ID   GSTO_APLCA              Reviewed;          92 AA.
AC   P81124;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Probable glutathione transferase;
DE            EC=2.5.1.18;
DE   AltName: Full=Glutathione-dependent dehydroascorbate reductase;
DE            EC=1.8.5.1;
DE   AltName: Full=Monomethylarsonic acid reductase;
DE            Short=MMA(V) reductase;
DE            EC=1.20.4.2;
DE   AltName: Full=Protein 9;
DE   Flags: Fragment;
OS   Aplysia californica (California sea hare).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Tectipleura; Aplysiida; Aplysioidea;
OC   Aplysiidae; Aplysia.
OX   NCBI_TaxID=6500;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-36 AND 56-92, NUCLEOTIDE SEQUENCE [MRNA] OF 37-55,
RP   AND INDUCTION.
RC   TISSUE=Abdominal ganglion {ECO:0000269|PubMed:8183885};
RX   PubMed=8183885; DOI=10.1073/pnas.91.10.4150;
RA   Noel F., Koumenis C., Nunez-Regueiro M., Raju U., Byrne J.H., Eskin A.;
RT   "Effects on protein synthesis produced by pairing depolarization with
RT   serotonin, an analogue of associative learning in Aplysia.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:4150-4154(1994).
CC   -!- FUNCTION: Exhibits glutathione-dependent thiol transferase activity.
CC       Has dehydroascorbate reductase activity and may contribute to the
CC       recycling of ascorbic acid. Participates in the biotransformation of
CC       inorganic arsenic and reduces monomethylarsonic acid (MMA) (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + RX = a halide anion + an S-substituted
CC         glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:90779; EC=2.5.1.18;
CC         Evidence={ECO:0000250|UniProtKB:P78417};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + L-dehydroascorbate = glutathione disulfide +
CC         L-ascorbate; Xref=Rhea:RHEA:24424, ChEBI:CHEBI:38290,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58539; EC=1.8.5.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + H(+) + methylarsonate = glutathione disulfide
CC         + H2O + methylarsonous acid; Xref=Rhea:RHEA:15969, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17826, ChEBI:CHEBI:33409,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.20.4.2;
CC   -!- INDUCTION: By treatment with KCl and serotonin.
CC       {ECO:0000269|PubMed:8183885}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Omega family.
CC       {ECO:0000255}.
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DR   AlphaFoldDB; P81124; -.
DR   SMR; P81124; -.
DR   GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050610; F:methylarsonate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF13417; GST_N_3; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Oxidoreductase; Transferase.
FT   CHAIN           <1..>92
FT                   /note="Probable glutathione transferase"
FT                   /id="PRO_0000291311"
FT   DOMAIN          <1..71
FT                   /note="GST N-terminal"
FT   ACT_SITE        3
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P78417"
FT   BINDING         30
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H4Y5"
FT   BINDING         43
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P78417"
FT   BINDING         55..56
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H4Y5"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:8183885"
FT   NON_TER         92
FT                   /evidence="ECO:0000303|PubMed:8183885"
SQ   SEQUENCE   92 AA;  10351 MW;  F7C6B9ECA950CF14 CRC64;
     RTCPYAQRAR LIIAAKGISA DLVNVDLNKK PDHFFDLNPY GEVPVVLHNG GHVYESLIAA
     EYLEEAFPDP PLFAKEALVR ANERIYFNHA TK