Top Level Name
⌊ Superfamily (core) Glutathione Transferase (cytosolic)
Total |
100% ![]() |
<100% ![]() |
Family unknown ![]() |
||||
Functional domains | 10639 | ||||||
UniProtKB | 53705 | 0 | 0 | 53705 | |||
GI | 105536 | 0 | 0 | 105536 | |||
Structures | 457 | ||||||
Reactions | 0 | ||||||
Functional domains of this superfamily were last updated on June 27, 2017 | |||||||
New functional domains were last added to this superfamily on Oct. 10, 2012 |
The cytosolic glutathione transferases (cytGSTs) are known for adding the tripeptide glutathione (GSH) to substrate compounds. The archetypal role of cytGSTs is in mammalian enzymatic detoxification, in which electrophilic small molecules are modified by the addition of GSH, making compounds more soluble. Glutathionylated compounds are recognized by transporters and exported from the cell. It is known that cytGSTs also catalyze other reactions like reduction of peroxides in which the glutathionylated compound is an intermediate. Certain bacteria use cytGSTs to exploit various compounds as a carbon source. All cytGSTs catalyze the nucleophilic attack of GSH on a substrate compound. The activation of GSH is achieved in part by interactions with a residue in the enzyme active site: a tyrosine ("AMPS" subgroup), or a serine or cysteine ("Main" subgroup). Cytosolic GSTs incorporate a distant variant of the thioredoxin fold. The great variation of reactions of the cytGSTs may be categorized into "reaction types" by similarities in chemistry. Key sequence and structure similarity networks colored and described similarly to figures 1, 3, and 5B in the publication, “Large-Scale Determination of Sequence, Structure, and Function Relationships in Cytosolic Glutathione Transferases across the Biosphere,” (PMID 24756107) are available for download from the Download Archived Data tab. Downloads of the fasta sequence set from that paper, along with annotation data are also available.
Mashiyama ST, Malabanan MM, Akiva E, Bhosle R, Branch MC, Hillerich B, Jagessar K, Kim J, Patskovsky Y, Seidel RD, Stead M, Toro R, Vetting MW, Almo SC, Armstrong RN, Babbitt PC
Large-scale determination of sequence, structure, and function relationships in cytosolic glutathione transferases across the biosphere
▸ Abstract
PLoS Biol 2014;12(4):None-None | PubMed ID: 24756107
EFI
Static File Downloads
File Name | Description | Parameters | Stats |
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sfld_superfamily_19.tsv | Annotation data table, tab separated columns | size=8.8M #rows=13098 |
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sfld_superfamily_19.fasta | Protein sequences, fasta format | size=3.7M #seqs=13097 |
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sfldAlignmentSF19.msa | Annotated Sequence Alignment, Stockholm format | 97 sequences size: 41K |
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Seq_Str_SimNetworks_forSFLDposting.tgz | Sequence and structure similarity networks associated with “Large-Scale Determination of Sequence, Structure, and Function Relationships in Cytosolic Glutathione Transferases across the Biosphere,” (PMID 24756107) |
Subgroup ▸ Legend | T ![]() |
S ![]() |
||
---|---|---|---|---|
AMPS (cytGST): Alpha-, Mu-, Pi-, and Sigma-like | 826 | 242 | ||
┗ 1: AMPS.1 | 769 | 242 | ||
Grx2-like | 0 | 0 | ||
┗ 1: Grx2-like.1 | 0 | 0 | ||
Main (cytGST) | 8806 | 198 | ||
┗ 1: Main.1: Beta-like | 1626 | 25 | ||
┗ 1: Main.2: Nu-like | 1606 | 26 | ||
┗ 1: Main.3: Omega- and Tau-like | 1011 | 16 | ||
┗ 1: Main.4: Theta-like | 806 | 35 | ||
┗ 1: Main.5: Phi-like | 401 | 15 | ||
┗ 1: Main.6 | 187 | 4 | ||
┗ 1: Main.7 | 314 | 3 | ||
┗ 1: Main.8: Zeta-like | 525 | 11 | ||
┗ 1: Main.9 | 236 | 9 | ||
┗ 1: Main.10 | 173 | 30 | ||
┗ 1: Main.11: Lambda-like | 53 | 2 | ||
┗ 1: Main.12 | 207 | 0 | ||
┗ 1: Main.13 | 338 | 6 | ||
┗ 1: Main.14 | 171 | 0 | ||
┗ 1: Main.15 | 179 | 2 | ||
┗ 1: Main.16 | 39 | 0 | ||
┗ 1: Main.17 | 107 | 0 | ||
┗ 1: Main.18 | 0 | 0 | ||
┗ 1: Main.19 | 34 | 0 | ||
┗ 1: Main.20 | 40 | 3 | ||
┗ 1: Main.21 | 49 | 0 | ||
┗ 1: Main.22 | 70 | 2 | ||
┗ 1: Main.23 | 64 | 2 | ||
┗ 1: Main.24 | 0 | 0 | ||
┗ 1: Main.25 | 29 | 2 | ||
┗ 1: Main.26 | 50 | 0 | ||
┗ 1: Main.27 | 51 | 0 | ||
┗ 1: Main.28 | 52 | 2 | ||
Prostaglandin E synthase like | 30 | 2 | ||
┗ 1: Prostaglandin E synthase like.1 | 30 | 2 | ||
SUF1 | 64 | 0 | ||
┗ 1: SUF1.1 | 63 | 0 | ||
SUF2 | 0 | 0 | ||
┗ 1: SUF2.1 | 0 | 0 | ||
┗ 1: SUF2.2 | 0 | 0 | ||
Xi (cytGST) | 891 | 11 | ||
┗ 1: Xi.1 | 891 | 11 |