ST6B1_GORGO
ID ST6B1_GORGO Reviewed; 303 AA.
AC Q6WG17;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Sulfotransferase 6B1;
DE Short=ST6B1;
DE AltName: Full=Thyroxine sulfotransferase;
DE EC=2.8.2.n2;
GN Name=SULT6B1;
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
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=AAQ23222.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY289789; AAQ23222.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY289783; AAQ23222.1; JOINED; Genomic_DNA.
DR EMBL; AY289784; AAQ23222.1; JOINED; Genomic_DNA.
DR EMBL; AY289785; AAQ23222.1; JOINED; Genomic_DNA.
DR EMBL; AY289786; AAQ23222.1; JOINED; Genomic_DNA.
DR EMBL; AY289787; AAQ23222.1; JOINED; Genomic_DNA.
DR EMBL; AY289788; AAQ23222.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; Q6WG17; -.
DR SMR; Q6WG17; -.
DR STRING; 9593.ENSGGOP00000008043; -.
DR eggNOG; KOG1584; Eukaryota.
DR InParanoid; Q6WG17; -.
DR Proteomes; UP000001519; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0051923; P:sulfation; IBA:GO_Central.
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_0000085170"
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; 34809 MW; 338D51A73727A0EE CRC64;
MADKSKFTEY IDKALEKSKE TALSHLFFTY QGIAYPITMC TSETFQALDT FEARHDDIVL
ASYPKCGSNW ILHIVSELIY AVSKKKYKYP EFPVLECGDS EKYQRMKGFP SPRILATHLH
YDKLPGSIFK NKAKILVIFR NPTDTAVSFF HFHNDVPDIP SYGSWDELFR QFMKGQVSWG
SYFDFAINWN KHLDGDNVKF ILYEDLKENL AAGIKQIPEF LGFFLTGEQI QTISVQSTFQ
AMRAKSQDTH GAVGPFLFRK GEVGDWKNLF SEIQNQEMDE KFKECLAGTS LGAKLKYESY
CQG