ID   GST3_CAEEL              Reviewed;         207 AA.
AC   O16116; Q21357;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 58.
DE   RecName: Full=Glutathione S-transferase 3;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-sigma;
DE   AltName: Full=CeGST3;
GN   Name=gst-3; ORFNames=K08F4.11;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Bristol N2;
RA   Tawe W.N., Eschbach M.-L., Walter R.D., Henkle-Duehrsen K.;
RT   "Paraquat mediates differential gene expression in C. elegans.";
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; 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
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Sigma family.
CC   -!- SIMILARITY: Contains 1 GST C-terminal domain.
CC   -!- SIMILARITY: Contains 1 GST N-terminal domain.
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DR   EMBL; AF010241; AAB65419.1; -; mRNA.
DR   EMBL; Z68879; CAA93088.2; -; Genomic_DNA.
DR   PIR; T23485; T23485.
DR   PIR; T37464; T37464.
DR   RefSeq; NP_501846.1; -.
DR   UniGene; Cel.19689; -.
DR   UniGene; Cel.35663; -.
DR   HSSP; P24472; 1GUK.
DR   Ensembl; K08F4.11; Caenorhabditis elegans.
DR   GeneID; 177883; -.
DR   KEGG; cel:K08F4.11; -.
DR   WormBase; WBGene00001751; gst-3.
DR   WormPep; K08F4.11; CE25050.
DR   OMA; O16116; DTFKDFI.
DR   BRENDA; 2.5.1.18; 672.
DR   NextBio; 898788; -.
DR   ArrayExpress; O16116; -.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:EC.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR017933; Glutathione_S_Trfase/Cl_chnl_C.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Transferase.
FT   CHAIN         1    207       Glutathione S-transferase 3.
FT                                /FTId=PRO_0000185926.
FT   DOMAIN        2     79       GST N-terminal.
FT   DOMAIN       81    207       GST C-terminal.
SQ   SEQUENCE   207 AA;  23735 MW;  72545319FCFCEDBA CRC64;
     MVHYKLTYFN ARGLAEISRQ LFHMAGVEFE DERINEEKFS QLKPTFPSGQ VPILCIDGAQ
     FSQSTAIARY LARKFGFVGQ TAEEELQADE VVDTFKDFIE SFRKFVIAVL SGESEEILKN
     IREEVIKPAV KTYTAYLKAI LEKSSSGYLV GNELTWADLV IADNLTTLIN AELLDIENDK
     LLKEFREKII ETPKLKEWLA KRPETRF
//