GST1_ASCSU
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 03-AUG-2022, entry version 84.
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}.
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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 AlphaFoldDB; P46436; -.
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 EnsemblMetazoa; AgR005_g358_t01; AgR005_g358_t01; AgR005_g358.
DR EnsemblMetazoa; AgR005_g358_t03; AgR005_g358_t03; AgR005_g358.
DR EnsemblMetazoa; AgR005_g358_t04; AgR005_g358_t04; AgR005_g358.
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:0006749; P:glutathione metabolic process; IEA:InterPro.
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 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 49..51
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O60760"
FT BINDING 63..64
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O60760"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:4Q5F"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:4Q5F"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:4Q5F"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:4Q5F"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:4Q5F"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:4Q5F"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:4Q5F"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:4Q5F"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:4Q5F"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:4Q5F"
FT HELIX 64..74
FT /evidence="ECO:0007829|PDB:4Q5F"
FT HELIX 82..102
FT /evidence="ECO:0007829|PDB:4Q5F"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:4Q5F"
FT HELIX 106..110
FT /evidence="ECO:0007829|PDB:4Q5F"
FT HELIX 117..123
FT /evidence="ECO:0007829|PDB:4Q5F"
FT HELIX 125..143
FT /evidence="ECO:0007829|PDB:4Q5F"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:4Q5F"
FT HELIX 155..170
FT /evidence="ECO:0007829|PDB:4Q5F"
FT TURN 172..177
FT /evidence="ECO:0007829|PDB:4Q5F"
FT HELIX 179..190
FT /evidence="ECO:0007829|PDB:4Q5F"
FT HELIX 192..200
FT /evidence="ECO:0007829|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
