Top Level Name

  ⌊ Superfamily (core) Glutathione Transferase (cytosolic)

    ⌊ Subgroup Main (cytGST)

  Main.3: Omega- and Tau-like

  ⌊ FunctionalDomain Cytosolic GST-like protein, similar to Omega and Tau class GSTs (ID 225655)

Superfamily Assignment Evidence Code(s) IEA
This entry was last updated onMarch 11, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Glycine max Taxon ID: 3847 351721193 NP_001237713.1 (RefSeq) PRP URP
Glycine max Taxon ID: 3847 2920666 AAC18566.1 (Genbank) PRP URP
Glycine max Taxon ID: 3847 659835590 PRP URP
Show All

Uniprot

Protein NameAccessionEC Number Identifier
n/a O49235 O49235_SOYBN (TrEMBL)

Sequence

Length of Enzyme (full-length): 219 | Length of Functional Domain: 219

1       10        20        30        40        50        60

MSDEVVLLDFWPSPFGMRVRIALAEKGIKYEYKEEDLRNKSPLLLQMNPVHKKIPVLIHN
GKPICESLIAVQYIEEVWNDRNPLLPSDPYQRAQTRFWADYVDKKIYDLGRKIWTSKGEE
KEAAKKEFIEALKLLEEQLGDKTYFGGDNLGFVDIALVPFYTWFKAYETFGTLNIESECP
KFIAWAKRCLQKESVAKSLPDQQKVYEFIMDLRKKLGIE
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.

Structures

PDB ID Title Molecule Name Number of
EFDs
Resolution (Å) Mutant? Het group Links
4TOP Glycine Max Glutathione Transferase 2,4-D Inducible Glutathione S-Transferase 3 2.35 Glutathione CSA • PDB • PDBSum
2VO4 Glutathione Transferase From Glycine Max 2,4-D Inducible Glutathione S-Transferase 3 1.75 4-Nitrophenyl Methanethiol
(2 more ⇓)
CSA • PDB • PDBSum
5AGY Crystal Structure Of A Tau Class Gst Mutant From Glycine Glutathione S-Transferase 3 1.75 Yes 4-Nitrophenyl Methanethiol
(2 more ⇓)
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
Aug. 16, 2016, 8:43 a.m. update curation agent smashiya setDomainBoundaries.py
update domain end position 192 219
update domain start position 5 1
EC number assigned by UniProtKB accession ID.