FT                   /note="Sulfotransferase 1A1"
FT                   /id="PRO_0000085129"
FT   ACT_SITE        108
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         48..53
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:P50225"
FT   BINDING         106..108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P50225"
FT   BINDING         130
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:P50225"
FT   BINDING         138
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:P50225"
FT   BINDING         193
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:P50225"
FT   BINDING         227..232
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:P50225"
FT   BINDING         255..259
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:P50225"
FT   MOD_RES         138
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P17988"
SQ   SEQUENCE   295 AA;  34239 MW;  BD51639D1570A841 CRC64;
     MELIQDTSRP PLEYVKGVPL IKYFAEALGP LQSFRARPDD LLISTYPKSG TTWVSQILDM
     IYQGGDLEKC RRAPIFMRVP FLEFKVPGIP SGMETLKDTP APRLLKTHLP LALLPQTLLD
     QKVKVVYVAR NAKDVAVSYY HFYHMAKVHP EPGTWDSFLE KFMAGEVSYG SWYQHVQEWW
     ELSHTHPVLY LFYEDMKENP KREIWKILEF VGRSLPEETV DLMVQHTSFK EMKKNPMANY
     TTIPQELMDH SISPFMRKGM TGDWKTTFTV AQNEHFDVDY AEKMAGCSLS FRSEL
//