Top Level Name

  ⌊ Superfamily (core) Glutathione Transferase (cytosolic)

    ⌊ Subgroup Xi (cytGST)

  ⌊ Xi.1

  ⌊ FunctionalDomain similar to Xi class cytGSTs (ID 227554)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Escherichia coli Taxon ID: 562 446453356 WP_000531211.1 (RefSeq) URP
Escherichia coli 53638 Taxon ID: 344610 188489220 EDU64323.1 (Genbank) URP

Uniprot

Protein NameAccessionEC Number Identifier
n/a A0A0E1SXP0 A0A0E1SXP0_ECOLX (TrEMBL)

Sequence

Length of Enzyme (full-length): 328 | Length of Functional Domain: 327

1       10        20        30        40        50        60

MGQLIDGVWHDTWYDTKSTGGKFQRSASAFRNWLTADGAPGPTGTGGFIAEKDRYHLYVS
LACPWAHRTLIMRKLKGLEPFISVSVVNPLMLENGWTFDDSFPGATGDTLYQHEFLYQLY
LRADPHYSGRVTVPVLWDKKNHTIVSNESAEIIRMFNTAFDALGAKAGDYYPPALQTKID
ELNGWIYDTVNNGVYKAGFATSQQAYDEAVEKVFESLARLEQILGQHRYLTGNQLTEADI
RLWTTLVRFDPVYVTHLKCDKHRISDYLNLYGFLRDIYQMPGIAETVNFDHIRNHYFRSH
KTINPTGIISIGPWQDLDEPHGRDVRFG
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
66 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
198 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
256 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
299 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
Aug. 16, 2016, 8:46 a.m. update curation agent smashiya setDomainBoundaries.py
update domain end position 280 327
update domain start position 119 1
EC number assigned by UniProtKB accession ID.