Top Level Name

  ⌊ Superfamily (core) Glutathione Transferase (cytosolic)

    ⌊ Subgroup Main (cytGST)

  ⌊ Main.8: Zeta-like

  ⌊ FunctionalDomain Cytosolic GST-like protein, similar to Zeta class GSTs (ID 233211)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Ralstonia sp. U2 Taxon ID: 70356 695199909 YP_009076550.1 (RefSeq)
Taxon ID: 80840 651312716 WP_026437509.1 (RefSeq)
Comamonas testosteroni Taxon ID: 285 692379049 KGH10191.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
Maleylpyruvate isomerase {ECO:0000303|PubMed:18824004, ECO:0000312|EMBL:AAD12621.1} O86043 NAGL_RALSP (Swiss-Prot)

Sequence

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

1       10        20        30        40        50        60

MKLYNFWRSGTSHRLRIALNLKGVPYEYLAVHLGKEEHLKDAFKALNPQQLVPALDTGAQ
VLIQSPAIIEWLEEQYPTPALLPADADGRQRVRALAAIVGCDIHPINNRRILEYLRKTFG
ADEAAINAWCGTWISAGFDAYEALLAVDPKRGRYSFGDTPTLADCYLVPQVESARRFQVD
LTPYPLIRAVDAACGELDAFRRAAPAAQPDSA
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
2V6K Structure Of Maleyl Pyruvate Isomerase, A Bacterial Glutathione-S-Transferase In Zeta Class, In Complex With Substrate Analogue Dicarboxyethyl Glutathione Maleylpyruvate Isomerase 3 1.3 Sodium Ion
(2 more ⇓) 		CSA • PDB • PDBSum
2JL4 Holo Structure Of Maleyl Pyruvate Isomerase, A Bacterial Glutathione-S-Transferase In Zeta Class Maleylpyruvate Isomerase 3 2.3 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
Aug. 16, 2016, 8:27 a.m. update curation agent smashiya setDomainBoundaries.py
update domain end position 196 212
EC number assigned by UniProtKB accession ID.