Top Level Name

  ⌊ Superfamily (core) Glutathione Transferase (cytosolic)

    ⌊ Subgroup Main (cytGST)

  ⌊ Main.1: Beta-like

  ⌊ FunctionalDomain Cytosolic GST-like protein, similar to Beta class GSTs (ID 56442)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Taxon ID: 561 446688395 WP_000765741.1 (RefSeq)
Escherichia albertii KF1 Taxon ID: 1440052 569539919 AHE62226.1 (Genbank) URP
Escherichia albertii TW07627 Taxon ID: 502347 170122328 EDS91259.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
n/a A0A0S3MVU2 A0A0S3MVU2_9ESCH (TrEMBL)
n/a A0A0K4INV7 A0A0K4INV7_ECOLX (TrEMBL)
n/a B1END7 B1END7_ESCAT (TrEMBL)
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Sequence

Length of Enzyme (full-length): 201 | Length of Functional Domain: 201

1       10        20        30        40        50        60

MKLFYKPGACSLASHITLRESGKDFTLVSVDLMKKRLENGDDYFAVNPKGQVPALLLDDG
TLLTEGVAIMQYLADSVPDRHLLASVNSISRYKTIEWLNYIATELHKGFTPLFRPDTPEE
YKPTVRAQLEKKLQYVNDTLKDGHWICGQRFTIADAYLFTVLRWAYGVKLNLEGLEHIAA
YMQRMAERPAVKAALTAEGLQ
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
1N2A Crystal Structure Of A Bacterial Glutathione Transferase From Escherichia Coli With Glutathione Sulfonate In The Active Site Glutathione S-Transferase 29 1.9 Glutathione Sulfonic Acid CSA • PDB • PDBSum
1A0F Crystal Structure Of Glutathione S-Transferase From Escherichia Coli Complexed With Glutathionesulfonic Acid Glutathione S-Transferase 29 2.1 Glutathione Sulfonic Acid CSA • PDB • PDBSum
4KGI Crystal Structure Of A Glutathione Transferase Family Member From Shigella Flexneri, Target Efi-507258, Bound Gsh, Tev-His-Tag Linker In Active Site Glutathione S-Transferase 28 1.6 Glutathione 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, 6:41 a.m. update curation agent smashiya setDomainBoundaries.py
update domain end position 201 188
Aug. 16, 2016, 8:34 a.m. update domain end position 188 201
EC number assigned by UniProtKB accession ID.