ID A0A2K6KF71_RHIBE Unreviewed; 226 AA.
AC A0A2K6KF71;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Glutathione S-transferase kappa {ECO:0000256|PIRNR:PIRNR006386};
DE EC=2.5.1.18 {ECO:0000256|PIRNR:PIRNR006386};
GN Name=GSTK1 {ECO:0000313|Ensembl:ENSRBIP00000009917.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000009917.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000009917.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000009917.1}
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 RefSeq; XP_017750779.1; XM_017895290.1.
DR AlphaFoldDB; A0A2K6KF71; -.
DR STRING; 61621.ENSRBIP00000009917; -.
DR Ensembl; ENSRBIT00000033539.1; ENSRBIP00000009917.1; ENSRBIG00000028820.1.
DR GeneID; 108544238; -.
DR CTD; 373156; -.
DR GeneTree; ENSGT00440000033697; -.
DR OMA; ECTNSKG; -.
DR OrthoDB; 4159077at2759; -.
DR Proteomes; UP000233180; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005777; C:peroxisome; IEA:Ensembl.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:Ensembl.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:Ensembl.
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 Reference proteome {ECO:0000313|Proteomes:UP000233180};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006386}.
FT DOMAIN 7..210
FT /note="DSBA-like thioredoxin"
FT /evidence="ECO:0000259|Pfam:PF01323"
FT ACT_SITE 16
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006386-1"
SQ SEQUENCE 226 AA; 25527 MW; E1B200DADCAC0F1D CRC64;
MGPLLRTVEL FYDVLSPYSW LGFEVLCRYQ NIWNINLQLR PSLIGGIMKD SGNKPPALLP
RKGQYMANDI KLLRHHFQIP IQFPKDFFSV IIEKGSLSAM RFLTAVSLEH PDMLEKVSRE
LWMRIWSKDE DITEPQSILA AAEKAGMSAE QAQGLLEKIS TPKVKNQLKE TTEAACRYGA
FGLPITVAHV DGQTHMIFGS DRMELLAYLL GEKWMGPVPP AVNARL
//
