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Links from Protein

Items: 14

1.

C-terminal domain of 1-Cys peroxiredoxin

This is the C-terminal domain of 1-Cys peroxiredoxin (1-cysPrx), a member of the peroxiredoxin superfamily which protect cells against membrane oxidation through glutathione (GSH)-dependent reduction of phospholipid hydroperoxides to corresponding alcohols [1]. The C-terminal domain is crucial for providing the extra cysteine necessary for dimerisation of the whole molecule. Loss of the enzyme's peroxidase activity is associated with oxidation of the catalytic cysteine, upstream of this domain; and glutathionylation, presumably through its disruption of protein structure, facilitates access for GSH, resulting in spontaneous reduction of the mixed disulfide to the sulfhydryl and consequent activation of the enzyme [2]. The domain is associated with family AhpC-TSA, Pfam:PF00578, which carries the catalytic cysteine. [1]. 9587003. Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution. Choi HJ, Kang SW, Yang CH, Rhee SG, Ryu SE;. Nat Struct Biol. 1998;5:400-406. [2]. 15004285. Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST. Manevich Y, Feinstein SI, Fisher AB;. Proc Natl Acad Sci U S A. 2004;101:3780-3785. (from Pfam)

GO Terms:
Molecular Function:
peroxiredoxin activity (GO:0051920)
Date:
2024-10-16
Family Accession:
NF021902.5
Method:
HMM
2.

redoxin family protein

This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins. (from Pfam)

GO Terms:
Molecular Function:
oxidoreductase activity (GO:0016491)
Date:
2024-08-14
Family Accession:
NF020123.5
Method:
HMM
3.

redoxin domain-containing protein

This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA). [1]. 8041738. Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes. Chae HZ, Robison K, Poole LB, Church G, Storz G, Rhee SG;. Proc Natl Acad Sci U S A 1994;91:7017-7021. (from Pfam)

GO Terms:
Molecular Function:
antioxidant activity (GO:0016209)
Molecular Function:
oxidoreductase activity (GO:0016491)
Date:
2024-10-16
Family Accession:
NF012787.5
Method:
HMM
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
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6.
new record, indexing in progress
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7.
new record, indexing in progress
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8.
new record, indexing in progress
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9.
new record, indexing in progress
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10.
new record, indexing in progress
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11.
new record, indexing in progress
Family Accession:
12.

peroxiredoxin

peroxiredoxin, also called thioredoxin peroxidase or alkyl hydroperoxide reductase, is a thiol-specific antioxidant protein that protects cells against reactive oxygen species

Date:
2017-02-03
Family Accession:
11496410
Method:
Sparcle
13.
new record, indexing in progress
Family Accession:
14.

alkyl hydroperoxide reductase subunit C

This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one subunit of a two-subunit complex with subunit F (TIGR03140). Usually these are found as an apparent operon. The gene has been characterized in Bacteroides fragilis, where it is important in oxidative stress defense. AhpC contains two invariant cysteine residues, one near the N-terminus and one near the C-terminus, each followed immediately by a proline residue.

Gene:
ahpC
GO Terms:
Biological Process:
response to oxidative stress (GO:0006979)
Molecular Function:
NADH-dependent peroxiredoxin activity (GO:0102039)
Date:
2022-03-01
Family Accession:
TIGR03137.1
Method:
HMM
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