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 05-MAY-2009, entry version 70. 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; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z46828; CAA86859.1; -; Genomic_DNA. DR PIR; T23872; T23872. DR RefSeq; NP_496357.1; -. DR UniGene; Cel.14876; -. DR PDB; 1ZL9; X-ray; 2.01 A; A/B=1-207. DR PDBsum; 1ZL9; -. DR DIP; DIP:26899N; -. DR IntAct; Q09596; 30. DR Ensembl; R03D7.6; Caenorhabditis elegans. DR GeneID; 187537; -. DR KEGG; cel:R03D7.6; -. DR NMPDR; fig|6239.3.peg.7351; -. DR WormBase; WBGene00001753; gst-5. DR WormPep; R03D7.6; CE01613. DR OMA; Q09596; KDYSSEA. DR BRENDA; 2.5.1.18; 672. DR NextBio; 935622; -. DR ArrayExpress; Q09596; -. DR GO; GO:0004364; F:glutathione transferase activity; IEA:EC. DR InterPro; IPR010987; Glutathione-S-Trfase_C-like. 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:1.20.1050.10; GST_C_like; 1. 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 1: Evidence at protein level; KW 3D-structure; Complete proteome; Transferase. FT CHAIN 1 207 Probable glutathione S-transferase 5. FT /FTId=PRO_0000185928. FT DOMAIN 2 81 GST N-terminal. FT DOMAIN 83 207 GST C-terminal. FT STRAND 4 12 FT HELIX 13 15 FT HELIX 16 25 FT STRAND 30 34 FT TURN 36 38 FT HELIX 39 44 FT STRAND 55 58 FT STRAND 61 64 FT HELIX 66 76 FT HELIX 84 111 FT HELIX 119 125 FT HELIX 127 145 FT STRAND 147 151 FT HELIX 157 171 FT HELIX 180 191 FT HELIX 193 201 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 //