Top Level Name

  ⌊ Superfamily (core) Glutathione Transferase (cytosolic)

    ⌊ Subgroup AMPS (cytGST): Alpha-, Mu-, Pi-, and Sigma-like

  ⌊ AMPS.1

  ⌊ FunctionalDomain similar to Alpha, Mu, Pi, and Sigma class cytGSTs (ID 55750)

Superfamily Assignment Evidence Code(s) ISS
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Rattus norvegicus Taxon ID: 10116 8393502 NP_058710.1 (RefSeq) PRP URP
Rattus norvegicus Taxon ID: 10116 38648907 AAH63172.1 (Genbank) PRP URP
n/a 594517 AAA56124.1 (Genbank)
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Uniprot

Protein NameAccessionEC Number Identifier
Glutathione S-transferase Mu 1 P04905 2.5.1.18 GSTM1_RAT (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 218 | Length of Functional Domain: 210

1       10        20        30        40        50        60

MPMILGYWNVRGLTHPIRLLLEYTDSSYEEKRYAMGDAPDYDRSQWLNEKFKLGLDFPNL
PYLIDGSRKITQSNAIMRYLARKHHLCGETEEERIRADIVENQVMDNRMQLIMLCYNPDF
EKQKPEFLKTIPEKMKLYSEFLGKRPWFAGDKVTYVDFLAYDILDQYHIFEPKCLDAFPN
LKDFLARFEGLKKISAYMKSSRYLSTPIFSKLAQWSNK
This shows the full-length sequence of the enzyme. The region of the functional domain is highlighted in black letters, while the residual residues are shown in grey. The Superfamily domain, when present, is shown using underlining. In many cases the functional domain is the full-length sequence.
Conserved catalytic residues (as determined by automated alignment to family, subgroup, or superfamily HMMs) are shown with teal highlighting . Conserved catalytic residues which do not matched the Conserved Alignment Residue are shown with maroon highlighting . Information regarding their function can be found in the Conserved Residues section below.
FASTA formatted full-length sequence.
BLAST this sequence against SFLD.
Scan SFLD-HMMs with this sequence.

Conserved Residues

Subgroup CAR This EFD conserves 1/1 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
7 Tyr (Y) side chain None -- ISS PubMed:9074797

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
5GST Reaction Coordinate Motion In An Snar Reaction Catalyzed By Glutathione Transferase Glutathione S-Transferase 12 2.0 Sulfate Ion • Glutathione S-(2,4 Dinitrobenzene) CSA • PDB • PDBSum
3GST Structure Of The Xenobiotic Substrate Binding Site Of A Glutathione S-Transferase As Revealed By X-Ray Crystallographic Analysis Of Product Complexes With The Diastereomers Of 9-(S-Glutathionyl)-10-Hydroxy-9, 10-Dihydrophenanthrene Glutathione S-Transferase 12 1.9 Sulfate Ion • (9R,10R)-9-(S-Glutathionyl)-10-Hydroxy-9,10-Dihydrophenanthrene CSA • PDB • PDBSum
6GST First-Sphere And Second-Sphere Electrostatic Effects In The Active Site Of A Class Mu Glutathione Transferase Mu Class Glutathione S-Transferase Of Isoenzyme 3-3 12 2.2 Glutathione CSA • PDB • PDBSum
1GSC New Crystal Forms Of A Mu Class Glutathione S-Transferase From Rat Liver Glutathione S-Transferase 12 2.5 CSA • PDB • PDBSum
1GSB New Crystal Forms Of A Mu Class Glutathione S-Transferase From Rat Liver Glutathione S-Transferase 12 2.5 CSA • PDB • PDBSum
2GST Structure Of The Xenobiotic Substrate Binding Site Of A Glutathione S-Transferase As Revealed By X-Ray Crystallographic Analysis Of Product Complexes With The Diastereomers Of 9-(S-Glutathionyl)-10-Hydroxy-9, 10-Dihydrophenanthrene Glutathione S-Transferase 12 1.8 Sulfate Ion • L-Gamma-Glutamyl-S-[(9S,10S)-10-Hydroxy-9,10-Dihydrophenanthren-9-Yl]-L-Cysteinylglycine CSA • PDB • PDBSum
4GST Reaction Coordinate Motion In An Snar Reaction Catalyzed By Glutathione Transferase Glutathione S-Transferase 12 1.9 Sulfate Ion • 1-(S-Glutathionyl)-2,4,6-Trinitrocyclohexa-2,5-Diene CSA • PDB • PDBSum
6GSV First-Sphere And Second-Sphere Electrostatic Effects In The Active Site Of A Class Mu Glutathione Transferase Mu Class Glutathione S-Transferase Of Isoenzyme 3-3 12 1.75 Yes Sulfate Ion • L-Gamma-Glutamyl-S-[(9S,10S)-10-Hydroxy-9,10-Dihydrophenanthren-9-Yl]-L-Cysteinylglycine CSA • PDB • PDBSum
6GSX First-Sphere And Second-Sphere Electrostatic Effects In The Active Site Of A Class Mu Glutathione Transferase Mu Class Glutathione S-Transferase Of Isoenzyme 3-3 12 1.91 Yes Sulfate Ion • L-Gamma-Glutamyl-S-[(9S,10S)-10-Hydroxy-9,10-Dihydrophenanthren-9-Yl]-L-Cysteinylglycine CSA • PDB • PDBSum
6GSY First-Sphere And Second-Sphere Electrostatic Effects In The Active Site Of A Class Mu Glutathione Transferase Mu Class Glutathione S-Transferase Of Isoenzyme 3-3 12 2.2 Yes Glutathione CSA • PDB • PDBSum
1MTC Glutathione Transferase Mutant Y115F Glutathione S-Transferase Yb1 12 2.2 Yes (9R,10R)-9-(S-Glutathionyl)-10-Hydroxy-9,10-Dihydrophenanthrene CSA • PDB • PDBSum
6GSW First-Sphere And Second-Sphere Electrostatic Effects In The Active Site Of A Class Mu Glutathione Transferase Mu Class Glutathione S-Transferase Of Isoenzyme 3-3 12 1.85 Yes Sulfate Ion • L-Gamma-Glutamyl-S-[(9S,10S)-10-Hydroxy-9,10-Dihydrophenanthren-9-Yl]-L-Cysteinylglycine CSA • PDB • PDBSum
6GSU First-Sphere And Second-Sphere Electrostatic Effects In The Active Site Of A Class Mu Glutathione Transferase Mu Class Glutathione S-Transferase Of Isoenzyme 3-3 12 1.85 Yes Sulfate Ion • L-Gamma-Glutamyl-S-[(9S,10S)-10-Hydroxy-9,10-Dihydrophenanthren-9-Yl]-L-Cysteinylglycine CSA • PDB • PDBSum
5FWG Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase Tetra-(5-Fluorotryptophanyl)-Glutathionetransferase Mu Class 12 2.0 Yes Fluorotryptophane • (9R,10R)-9-(S-Glutathionyl)-10-Hydroxy-9,10-Dihydrophenanthrene CSA • PDB • PDBSum
Percent identity and alignment length from the BLAST match of the Functional Domain sequence to the PDB sequence.
"Yes" indicates that a GI associated with this Functional Domain was mapped to the PDB ID via UniProtKB.

Curation History
Time Change Annotation Old Value New Value
May 3, 2014, 6:39 a.m. update curation agent smashiya setDomainBoundaries.py
update domain end position 218 200
update domain start position 1 2
Aug. 16, 2016, 8:33 a.m. update domain end position 200 210
update domain start position 2 1
EC number assigned by UniProtKB accession ID.