Top Level Name

  ⌊ Superfamily (core) Glutathione Transferase (cytosolic)

    ⌊ Subgroup Main (cytGST)

  ⌊ Main.5: Phi-like

  ⌊ FunctionalDomain Cytosolic GST-like protein, similar to Phi class GSTs (ID 234537)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Zea mays Taxon ID: 4577 413952343 AFW84992.1 (Genbank) URP
n/a 260058302 ACX27919.1 (Genbank)
Zea mays Taxon ID: 4577 224034943 ACN36547.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
n/a B6SKA0 B6SKA0_MAIZE (TrEMBL)

Sequence

Length of Enzyme (full-length): 214 | Length of Functional Domain: 212

1       10        20        30        40        50        60

MAPMKLYGAVMSWNVTRCATALEEAGSDYEIVPINFATAEHKSPEHLVRNPFGQVPALQD
GDLYLFESRAICKYAARKNKPELLREGNLEEAAMVDVWIEVEANQYTAALNPILFQVLIS
PMLGGTTDQKVVDENLEKLKKVLEVYEARLTKCKYLAGDFLSLADLNHVSVTLCLFATPY
ASVLDAYPHVKAWWSGLMERPSVQKVAALMKPSA
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
12 Ser (S) side chain None -- ICS PubMed:9417936

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
1AXD Structure Of Glutathione S-Transferase-I Bound With The Ligand Lactoylglutathione Glutathione S-Transferase I • Lactoylglutathione 6 2.5 L-Glutamic Acid • S-[(2R)-2-Hydroxypropanoyl]-L-Cysteine CSA • PDB • PDBSum
1BYE Glutathione S-Transferase I From Mais In Complex With Atrazine Glutathione Conjugate Protein (Glutathione S-Transferase) 6 2.8 Atrazine Glutathione Conjugate 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, 8:30 a.m. update curation agent smashiya setDomainBoundaries.py
update domain end position 200 212
update domain start position 4 1
EC number assigned by UniProtKB accession ID.