GST_BRUAN
ID GST_BRUAN Reviewed; 201 AA.
AC P81065;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Glutathione S-transferase;
DE EC=2.5.1.18;
GN Name=gst;
OS Brucella anthropi (Ochrobactrum anthropi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=529;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25 AND 50-74, AND
RP MUTAGENESIS.
RX PubMed=9794797; DOI=10.1042/bj3350573;
RA Favaloro B., Tamburro A., Angelucci S., de Luca A., di Ilio C., Rotilio D.;
RT "Molecular cloning, expression and site-directed mutagenesis of glutathione
RT S-transferase from Ochrobactrum anthropi.";
RL Biochem. J. 335:573-579(1998).
RN [2]
RP PROTEIN SEQUENCE OF 1-25.
RX PubMed=9495016; DOI=10.1111/j.1574-6968.1998.tb12894.x;
RA Favaloro B., Melino S., Petruzzelli R., di Ilio C., Rotilio D.;
RT "Purification and characterization of a novel glutathione transferase from
RT Ochrobactrum anthropi.";
RL FEMS Microbiol. Lett. 160:81-86(1998).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE,
RP CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-10, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=18076047; DOI=10.1002/prot.21835;
RA Allocati N., Federici L., Masulli M., Favaloro B., Di Ilio C.;
RT "Cysteine 10 is critical for the activity of Ochrobactrum anthropi
RT glutathione transferase and its mutation to alanine causes the preferential
RT binding of glutathione to the H-site.";
RL Proteins 71:16-23(2008).
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 Evidence={ECO:0000269|PubMed:18076047};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.132 mM for glutathione {ECO:0000269|PubMed:18076047};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Beta family. {ECO:0000305}.
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DR EMBL; Y17279; CAA76728.1; -; Genomic_DNA.
DR RefSeq; WP_010659377.1; NZ_WBXA01000003.1.
DR PDB; 2NTO; X-ray; 2.10 A; A=1-201.
DR PDB; 2PVQ; X-ray; 1.80 A; A=1-201.
DR PDBsum; 2NTO; -.
DR PDBsum; 2PVQ; -.
DR AlphaFoldDB; P81065; -.
DR SMR; P81065; -.
DR GeneID; 61318189; -.
DR BRENDA; 2.5.1.18; 4382.
DR SABIO-RK; P81065; -.
DR EvolutionaryTrace; P81065; -.
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; IPR040079; Glutathione_S-Trfase.
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 SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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..201
FT /note="Glutathione S-transferase"
FT /id="PRO_0000185973"
FT DOMAIN 1..81
FT /note="GST N-terminal"
FT DOMAIN 87..201
FT /note="GST C-terminal"
FT BINDING 10
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:18076047"
FT BINDING 35
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:18076047"
FT BINDING 52
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:18076047"
FT BINDING 65..66
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:18076047"
FT BINDING 102..105
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:18076047"
FT MUTAGEN 10
FT /note="C->A: Strongly reduced affinity for glutathione.
FT Reduces enzyme activity by about 50%."
FT /evidence="ECO:0000269|PubMed:18076047"
FT MUTAGEN 11
FT /note="S->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:9794797"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:2PVQ"
FT HELIX 12..21
FT /evidence="ECO:0007829|PDB:2PVQ"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:2PVQ"
FT TURN 32..35
FT /evidence="ECO:0007829|PDB:2PVQ"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:2PVQ"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:2PVQ"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:2PVQ"
FT HELIX 66..75
FT /evidence="ECO:0007829|PDB:2PVQ"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:2PVQ"
FT HELIX 89..109
FT /evidence="ECO:0007829|PDB:2PVQ"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:2PVQ"
FT HELIX 118..138
FT /evidence="ECO:0007829|PDB:2PVQ"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:2PVQ"
FT HELIX 153..167
FT /evidence="ECO:0007829|PDB:2PVQ"
FT HELIX 176..186
FT /evidence="ECO:0007829|PDB:2PVQ"
FT HELIX 189..197
FT /evidence="ECO:0007829|PDB:2PVQ"
SQ SEQUENCE 201 AA; 21739 MW; 763B2D3DECA21F2D CRC64;
MKLYYKVGAC SLAPHIILSE AGLPYELEAV DLKAKKTADG GDYFAVNPRG AVPALEVKPG
TVITQNAAIL QYIGDHSDVA AFKPAYGSIE RARLQEALGF CSDLHAAFSG LFAPNLSEEA
RAGVIANINR RLGQLEAMLS DKNAYWLGDD FTQPDAYASV IIGWGVGQKL DLSAYPKALK
LRERVLARPN VQKAFKEEGL N
