LST_PHOPY
ID LST_PHOPY Reviewed; 370 AA.
AC A0A173GP47;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Luciferin sulfotransferase {ECO:0000303|PubMed:27227579};
DE EC=2.8.2.- {ECO:0000269|PubMed:27227579};
GN Name=LST {ECO:0000303|PubMed:27227579, ECO:0000312|EMBL:ANH56803.1};
OS Photinus pyralis (Common eastern firefly) (Lampyris pyralis).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Elateriformia; Elateroidea;
OC Lampyridae; Lampyrinae; Photinus.
OX NCBI_TaxID=7054;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND BIOTECHNOLOGY.
RX PubMed=27227579; DOI=10.1021/acs.biochem.6b00402;
RA Fallon T.R., Li F.S., Vicent M.A., Weng J.K.;
RT "Sulfoluciferin is Biosynthesized by a Specialized Luciferin
RT Sulfotransferase in Fireflies.";
RL Biochemistry 55:3341-3344(2016).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=28004739; DOI=10.1038/srep38556;
RA Al-Wathiqui N., Fallon T.R., South A., Weng J.K., Lewis S.M.;
RT "Molecular characterization of firefly nuptial gifts: a multi-omics
RT approach sheds light on postcopulatory sexual selection.";
RL Sci. Rep. 6:38556-38556(2016).
CC -!- FUNCTION: Catalyzes the production of firefly sulfoluciferin from
CC luciferin using the sulfo-donor 3'-phosphoadenylyl sulfate (PAPS). Is
CC also able to catalyze the reverse reaction, i.e. the adenosine 3',5'-
CC bisphosphate-dependent desulfonation of sulfoluciferin. Can use either
CC D- or L-luciferin stereoisomer as substrate. Sulfoluciferin, which is
CC not a substrate of P.pyralis luciferase, likely serves as a luciferin
CC storage form in fireflies. {ECO:0000269|PubMed:27227579}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + firefly D-luciferin = adenosine
CC 3',5'-bisphosphate + firefly D-sulfoluciferin + H(+);
CC Xref=Rhea:RHEA:59300, ChEBI:CHEBI:15378, ChEBI:CHEBI:58038,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:143025;
CC Evidence={ECO:0000269|PubMed:27227579};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + firefly L-luciferin = adenosine
CC 3',5'-bisphosphate + firefly L-sulfoluciferin + H(+);
CC Xref=Rhea:RHEA:59304, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:138329, ChEBI:CHEBI:143028;
CC Evidence={ECO:0000269|PubMed:27227579};
CC -!- ACTIVITY REGULATION: Sulfoluciferin formation is inhibited by the
CC product adenosine 3',5'-bisphosphate. {ECO:0000269|PubMed:27227579}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is at least 3 sec(-1) with D-luciferin as substrate.
CC {ECO:0000269|PubMed:27227579};
CC -!- BIOTECHNOLOGY: LST may find use as a new tool to modulate existing
CC biotechnological applications of the firefly bioluminescent system.
CC {ECO:0000305|PubMed:27227579}.
CC -!- MISCELLANEOUS: Both D- and L-luciferin stereoisomers are found within
CC the firefly. L-luciferin is the likely biosynthetic precursor to D-
CC luciferin, though D-luciferin is the major stereoisomer by static
CC abundance. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; KX097998; ANH56803.1; -; mRNA.
DR EMBL; GEZM01002344; JAV97315.1; -; Transcribed_RNA.
DR AlphaFoldDB; A0A173GP47; -.
DR SMR; A0A173GP47; -.
DR BRENDA; 2.8.2.10; 4775.
DR GO; GO:0008146; F:sulfotransferase activity; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Transferase.
FT CHAIN 1..370
FT /note="Luciferin sulfotransferase"
FT /id="PRO_0000446868"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 90..95
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O75897"
FT BINDING 189
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O75897"
FT BINDING 197
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O75897"
FT BINDING 250
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O75897"
FT BINDING 284..289
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O75897"
FT BINDING 316..320
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O75897"
SQ SEQUENCE 370 AA; 43274 MW; E299E8B1EBB6F05D CRC64;
MFASILGKIP QYSTISSKCS LKECRKVKKV ENSDEIGEII HRDFLDPFCN EYVLIGEEET
SLGINYLQFE EEIRTFEIRD SDIIVASYPK AGTTWTQELV WLIGNDLDFK AAEEHLDKRF
PHFELCTIVN FAKMTEMLGS TRPEYIGNSI NYLRDLEGTR FIKTHLTYNL LPEQILNGNR
KPKIIYVMRD PKDVCVSYYH HGRLIQGWRA DFQNFSKVFL SEKIMFGSYW KHVLGYWEHR
DKPNVLILTY EEMKKDLLSV IRKTAQFLDK KLNENKIPQL LKHLSFESMK NNRAVNQQDK
IESRMKHKLV PEQGAFMRSG TSQNYKGEMS EELILKFDEW TKKSISGSSF VTEPIADLYL
NTSQKSVPKM
