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 07-OCT-2020, entry version 78. 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; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris. OX NCBI_TaxID=6253; RN [1] RP NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 2-41. RX 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 PubMed=9182731; DOI=10.1042/bj3240659; RA Liebau E., Eckelt V.H., Wildenburg G., Teesdale-Spittle P., Brophy P.M., RA Walter R.D., Henkle-Duehrsen K.; RT "Structural and functional analysis of a glutathione S-transferase from RT 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 function CC as a GSH peroxidase. 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}. 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 PDB; 4Q5F; X-ray; 2.45 A; A/D=1-206. DR PDBsum; 4Q5F; -. DR SMR; P46436; -. DR Allergome; 10991; Asc l 13. DR Allergome; 10992; Asc l 13.0101. DR Allergome; 11669; Asc s 13.0101. DR Allergome; 7680; Asc s 13. DR BRENDA; 2.5.1.18; 474. DR GO; GO:0005903; C:brush border; IDA:WormBase. DR GO; GO:0005737; C:cytoplasm; IDA:WormBase. DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:WormBase. DR GO; GO:0004364; F:glutathione transferase activity; IDA:WormBase. DR GO; GO:0098869; P:cellular oxidant detoxification; IDA:UniProtKB. DR GO; GO:0055114; P:oxidation-reduction process; IDA:WormBase. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR010987; Glutathione-S-Trfase_C-like. DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf. 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 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; Direct protein sequencing; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:8183318" FT CHAIN 2..206 FT /note="Glutathione S-transferase 1" FT /id="PRO_0000185922" FT DOMAIN 2..79 FT /note="GST N-terminal" FT DOMAIN 81..206 FT /note="GST C-terminal" FT REGION 49..51 FT /note="Glutathione binding" FT /evidence="ECO:0000250|UniProtKB:O60760" FT REGION 63..64 FT /note="Glutathione binding" FT /evidence="ECO:0000250|UniProtKB:O60760" FT BINDING 8 FT /note="Glutathione" FT /evidence="ECO:0000250|UniProtKB:O60760" FT BINDING 39 FT /note="Glutathione" FT /evidence="ECO:0000250|UniProtKB:O60760" FT BINDING 43 FT /note="Glutathione" FT /evidence="ECO:0000250|UniProtKB:P46088" FT STRAND 4..11 FT /evidence="ECO:0000244|PDB:4Q5F" FT TURN 13..15 FT /evidence="ECO:0000244|PDB:4Q5F" FT HELIX 16..24 FT /evidence="ECO:0000244|PDB:4Q5F" FT STRAND 30..34 FT /evidence="ECO:0000244|PDB:4Q5F" FT HELIX 36..38 FT /evidence="ECO:0000244|PDB:4Q5F" FT HELIX 39..42 FT /evidence="ECO:0000244|PDB:4Q5F" FT HELIX 43..45 FT /evidence="ECO:0000244|PDB:4Q5F" FT STRAND 46..49 FT /evidence="ECO:0000244|PDB:4Q5F" FT STRAND 53..56 FT /evidence="ECO:0000244|PDB:4Q5F" FT STRAND 59..62 FT /evidence="ECO:0000244|PDB:4Q5F" FT HELIX 64..74 FT /evidence="ECO:0000244|PDB:4Q5F" FT HELIX 82..102 FT /evidence="ECO:0000244|PDB:4Q5F" FT HELIX 103..105 FT /evidence="ECO:0000244|PDB:4Q5F" FT HELIX 106..110 FT /evidence="ECO:0000244|PDB:4Q5F" FT HELIX 117..123 FT /evidence="ECO:0000244|PDB:4Q5F" FT HELIX 125..143 FT /evidence="ECO:0000244|PDB:4Q5F" FT STRAND 145..152 FT /evidence="ECO:0000244|PDB:4Q5F" FT HELIX 155..170 FT /evidence="ECO:0000244|PDB:4Q5F" FT TURN 172..177 FT /evidence="ECO:0000244|PDB:4Q5F" FT HELIX 179..190 FT /evidence="ECO:0000244|PDB:4Q5F" FT HELIX 192..200 FT /evidence="ECO:0000244|PDB:4Q5F" 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 //