ID A0A087XRL7_POEFO Unreviewed; 155 AA.
AC A0A087XRL7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Microsomal glutathione S-transferase 1 {ECO:0000256|ARBA:ARBA00039397};
DE EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000008420.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000008420.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles.
CC {ECO:0000256|ARBA:ARBA00003701}.
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 Evidence={ECO:0000256|ARBA:ARBA00035754};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
CC Evidence={ECO:0000256|ARBA:ARBA00035754};
CC -!- SUBUNIT: Homotrimer; The trimer binds only one molecule of glutathione.
CC {ECO:0000256|ARBA:ARBA00038540}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004294}.
CC -!- SIMILARITY: Belongs to the MAPEG family.
CC {ECO:0000256|ARBA:ARBA00010459}.
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DR EMBL; AYCK01005173; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A087XRL7; -.
DR STRING; 48698.ENSPFOP00000008420; -.
DR Ensembl; ENSPFOT00000008432.1; ENSPFOP00000008420.1; ENSPFOG00000008473.1.
DR eggNOG; ENOG502S0BD; Eukaryota.
DR GeneTree; ENSGT00390000011980; -.
DR OMA; TFSMAYN; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.20.120.550; Membrane associated eicosanoid/glutathione metabolism-like domain; 1.
DR InterPro; IPR023352; MAPEG-like_dom_sf.
DR InterPro; IPR001129; Membr-assoc_MAPEG.
DR InterPro; IPR040162; MGST1-like.
DR PANTHER; PTHR10689; MICROSOMAL GLUTATHIONE S-TRANSFERASE 1; 1.
DR PANTHER; PTHR10689:SF3; MICROSOMAL GLUTATHIONE S-TRANSFERASE 1; 1.
DR Pfam; PF01124; MAPEG; 1.
DR SUPFAM; SSF161084; MAPEG domain-like; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 80..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 155 AA; 17728 MW; 64CC208D1EFF3CB2 CRC64;
SVEMATLMEN EVFKAFASYA AIVTLKMMLM GPVTVYFRFT RGSFSNEEDV AKETNEEKKK
KMLRAHPDVE RAQRCHHNDL ENIIPFFFIG LLYALSGPKL SIALIHFRVF TASRIFHSFA
YILAFPQPSR ALSYLLGMLT TFSMAFNLLI TVFVL
//
