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Links from Protein

Items: 15

1.

NAD(P)-binding domain-containing protein

Date:
2024-08-14
Family Accession:
NF025114.5
Method:
HMM
2.

FAD-dependent oxidoreductase

This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain. [1]. 8805537. Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase. Mande SS, Sarfaty S, Allen MD, Perham RN, Hol WG;. Structure 1996;4:277-286. (from Pfam)

GO Terms:
Molecular Function:
oxidoreductase activity (GO:0016491)
Date:
2024-10-16
Family Accession:
NF019604.5
Method:
HMM
3.

Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain

This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. [1]. 8771196. The crystal structure of trypanothione reductase from the human pathogen Trypanosoma cruzi at 2.3 A resolution. Zhang Y, Bond CS, Bailey S, Cunningham ML, Fairlamb AH, Hunter WN;. Protein Sci 1996;5:52-61. (from Pfam)

GO Terms:
Biological Process:
cell redox homeostasis (GO:0045454)
Date:
2024-10-16
Family Accession:
NF014860.5
Method:
HMM
4.

NAD-binding protein

This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain. [1]. 8805537. Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase. Mande SS, Sarfaty S, Allen MD, Perham RN, Hol WG;. Structure 1996;4:277-286. (from Pfam)

Date:
2024-10-16
Family Accession:
NF012299.5
Method:
HMM
5.
new record, indexing in progress
Family Accession:
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
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12.
new record, indexing in progress
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13.

glutathione-disulfide reductase

glutathione-disulfide reductase catalyzes the reduction of glutathione disulfide (GSSG) to form two molecules of glutathione (GSH); functions in the maintenance of high levels of reduced glutathione in the cytosol

Date:
2023-03-17
Family Accession:
11482057
Method:
Sparcle
14.

glutathione-disulfide reductase

The tripeptide glutathione is an important reductant, e.g., for maintaining the cellular thiol/disulfide status and for protecting against reactive oxygen species such as hydrogen peroxide. Glutathione-disulfide reductase regenerates reduced glutathione from oxidized glutathione (glutathione disulfide) + NADPH. This HMM represents one of two closely related subfamilies of glutathione-disulfide reductase. Both are closely related to trypanothione reductase, and separate models are built so each of the three can describe proteins with conserved function. This model describes glutathione-disulfide reductases of animals, yeast, and a number of animal-resident bacteria.

Gene:
gor
GO Terms:
Molecular Function:
glutathione-disulfide reductase (NADPH) activity (GO:0004362)
Biological Process:
glutathione metabolic process (GO:0006749)
Biological Process:
cell redox homeostasis (GO:0045454)
Molecular Function:
flavin adenine dinucleotide binding (GO:0050660)
Molecular Function:
NADP binding (GO:0050661)
Date:
2024-06-04
Family Accession:
TIGR01421.1
Method:
HMM
15.

glutathione-disulfide reductase

Gene:
gorA
GO Terms:
Molecular Function:
glutathione-disulfide reductase (NADPH) activity (GO:0004362)
Biological Process:
glutathione metabolic process (GO:0006749)
Biological Process:
cell redox homeostasis (GO:0045454)
Molecular Function:
flavin adenine dinucleotide binding (GO:0050660)
Molecular Function:
NADP binding (GO:0050661)
Date:
2021-07-28
Family Accession:
NF004776.0
Method:
HMM
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