ID   ST6B1_PANTR             Reviewed;         303 AA.
AC   Q6WG18;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 2.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Sulfotransferase 6B1;
DE            Short=ST6B1;
DE   AltName: Full=Thyroxine sulfotransferase;
DE            EC=2.8.2.n2;
GN   Name=SULT6B1;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=14676822; DOI=10.1038/sj.tpj.6500223;
RA   Freimuth R.R., Wiepert M., Chute C.G., Wieben E.D., Weinshilboum R.M.;
RT   "Human cytosolic sulfotransferase database mining: identification of seven
RT   novel genes and pseudogenes.";
RL   Pharmacogenomics J. 4:54-65(2004).
CC   -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC       (PAPS) as sulfonate donor to catalyze the sulfate conjugation of
CC       thyroxine. Involved in the metabolism of thyroxine (By similarity).
CC       {ECO:0000250|UniProtKB:P0CC03}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + thyroxine = adenosine 3',5'-
CC         bisphosphate + H(+) + thyroxine sulfate; Xref=Rhea:RHEA:26422,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC         ChEBI:CHEBI:58910, ChEBI:CHEBI:305790; EC=2.8.2.n2;
CC         Evidence={ECO:0000250|UniProtKB:P0CC03};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P0CC03}.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAQ23221.1; Type=Erroneous initiation; Evidence={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; AY289782; AAQ23221.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AY289776; AAQ23221.1; JOINED; Genomic_DNA.
DR   EMBL; AY289777; AAQ23221.1; JOINED; Genomic_DNA.
DR   EMBL; AY289778; AAQ23221.1; JOINED; Genomic_DNA.
DR   EMBL; AY289779; AAQ23221.1; JOINED; Genomic_DNA.
DR   EMBL; AY289780; AAQ23221.1; JOINED; Genomic_DNA.
DR   EMBL; AY289781; AAQ23221.1; JOINED; Genomic_DNA.
DR   AlphaFoldDB; Q6WG18; -.
DR   SMR; Q6WG18; -.
DR   STRING; 9598.ENSPTRP00000020325; -.
DR   PaxDb; Q6WG18; -.
DR   eggNOG; KOG1584; Eukaryota.
DR   InParanoid; Q6WG18; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0005829; C:cytosol; 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   3: Inferred from homology;
KW   Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..303
FT                   /note="Sulfotransferase 6B1"
FT                   /id="PRO_0000085172"
FT   ACT_SITE        118
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P49891"
FT   BINDING         65..70
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:P49891"
FT   BINDING         140
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:P49891"
FT   BINDING         148
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:P49891"
FT   BINDING         203
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:P49891"
FT   BINDING         237..242
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:P49891"
FT   BINDING         259..261
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:P49891"
SQ   SEQUENCE   303 AA;  34820 MW;  4EA8F57A2ED52052 CRC64;
     MADKSKFIEY IDEALEKSKE TALSHLFFTY QGIPYPITMC TSETFQALDT FEARHDDIVL
     ASYPKCGSNW ILHIVSELIY AVSKKKYEYP EFPVLECGDS EKYQRMKGFP SPRILATHLH
     YDKLPGSIFK NKAKILVIFR NPKDTAVSFF HFHNDVPDIP SYGSWDEFFR QLMKGQVSWG
     SYFDFAINWN KHLDGDNVKF ILYEDLKENL AAGIKQIAEF LGFFLTGEQI QTISVQSTFQ
     AMRAKSQDTH GAVGPFLFRK GEVGDWKNLF GEIQNQEMDE KFKECLAGTS LGAKLKYESY
     CQG