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Database: UniProt
Entry: A0A3B4U9G4_SERDU
LinkDB: A0A3B4U9G4_SERDU
Original site: A0A3B4U9G4_SERDU 
ID   A0A3B4U9G4_SERDU        Unreviewed;       230 AA.
AC   A0A3B4U9G4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Glutathione S-transferase kappa {ECO:0000256|PIRNR:PIRNR006386};
DE            EC=2.5.1.18 {ECO:0000256|PIRNR:PIRNR006386};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000015286.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000015286.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000710,
CC         ECO:0000256|PIRNR:PIRNR006386};
CC   -!- SIMILARITY: Belongs to the GST superfamily. Kappa family.
CC       {ECO:0000256|ARBA:ARBA00006494, ECO:0000256|PIRNR:PIRNR006386}.
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DR   AlphaFoldDB; A0A3B4U9G4; -.
DR   STRING; 41447.ENSSDUP00000015286; -.
DR   Ensembl; ENSSDUT00000015572.1; ENSSDUP00000015286.1; ENSSDUG00000011059.1.
DR   GeneTree; ENSGT00440000033697; -.
DR   Proteomes; UP000261420; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   CDD; cd03021; DsbA_GSTK; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR   InterPro; IPR044088; GSTK.
DR   InterPro; IPR014440; HCCAis_GSTk.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR42943; GLUTATHIONE S-TRANSFERASE KAPPA; 1.
DR   PANTHER; PTHR42943:SF2; GLUTATHIONE S-TRANSFERASE KAPPA 1; 1.
DR   Pfam; PF01323; DSBA; 1.
DR   PIRSF; PIRSF006386; HCCAis_GSTk; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
PE   3: Inferred from homology;
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006386}.
FT   DOMAIN          6..212
FT                   /note="DSBA-like thioredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF01323"
FT   ACT_SITE        15
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006386-1"
SQ   SEQUENCE   230 AA;  25897 MW;  F3961510E98F1CA4 CRC64;
     MTSKKVIELF YDVVSPYSWL GFEIMCRYRN VWNIELKLRP AFLGGIMQGS GNKPPGLVPN
     KFMYMTKDLN RLAQYFDVPL QPPSDPFEAM FKKGTCSLSA MRFVAAVQER EKGGDKQVEQ
     VSRELWRRIW SEDKDITEPA SLSEAAKKAG LSDGEIKEVL QMSTSKEIKD KLKSTTQDAL
     DIGAFGFPLV VCHVDGKPEM FFGSDRFELM AHCIGEKWLG PQPGKSAAKL
//
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