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Links from Protein

Items: 19

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.

rhodanese-like domain-containing protein

Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases. Crystal structure. [1]. 8702871. Active site structural features for chemically modified forms of rhodanese. Gliubich F, Gazerro M, Zanotti G, Delbono S, Bombieri G, Berni R;. J Biol Chem 1996;271:21054-21061. (from Pfam)

Date:
2024-10-16

Family Accession:
NF012790.5
Method:
HMM

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.
new record, indexing in progress
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14.
new record, indexing in progress
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15.
new record, indexing in progress
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16.
new record, indexing in progress
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17.

pyridine nucleotide-disulfide oxidoreductase family protein

pyridine nucleotide-disulfide oxidoreductase (PNDOR) family protein containing both flavoprotein reductase and rhodanese domains; similar to Shewanella loihica NADH-dependent persulfide reductase (Npsr) that is involved in the dissimilatory reduction of sulfur

Date:
2019-12-09

Family Accession:
11496784
Method:
Sparcle

18.

CoA-disulfide reductase

NADPH-dependent; catalyzes the reduction of coenzyme A disulfide

GO Terms:
Molecular Function:
oxidoreductase activity (GO:0016491)
Biological Process:
cell redox homeostasis (GO:0045454)
Date:
2021-10-13

Family Accession:
NF010037.0
Method:
HMM

19.

CoA-disulfide reductase

Members of this protein family are CoA-disulfide reductase (EC 1.8.1.14), as characterized in Staphylococcus aureus, Pyrococcus horikoshii, and Borrelia burgdorferi, and inferred in several other species on the basis of high levels of CoA and an absence of glutathione as a protective thiol.

Gene:
cdr
GO Terms:
Molecular Function:
protein disulfide isomerase activity (GO:0003756)
Molecular Function:
CoA-disulfide reductase (NADPH) activity (GO:0050451)
Molecular Function:
flavin adenine dinucleotide binding (GO:0050660)
Molecular Function:
NADP binding (GO:0050661)
Date:
2024-05-30

Family Accession:
TIGR03385.1
Method:
HMM

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