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Links from Protein

Items: 6

1.

Glutathione S-transferase, N-terminal domain

This family is closely related to Pfam:PF02798. (from Pfam)

GO Terms:
Molecular Function:
protein binding (GO:0005515)
Biological Process:
glutathione metabolic process (GO:0006749)
Date:
2024-08-14
Family Accession:
NF024801.5
Method:
HMM
2.

glutaredoxin domain-containing protein

GO Terms:
Molecular Function:
protein-disulfide reductase activity (GO:0015035)
Date:
2024-08-14
Family Accession:
NF012675.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.

glutaredoxin 3

Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system [1]. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This family of glutaredoxins includes the E. coli protein GrxC (Grx3) which appears to have a secondary role in reducing ribonucleotide reductase (in the absence of GrxA) possibly indicating a role in the reduction of other protein disulfides [2].

Gene:
grxC
GO Terms:
Biological Process:
cell redox homeostasis (GO:0045454)
Date:
2024-06-24
Family Accession:
TIGR02181.1
Method:
HMM
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