GST5_CAEEL
ID GST5_CAEEL Reviewed; 207 AA.
AC Q09596;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Probable glutathione S-transferase 5;
DE EC=2.5.1.18;
DE AltName: Full=GST class-sigma;
GN Name=gst-5; ORFNames=R03D7.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION.
RX PubMed=22216003; DOI=10.1371/journal.ppat.1002453;
RA Hoeven R.V., McCallum K.C., Cruz M.R., Garsin D.A.;
RT "Ce-Duox1/BLI-3 generated reactive oxygen species trigger protective SKN-1
RT activity via p38 MAPK signaling during infection in C. elegans.";
RL PLoS Pathog. 7:E1002453-E1002453(2011).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles (By similarity). May
CC play a role in the detoxification of reactive oxygen species produced
CC during pathogenic bacterial infection (PubMed:22216003).
CC {ECO:0000250|UniProtKB:P46436, ECO:0000269|PubMed:22216003}.
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 -!- SIMILARITY: Belongs to the GST superfamily. Sigma family.
CC {ECO:0000305}.
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DR EMBL; Z46828; CAA86859.1; -; Genomic_DNA.
DR PIR; T23872; T23872.
DR RefSeq; NP_001254267.1; NM_001267338.1.
DR PDB; 1ZL9; X-ray; 2.01 A; A/B=1-207.
DR PDBsum; 1ZL9; -.
DR AlphaFoldDB; Q09596; -.
DR SMR; Q09596; -.
DR BioGRID; 52227; 43.
DR DIP; DIP-26899N; -.
DR IntAct; Q09596; 26.
DR STRING; 6239.R03D7.6a; -.
DR EPD; Q09596; -.
DR PaxDb; Q09596; -.
DR PeptideAtlas; Q09596; -.
DR EnsemblMetazoa; R03D7.6a.1; R03D7.6a.1; WBGene00001753.
DR GeneID; 187537; -.
DR KEGG; cel:CELE_R03D7.6; -.
DR UCSC; R03D7.6; c. elegans.
DR CTD; 187537; -.
DR WormBase; R03D7.6a; CE01613; WBGene00001753; gst-5.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00970000196005; -.
DR HOGENOM; CLU_039475_1_1_1; -.
DR InParanoid; Q09596; -.
DR OMA; PWDLIFF; -.
DR OrthoDB; 1162336at2759; -.
DR PhylomeDB; Q09596; -.
DR Reactome; R-CEL-156590; Glutathione conjugation.
DR Reactome; R-CEL-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR SignaLink; Q09596; -.
DR EvolutionaryTrace; Q09596; -.
DR PRO; PR:Q09596; -.
DR Proteomes; UP000001940; Chromosome II.
DR ExpressionAtlas; Q09596; baseline and differential.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; HEP:WormBase.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Transferase.
FT CHAIN 1..207
FT /note="Probable glutathione S-transferase 5"
FT /id="PRO_0000185928"
FT DOMAIN 2..81
FT /note="GST N-terminal"
FT DOMAIN 83..207
FT /note="GST C-terminal"
FT BINDING 8
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O60760"
FT BINDING 39
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O60760"
FT BINDING 43
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P46088"
FT BINDING 51..53
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O60760"
FT BINDING 65..66
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O60760"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:1ZL9"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1ZL9"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:1ZL9"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:1ZL9"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:1ZL9"
FT HELIX 39..44
FT /evidence="ECO:0007829|PDB:1ZL9"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:1ZL9"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:1ZL9"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:1ZL9"
FT HELIX 84..111
FT /evidence="ECO:0007829|PDB:1ZL9"
FT HELIX 119..125
FT /evidence="ECO:0007829|PDB:1ZL9"
FT HELIX 127..145
FT /evidence="ECO:0007829|PDB:1ZL9"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:1ZL9"
FT HELIX 157..171
FT /evidence="ECO:0007829|PDB:1ZL9"
FT HELIX 180..191
FT /evidence="ECO:0007829|PDB:1ZL9"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:1ZL9"
SQ SEQUENCE 207 AA; 23252 MW; 7FDE101B24F7468B CRC64;
MVSYKLTYFN GRGAGEVSRQ IFAYAGQQYE DNRVTQEQWP ALKETCAAPF GQLPFLEVDG
KKLAQSHAIA RFLAREFKLN GKTAWEEAQV NSLADQYKDY SSEARPYFYA VMGFGPGDVE
TLKKDIFLPA FEKFYGFLVN FLKASGSGFL VGDSLTWIDL AIAQHSADLI AKGGDFSKFP
ELKAHAEKIQ AIPQIKKWIE TRPVTPF
