ID A0A099Z1X6_TINGU Unreviewed; 294 AA.
AC A0A099Z1X6;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Sulfotransferase {ECO:0000256|RuleBase:RU361155};
DE EC=2.8.2.- {ECO:0000256|RuleBase:RU361155};
GN ORFNames=N309_08984 {ECO:0000313|EMBL:KGL75108.1};
OS Tinamus guttatus (White-throated tinamou).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL75108.1, ECO:0000313|Proteomes:UP000053641};
RN [1] {ECO:0000313|EMBL:KGL75108.1, ECO:0000313|Proteomes:UP000053641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL75108.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00024561};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67889;
CC Evidence={ECO:0000256|ARBA:ARBA00024561};
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:0000256|ARBA:ARBA00024579};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67877;
CC Evidence={ECO:0000256|ARBA:ARBA00024579};
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:0000256|ARBA:ARBA00024508};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67893;
CC Evidence={ECO:0000256|ARBA:ARBA00024508};
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:0000256|ARBA:ARBA00024527};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12165;
CC Evidence={ECO:0000256|ARBA:ARBA00024527};
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family.
CC {ECO:0000256|ARBA:ARBA00005771, ECO:0000256|RuleBase:RU361155}.
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DR EMBL; KL887657; KGL75108.1; -; Genomic_DNA.
DR RefSeq; XP_010209785.1; XM_010211483.1.
DR AlphaFoldDB; A0A099Z1X6; -.
DR STRING; 94827.A0A099Z1X6; -.
DR GeneID; 104564846; -.
DR KEGG; tgt:104564846; -.
DR CTD; 27284; -.
DR OrthoDB; 3083090at2759; -.
DR Proteomes; UP000053641; Unassembled WGS sequence.
DR GO; GO:0004062; F:aryl sulfotransferase activity; IEA:UniProt.
DR GO; GO:0051923; P:sulfation; IEA:UniProt.
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:SF14; SULFOTRANSFERASE 1B1; 1.
DR PANTHER; PTHR11783; SULFOTRANSFERASE SULT; 1.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053641};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361155}.
FT DOMAIN 38..286
FT /note="Sulfotransferase"
FT /evidence="ECO:0000259|Pfam:PF00685"
SQ SEQUENCE 294 AA; 33932 MW; BBEFE58B7AF9656D CRC64;
MASTNSWMRQ PFRMVHGIPM VSTFVPGWDQ VDAFQSHPED IVVATFPKSG TTWMCEVVDM
ILKGGDTEKC KDFIHNRVPM LELVAPGMSA GTELLPKMAS PRIIKTHIPA HILPKSFWEN
HCKVIYLARN AKDVAVSYYH FDLMNKLHPH PGTWAEYLEK FMAGKVAYGS WYDHVKGYWA
RRKEHPILFL FYEDMKEDPQ REIGKVVQFL QRELSPAVLD AIAHHTSFES MRDNPTTNYT
SVPADLMDHH VSPFMRKGIA GDWKNHFTVA QSERFDEDYA RKMAGTDLRF RTEL
//