Top Level Name

  ⌊ Superfamily (core) Glutathione Transferase (cytosolic)

    ⌊ Subgroup Main (cytGST)

  ⌊ Main.2: Nu-like

  ⌊ FunctionalDomain Cytosolic GST-like protein, similar to Nu class GSTs (ID 224774)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Saccharomyces paradoxus Taxon ID: 27291 22094608 AAM91938.1 (Genbank)
Saccharomyces douglasii Taxon ID: 46617 14009512 AAK51641.1 (Genbank)
Saccharomyces paradoxus Taxon ID: 27291 54036582

Uniprot

Protein NameAccessionEC Number Identifier
Protein URE2 Q7LLZ8 URE2_SACPA (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 359 | Length of Functional Domain: 231

1       10        20        30        40        50        60

MMNNNGNQVSNLSNALRQVNIGNRNSNTTTDQSNINFEFSAGVNNNNNNSSSSNNNNNNN
NNAQNNNSGRNGSQSNDNGNNIKDTLEQHRQQQQAFSDMSHVEYSRITKFFQEQPLEGYT
LFSHRSAPNGFKVAIVLSELGFHYNTIFLDFNLGEHRAPEFVSVNPNARVPALIDHGMDN
LSIWESGAILLHLVNKYYKETGNPLLWSDDLADQSQINAWLFFQTSGHAPMIGQALHFRY
FHSQKIASAVERYTDEVRRVYGVVEMALAERREALVMELDTENAAAYSAGTTPMSQSRFF
DYPVWLVGDKLTIADLAFVPWNNVVDRIGINIKIEFPEVYKWTKHMMRRPAVIKALRGE
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
1G6Y Crystal Structure Of The Globular Region Of The Prion Protien Ure2 From Yeast Saccharomyces Cerevisiae Ure2 Protein 13 2.8 CSA • PDB • PDBSum
1G6W Crystal Structure Of The Globular Region Of The Prion Protein Ure2 From The Yeast Saccaromyces Cerevisiae Ure2 Protein 13 2.5 CSA • PDB • PDBSum
1K0D Ure2P In Complex With Glutathione Ure2 Protein 13 2.2 Glutathione CSA • PDB • PDBSum
1K0C Ure2P In Complex With S-P-Nitrobenzylglutathione Ure2 Protein 13 2.5 S-(P-Nitrobenzyl)Glutathione • Glutathione CSA • PDB • PDBSum
1JZR Ure2P In Complex With Glutathione Ure2 Protein 13 2.9 Glutathione CSA • PDB • PDBSum
1K0B Ure2P In Complex With Glutathione Ure2 Protein 13 2.5 Glutathione CSA • PDB • PDBSum
1K0A Ure2P In Complex With S-Hexylglutathione Ure2 Protein 13 2.5 S-Hexylglutathione • Glutathione CSA • PDB • PDBSum
1HQO Crystal Structure Of The Nitrogen Regulation Fragment Of The Yeast Prion Protein Ure2P Ure2 Protein 13 2.3 Selenomethionine 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.
EC number assigned by UniProtKB accession ID.