Top Level Name

  ⌊ Superfamily (core) Glutathione Transferase (cytosolic)

    ⌊ Subgroup Xi (cytGST)

  ⌊ Xi.1

  ⌊ FunctionalDomain similar to Xi class cytGSTs (ID 224988)

Superfamily Assignment Evidence Code(s) ISS
This entry was last updated onFeb. 14, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Shigella boydii 4444-74 Taxon ID: 766140 391276044 EIQ34825.1 (Genbank) URP
Shigella flexneri CCH060 Taxon ID: 754091 391248998 EIQ08235.1 (Genbank) URP
Shigella boydii 3594-74 Taxon ID: 766139 332092041 EGI97119.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
n/a Q31WS6 Q31WS6_SHIBS (TrEMBL)
n/a E7TEZ9 E7TEZ9_SHIFL (TrEMBL)
n/a I6DST3 I6DST3_SHIBO (TrEMBL)

Sequence

Length of Enzyme (full-length): 291 | Length of Functional Domain: 290

1       10        20        30        40        50        60

MTPGPTGTGGFIAEKDRYHLYVSLACPWAHRTLIMRKLKGLEPFISVSVVNPLMLENGWT
FDDSFPGATGDTLYQHEFLYQLYLHADPHYSGRVTVPVLWDKKNHTIVSNESAEIIRMFN
TAFDALGAKAGDYYPPALQTKIDELNGWIYDTVNNGVYKAGFATSQQAYDEAVAKVFESL
ARLEQILGQHRYLTGNQLTEADIRLWTTLVRFDPVYVTHFKCDKHRISDYLNLYGFLRDI
YQMPGIAETVNFDHIRNHYFRSHKTINPTGIISIGPWQDLDEPHGRDVRFG
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 0/4 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
29 Ala (A) side chain MISMATCH: This residue does not match the specified amino acid type of C, and thus may not function in the same manner as other sequences in the subgroup
161 Gly (G) side chain MISMATCH: This residue does not match the specified amino acid type of Y, and thus may not function in the same manner as other sequences in the subgroup
219 His (H) side chain MISMATCH: This residue does not match the specified amino acid type of Y, and thus may not function in the same manner as other sequences in the subgroup
262 Ser (S) side chain MISMATCH: This residue does not match the specified amino acid type of Y, and thus may not function in the same manner as other sequences in the subgroup

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
3R3E The Glutathione Bound Structure Of Yqjg, A Glutathione Transferase Homolog From Escherichia Coli K-12 Uncharacterized Protein Yqjg 36 2.21 Glutathione • Sulfate Ion CSA • PDB • PDBSum
4G0L Glutathionyl-Hydroquinone Reductase, Yqjg, Of E.Coli Complexed With Gsh Protein Yqjg 36 2.62 Glutathione
(2 more ⇓) 		CSA • PDB • PDBSum
4G0K Glutathionyl-Hydroquinone Reductase, Yqjg, Of E.Coli Complexed With Gs-Menadione Protein Yqjg 36 2.56 Sulfate Ion
(2 more ⇓) 		CSA • PDB • PDBSum
4G0I Glutathionyl-Hydroquinone Reductase, Yqjg Of Escherichia Coli Protein Yqjg 36 2.05 Sulfate Ion • 2-(N-Morpholino)-Ethanesulfonic Acid 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, 6:49 a.m. update curation agent smashiya setDomainBoundaries.py
update domain end position 243 259
update domain start position 85 89
Aug. 16, 2016, 8:44 a.m. update domain end position 259 290
update domain start position 89 1
EC number assigned by UniProtKB accession ID.