ID GST1_ASCSU Reviewed; 206 AA. AC P46436; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 08-FEB-2011, entry version 44. DE RecName: Full=Glutathione S-transferase 1; DE EC=2.5.1.18; DE AltName: Full=GST class-sigma; GN Name=GST1; OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides). OC Eukaryota; Metazoa; Nematoda; Chromadorea; Ascaridida; Ascaridoidea; OC Ascarididae; Ascaris. OX NCBI_TaxID=6253; RN [1] RP NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 2-41. RX MEDLINE=94239466; PubMed=8183318; DOI=10.1016/0166-6851(94)90021-3; RA Liebau E., Schoenberger O.L., Walter R.D., Henkle-Duehrsen K.J.; RT "Molecular cloning and expression of a cDNA encoding glutathione S- RT transferase from Ascaris suum."; RL Mol. Biochem. Parasitol. 63:167-170(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=97307883; PubMed=9182731; RA Liebau E., Eckelt V.H., Wildenburg G., Teesdale-Spittle P., RA Brophy P.M., Walter R.D., Henkle-Duehrsen K.; RT "Structural and functional analysis of a glutathione S-transferase RT from Ascaris suum."; RL Biochem. J. 324:659-666(1997). CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of CC exogenous and endogenous hydrophobic electrophiles. Can also CC function as a GSH peroxidase. 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 https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X75502; CAA53218.1; -; mRNA. DR EMBL; Y10613; CAA71620.1; -; Genomic_DNA. DR PIR; S38626; S38626. DR ProteinModelPortal; P46436; -. DR SMR; P46436; 1-206. DR BRENDA; 2.5.1.18; 649. DR GO; GO:0004364; F:glutathione transferase activity; NAS:UniProtKB. 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; IPR012336; Thioredoxin-like_fold. 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 SUPFAM; SSF47616; GST_C_like; 1. DR SUPFAM; SSF52833; Thiordxn-like_fd; 1. DR PROSITE; PS50405; GST_CTER; 1. DR PROSITE; PS50404; GST_NTER; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Transferase. FT INIT_MET 1 1 Removed. FT CHAIN 2 206 Glutathione S-transferase 1. FT /FTId=PRO_0000185922. FT DOMAIN 2 79 GST N-terminal. FT DOMAIN 81 206 GST C-terminal. FT REGION 50 51 Glutathione binding (By similarity). FT REGION 63 64 Glutathione binding (By similarity). FT BINDING 8 8 Glutathione (By similarity). FT BINDING 39 39 Glutathione (By similarity). FT BINDING 43 43 Glutathione (By similarity). SQ SEQUENCE 206 AA; 23585 MW; B8366238A63DF399 CRC64; MPQYKLTYFD IRGLGEGARL IFHQAGVKFE DNRLKREDWP ALKPKTPFGQ LPLLEVDGEV LAQSAAIYRY LGRQFGLAGK TPMEEAQVDS IFDQFKDFMA ELRPCFRVLA GFEEGDKEKV LKEVAVPARD KHLPLLEKFL AKSGSEYMVG KSVTWADLVI TDSLASWESL IPDFLSGHLQ LKKYIEHVRE LPNIKKWIAE RPKTPY //