ST1B1_BOVIN
ID ST1B1_BOVIN Reviewed; 296 AA.
AC Q3T0Y3;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Sulfotransferase 1B1;
DE Short=ST1B1;
DE EC=2.8.2.1 {ECO:0000269|PubMed:25539458};
DE AltName: Full=Sulfotransferase family cytosolic 1B member 1;
GN Name=SULT1B1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25539458; DOI=10.3109/00498254.2014.997325;
RA Choughule K.V., Locuson C.W., Coughtrie M.W.;
RT "Characterization of bovine phenol sulfotransferases: evidence of a major
RT role for SULT1B1 in the liver.";
RL Xenobiotica 45:495-502(2015).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the sulfate conjugation of
CC dopamine small phenols such as 1-naphthol and 4-nitrophenol
CC (PubMed:25539458). Catalyzes also the sulfate conjugation of dopamine
CC and thyroid hormones, including 3,3'-diiodothyronine, triidothyronine
CC (T3) and reverse triiodothyronine (rT3) (By similarity). May play a
CC role in gut microbiota-host metabolic interaction. O-sulfonates 4-
CC ethylphenol (4-EP), a dietary tyrosine-derived metabolite produced by
CC gut bacteria. The product 4-EPS crosses the blood-brain barrier and may
CC negatively regulate oligodendrocyte maturation and myelination,
CC affecting the functional connectivity of different brain regions
CC associated with the limbic system. {ECO:0000250|UniProtKB:O43704,
CC ECO:0000269|PubMed:25539458}.
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:0000269|PubMed:25539458};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12165;
CC Evidence={ECO:0000269|PubMed:25539458};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3,3',5-triiodo-L-thyronine =
CC 3,3',5-triiodo-L-thyronine sulfate + adenosine 3',5'-bisphosphate +
CC H(+); Xref=Rhea:RHEA:67876, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:176511, ChEBI:CHEBI:533015;
CC Evidence={ECO:0000250|UniProtKB:O43704};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67877;
CC Evidence={ECO:0000250|UniProtKB:O43704};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3,3',5'-triiodo-L-thyronine =
CC 3,3',5'-triiodo-L-thyronine sulfate + adenosine 3',5'-bisphosphate +
CC H(+); Xref=Rhea:RHEA:67888, ChEBI:CHEBI:15378, ChEBI:CHEBI:57261,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:176513;
CC Evidence={ECO:0000250|UniProtKB:O43704};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67889;
CC Evidence={ECO:0000250|UniProtKB:O43704};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3,3'-diiodo-L-thyronine = 3,3'-
CC diiodo-L-thyronine sulfate + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:67892, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:176514, ChEBI:CHEBI:176515;
CC Evidence={ECO:0000250|UniProtKB:O43704};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67893;
CC Evidence={ECO:0000250|UniProtKB:O43704};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + dopamine = adenosine 3',5'-
CC bisphosphate + dopamine 3-O-sulfate + H(+); Xref=Rhea:RHEA:67880,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:59905, ChEBI:CHEBI:133524;
CC Evidence={ECO:0000250|UniProtKB:O43704};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67881;
CC Evidence={ECO:0000250|UniProtKB:O43704};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + dopamine = adenosine 3',5'-
CC bisphosphate + dopamine 4-O-sulfate + H(+); Xref=Rhea:RHEA:67884,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:59905, ChEBI:CHEBI:133529;
CC Evidence={ECO:0000250|UniProtKB:O43704};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67885;
CC Evidence={ECO:0000250|UniProtKB:O43704};
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:O43704};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70608;
CC Evidence={ECO:0000250|UniProtKB:O43704};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=31 uM for 4-nitrophenol {ECO:0000269|PubMed:25539458};
CC Vmax=3.5 umol/min/mg enzyme with 4-nitropenol as substrate
CC {ECO:0000269|PubMed:25539458};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:25539458}.
CC -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:25539458}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; BC102208; AAI02209.1; -; mRNA.
DR RefSeq; NP_001069291.1; NM_001075823.2.
DR RefSeq; XP_005208096.1; XM_005208039.3.
DR RefSeq; XP_005208098.1; XM_005208041.3.
DR RefSeq; XP_010804466.1; XM_010806164.2.
DR RefSeq; XP_015327144.1; XM_015471658.1.
DR AlphaFoldDB; Q3T0Y3; -.
DR SMR; Q3T0Y3; -.
DR STRING; 9913.ENSBTAP00000001650; -.
DR PaxDb; Q3T0Y3; -.
DR PeptideAtlas; Q3T0Y3; -.
DR Ensembl; ENSBTAT00000001650; ENSBTAP00000001650; ENSBTAG00000001249.
DR GeneID; 521920; -.
DR KEGG; bta:521920; -.
DR CTD; 27284; -.
DR VEuPathDB; HostDB:ENSBTAG00000001249; -.
DR VGNC; VGNC:53777; SULT1B1.
DR eggNOG; KOG1584; Eukaryota.
DR GeneTree; ENSGT00940000161848; -.
DR HOGENOM; CLU_027239_1_2_1; -.
DR InParanoid; Q3T0Y3; -.
DR OMA; CAFVSNW; -.
DR OrthoDB; 780670at2759; -.
DR TreeFam; TF321745; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000001249; Expressed in rumen papilla and 82 other tissues.
DR ExpressionAtlas; Q3T0Y3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004062; F:aryl sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; IEA:Ensembl.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0006068; P:ethanol catabolic process; IEA:Ensembl.
DR GO; GO:0009812; P:flavonoid metabolic process; IEA:Ensembl.
DR GO; GO:0051923; P:sulfation; IDA:UniProtKB.
DR GO; GO:0042403; P:thyroid hormone metabolic process; ISS:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; IEA:Ensembl.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR InterPro; IPR033289; SULT1B1.
DR PANTHER; PTHR11783:SF14; PTHR11783:SF14; 1.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..296
FT /note="Sulfotransferase 1B1"
FT /id="PRO_0000284968"
FT ACT_SITE 109
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:O43704"
FT BINDING 107..109
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O43704"
FT BINDING 139
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O43704"
FT BINDING 194
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O43704"
FT BINDING 228..233
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O43704"
FT BINDING 258..260
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O43704"
SQ SEQUENCE 296 AA; 34674 MW; 8A44653780078275 CRC64;
MTSPKDVLRK NLKLIHGCPI TYAFANNWEK IEQFQSRPDD IMIVTYPKSG TTWISEIVDM
VLHDGDVEKC KRDVITAKVP MLELALPGLR TSGLEQLEKN PSPRVVKTHL PIDLIPKSFW
ENNCKIIYLA RNAKDVAVSF YHFDLMNNLQ PLPGTWGEYL EKFLTGNVAY GSWFNHVKSW
WKKKEGHPIL FLFYEDMKEN PKQEIKKVVR FLEKNLDDEI LDKIIYHTSF EMMKDNPLVN
YTHLPSEVMD HSKSSFMRKG IAGDWKNYFT VAQNEKFDAI YKKEMSETEL QFRTEI
