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
sfld_superfamily_19.tsv Annotation data table, tab separated columns size=8.8M
#rows=13098
sfld_superfamily_19.fasta Protein sequences, fasta format size=3.7M
#seqs=13097
sfldAlignmentSF19.msa Annotated Sequence Alignment, Stockholm format 97 sequences
size: 41K
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)

Total number of functional domains in this group.
Number of Functional Domains that have been manually or automatically been assigned to a family.
Number of Functional Domains that have not been assigned to a family.
Number of structures available from the PDB for members of this group.
Number of Functional Domains with 100% of Conserved Residues
Number of Functional Domains with less than 100% Conserved Residues
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
Depth of the multi-level Subgroup hierarchy.