ID D2I2Q7_AILME Unreviewed; 293 AA.
AC D2I2Q7;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Sulfotransferase {ECO:0000256|RuleBase:RU361155};
DE EC=2.8.2.- {ECO:0000256|RuleBase:RU361155};
DE Flags: Fragment;
GN ORFNames=PANDA_019697 {ECO:0000313|EMBL:EFB15166.1};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|EMBL:EFB15166.1};
RN [1] {ECO:0000313|EMBL:EFB15166.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(24S)-hydroxycholesterol + 3'-phosphoadenylyl sulfate = (24S)-
CC hydroxycholesterol 3-sulfate + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:52348, ChEBI:CHEBI:15378, ChEBI:CHEBI:34310,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136567;
CC Evidence={ECO:0000256|ARBA:ARBA00043800};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52349;
CC Evidence={ECO:0000256|ARBA:ARBA00043800};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol + 3'-phosphoadenylyl sulfate = 17beta-
CC estradiol 3-sulfate + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:52372, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136582;
CC Evidence={ECO:0000256|ARBA:ARBA00043684};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52373;
CC Evidence={ECO:0000256|ARBA:ARBA00043684};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3beta-hydroxyandrost-5-en-17-one
CC = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate +
CC H(+); Xref=Rhea:RHEA:51216, ChEBI:CHEBI:15378, ChEBI:CHEBI:28689,
CC ChEBI:CHEBI:57905, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343;
CC Evidence={ECO:0000256|ARBA:ARBA00043689};
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:0000256|ARBA:ARBA00033673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70608;
CC Evidence={ECO:0000256|ARBA:ARBA00033673};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + estrone = adenosine 3',5'-
CC bisphosphate + estrone 3-sulfate + H(+); Xref=Rhea:RHEA:15973,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17263, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:60050; EC=2.8.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00043703};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15974;
CC Evidence={ECO:0000256|ARBA:ARBA00043703};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family.
CC {ECO:0000256|ARBA:ARBA00005771, ECO:0000256|RuleBase:RU361155}.
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DR EMBL; GL194200; EFB15166.1; -; Genomic_DNA.
DR AlphaFoldDB; D2I2Q7; -.
DR HOGENOM; CLU_027239_1_2_1; -.
DR InParanoid; D2I2Q7; -.
DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR GO; GO:0008146; F:sulfotransferase activity; IEA:InterPro.
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:SF53; SULFOTRANSFERASE 1E1; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00022665};
KW Steroid-binding {ECO:0000256|ARBA:ARBA00022665};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361155}.
FT DOMAIN 36..285
FT /note="Sulfotransferase"
FT /evidence="ECO:0000259|Pfam:PF00685"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EFB15166.1"
FT NON_TER 293
FT /evidence="ECO:0000313|EMBL:EFB15166.1"
SQ SEQUENCE 293 AA; 34593 MW; 767E66096DC2FFBB CRC64;
SSKSGYGTFF GKVHGILMYK DFMKYWDDVE TFQARPDDIV IVTYPRSGTT WVSEIIYMIC
KEGDVEKCKE DVIFNRVPYL ECRKEEIMNG VKQLKQMASP RIVKTHLPAE LFPASFWEKN
CKMIYLCRNA KDVVVSYYYF FQMVAGHPDP GSFQEFVEKF MDGEVPYGSW YKHAKSWWEK
RDNPHALFLF YEDMKEDIRK EVIKVIQFLG RQPSEELVDK IVQHTSFQEM KNNASTNYTT
LPDEIMNQKV SPFMRKGIAG DWKNHFTVAL NEKFDKHYEQ EMKGSTLKLR TEI
//
