GST_PROMI
ID GST_PROMI Reviewed; 203 AA.
AC P15214;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Glutathione S-transferase GST-6.0;
DE EC=2.5.1.18;
DE AltName: Full=GST B1-1;
GN Name=gstB;
OS Proteus mirabilis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=584;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AF 2924;
RX PubMed=8761466; DOI=10.1042/bj3180157;
RA Perito B., Allocati N., Casalone E., Masulli M., Dragani B., Polsinelli M.,
RA Aceto A., Di Ilio C.;
RT "Molecular cloning and overexpression of a glutathione transferase gene
RT from Proteus mirabilis.";
RL Biochem. J. 318:157-162(1996).
RN [2]
RP PROTEIN SEQUENCE.
RC STRAIN=AF 2924;
RX PubMed=8436105; DOI=10.1111/j.1432-1033.1993.tb17566.x;
RA Mignogna G., Allocati N., Aceto A., Piccolomini R., Di Ilio C., Barra D.,
RA Martini F.;
RT "The amino acid sequence of glutathione transferase from Proteus mirabilis,
RT a prototype of a new class of enzymes.";
RL Eur. J. Biochem. 211:421-425(1993).
RN [3]
RP PROTEIN SEQUENCE OF 1-38.
RC STRAIN=AF 2924;
RX PubMed=2661269; DOI=10.1016/0014-5793(89)80684-2;
RA Di Ilio C., Aceto A., Piccolomini R., Allocati N., Caccuri A.M., Barra D.,
RA Feferici G.;
RT "N-terminal region of Proteus mirabilis glutathione transferase is not
RT homologous to mammalian and plant glutathione transferases.";
RL FEBS Lett. 250:57-59(1989).
RN [4]
RP PROTEIN SEQUENCE OF 1-5 AND 36-42.
RX PubMed=8645008; DOI=10.1006/abbi.1996.0177;
RA Aceto A., Dragani B., Allocati N., Masulli M., Petruzzelli R., Di Ilio C.;
RT "Purification and characterization of a heterodimeric 23/20-kDa proteolytic
RT fragment of bacterial glutathione transferase B1-1.";
RL Arch. Biochem. Biophys. 328:302-308(1996).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.
RX PubMed=9655824; DOI=10.1016/s0969-2126(98)00074-4;
RA Rossjohn J., Polekhina G., Feil S.C., Allocati N., Masulli M., Di Ilio C.,
RA Parker M.W.;
RT "A mixed disulfide bond in bacterial glutathione transferase: functional
RT and evolutionary implications.";
RL Structure 6:721-734(1998).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles.
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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9655824}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the GST superfamily. Beta family. {ECO:0000305}.
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DR EMBL; U38482; AAC44362.1; -; Genomic_DNA.
DR PIR; S71882; S71882.
DR RefSeq; WP_004248152.1; NZ_WEKK01000004.1.
DR PDB; 1PMT; X-ray; 2.50 A; A=1-203.
DR PDB; 2PMT; X-ray; 2.70 A; A/B/C/D=1-203.
DR PDBsum; 1PMT; -.
DR PDBsum; 2PMT; -.
DR AlphaFoldDB; P15214; -.
DR SMR; P15214; -.
DR STRING; 584.AOUC001_08665; -.
DR GeneID; 6801758; -.
DR PATRIC; fig|584.120.peg.1817; -.
DR OMA; YVATELH; -.
DR EvolutionaryTrace; P15214; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
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; PF00043; GST_C; 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; Cytoplasm; Direct protein sequencing; Transferase.
FT CHAIN 1..203
FT /note="Glutathione S-transferase GST-6.0"
FT /id="PRO_0000185974"
FT DOMAIN 1..81
FT /note="GST N-terminal"
FT DOMAIN 87..203
FT /note="GST C-terminal"
FT BINDING 10
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:9655824"
FT BINDING 35
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:9655824"
FT BINDING 52
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:9655824"
FT BINDING 65..66
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:9655824"
FT BINDING 99
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:9655824"
FT BINDING 103..107
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:9655824"
FT CONFLICT 20
FT /note="E -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 34..36
FT /note="TKK -> RLL (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:1PMT"
FT HELIX 12..20
FT /evidence="ECO:0007829|PDB:1PMT"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:1PMT"
FT TURN 32..35
FT /evidence="ECO:0007829|PDB:1PMT"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1PMT"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:1PMT"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:1PMT"
FT HELIX 66..74
FT /evidence="ECO:0007829|PDB:1PMT"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:1PMT"
FT HELIX 89..103
FT /evidence="ECO:0007829|PDB:1PMT"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:1PMT"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:1PMT"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:1PMT"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:1PMT"
FT HELIX 122..140
FT /evidence="ECO:0007829|PDB:1PMT"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:1PMT"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:1PMT"
FT HELIX 153..162
FT /evidence="ECO:0007829|PDB:1PMT"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:1PMT"
FT HELIX 176..186
FT /evidence="ECO:0007829|PDB:1PMT"
FT HELIX 189..197
FT /evidence="ECO:0007829|PDB:1PMT"
SQ SEQUENCE 203 AA; 22852 MW; 2021F194D5CF105E CRC64;
MKLYYTPGSC SLSPHIVLRE TGLDFSIERI DLRTKKTESG KDFLAINPKG QVPVLQLDNG
DILTEGVAIV QYLADLKPDR NLIAPPKALE RYHQIEWLNF LASEVHKGYS PLFSSDTPES
YLPVVKNKLK SKFVYINDVL SKQKCVCGDH FTVADAYLFT LSQWAPHVAL DLTDLSHLQD
YLARIAQRPN VHSALVTEGL IKE
