ST1B1_CHICK
ID ST1B1_CHICK Reviewed; 296 AA.
AC Q8JG30;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Sulfotransferase 1B1;
DE Short=ST1B1;
DE EC=2.8.2.1 {ECO:0000269|PubMed:15234270};
DE AltName: Full=Sulfotransferase family cytosolic 1B member 1;
GN Name=SULT1B1; Synonyms=SULT1B;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Lymphoid tissue;
RX PubMed=15234270; DOI=10.1016/j.abb.2004.05.008;
RA Wilson L.A., Reyns G.E., Darras V.M., Coughtrie M.W.H.;
RT "cDNA cloning, functional expression, and characterization of chicken
RT sulfotransferases belonging to the SULT1B and SULT1C families.";
RL Arch. Biochem. Biophys. 428:64-72(2004).
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 p-nitrophenol and
CC thyroid hormones, including 3,3'-diiodothyronine, triidothyronine (T3)
CC and reverse triiodothyronine (rT3). {ECO:0000269|PubMed:15234270}.
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:15234270};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12165;
CC Evidence={ECO:0000305|PubMed:15234270};
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:0000269|PubMed:15234270};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67877;
CC Evidence={ECO:0000305|PubMed:15234270};
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:0000269|PubMed:15234270};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67893;
CC Evidence={ECO:0000269|PubMed:15234270};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 uM for 2-bromophenol {ECO:0000269|PubMed:15234270};
CC KM=41 uM for 3,3'-diiodo-L-thyronine (T2)
CC {ECO:0000269|PubMed:15234270};
CC KM=67 uM for 3,3',5-triiodo-L-thyronine (T3)
CC {ECO:0000269|PubMed:15234270};
CC KM=22 uM for 3,3',5'-triiodo-L-thyronine (rT3)
CC {ECO:0000269|PubMed:15234270};
CC KM=72 uM for thyroxine {ECO:0000269|PubMed:15234270};
CC Vmax=22 nmol/min/mg enzyme with 3,3'-diiodo-L-thyronine as substrate
CC {ECO:0000269|PubMed:15234270};
CC Vmax=2.3 nmol/min/mg enzyme with 3,3',5-triiodo-L-thyronine as
CC substrate {ECO:0000269|PubMed:15234270};
CC Vmax=0.1 nmol/min/mg enzyme with thyroxyne as substrate
CC {ECO:0000269|PubMed:15234270};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43704}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; AJ494980; CAD41949.1; -; mRNA.
DR RefSeq; NP_989876.1; NM_204545.1.
DR AlphaFoldDB; Q8JG30; -.
DR SMR; Q8JG30; -.
DR STRING; 9031.ENSGALP00000019258; -.
DR PaxDb; Q8JG30; -.
DR Ensembl; ENSGALT00000019283; ENSGALP00000019258; ENSGALG00000023120.
DR GeneID; 395227; -.
DR KEGG; gga:395227; -.
DR CTD; 27284; -.
DR VEuPathDB; HostDB:geneid_395227; -.
DR eggNOG; KOG1584; Eukaryota.
DR GeneTree; ENSGT00940000161848; -.
DR HOGENOM; CLU_027239_1_2_1; -.
DR InParanoid; Q8JG30; -.
DR OMA; PVQFLPQ; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; Q8JG30; -.
DR TreeFam; TF321745; -.
DR Reactome; R-GGA-156584; Cytosolic sulfonation of small molecules.
DR PRO; PR:Q8JG30; -.
DR Proteomes; UP000000539; Chromosome 4.
DR Bgee; ENSGALG00000023120; Expressed in kidney and 11 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004062; F:aryl sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0051923; P:sulfation; IDA:UniProtKB.
DR GO; GO:0042403; P:thyroid hormone metabolic process; IDA:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; IEA:InterPro.
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_0000085164"
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; 34074 MW; 487AB790416995F5 CRC64;
MGTVDAYLRQ PWSTVHAIPM VSAFAQNWER VDNFQSRPDD IVVATFPKSG TTWISEIVDM
ILQGGDPKKC KRDAIVNRVP MLEFAAPGQM PAGTEQLENM PSPRIIKTHI PADILPKSFW
DKSCKMIYVG RNAKDVAVSY YHFDLMNKLH PHPGTWDQYL EAFMAGKVAY GSWFDHVRGY
WERRQEHPIL YLFYEDMKED LRREVAKVAQ FLGRELTEVA LDAIAHHTSF EAMRDNPSTN
YSVVPSQLMD HGISPFMRKG ITGDWKNHFT VAQSAHFDQY YAQKMAGTDL RFRTHI
