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Links from Protein

Items: 20

1.

FAD-dependent oxidoreductase

This family of proteins contains FAD dependent oxidoreductases and related proteins. (from Pfam)

Date:
2024-08-14
Family Accession:
NF024240.5
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:
2024-08-14
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:
2024-08-14
Family Accession:
NF014860.5
Method:
HMM
4.

FAD-dependent oxidoreductase

Date:
2024-08-14
Family Accession:
NF013314.5
Method:
HMM
5.

FAD-binding protein

This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase. [1]. 8061609. Structure of glutathione reductase from Escherichia coli at 1.86. A resolution: comparison with the enzyme from human. erythrocytes.. Mittl PR, Schulz GE. Protein Sci 1994;3:799-809. (from Pfam)

Date:
2024-08-14
Family Accession:
NF013086.5
Method:
HMM
6.

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:
2024-08-14
Family Accession:
NF012299.5
Method:
HMM
7.
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19.

dihydrolipoyl dehydrogenase

This HMM describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.

Gene:
lpdA
GO Terms:
Molecular Function:
dihydrolipoyl dehydrogenase activity (GO:0004148)
Molecular Function:
flavin adenine dinucleotide binding (GO:0050660)
Date:
2024-06-27
Family Accession:
TIGR01350.1
Method:
HMM
20.

dihydrolipoyl dehydrogenase family protein

dihydrolipoyl dehydrogenase family protein belonging to the class-I pyridine nucleotide-disulfide oxidoreductase superfamily may function as a FAD/NAD(P)-dependent oxidoreductase, similar to dihydrolipoyl dehydrogenase which catalyzes the oxidation of dihydrolipoamide to lipoamide and is often a component of multienzyme 2-oxo-acid dehydrogenase complexes

Date:
2024-07-05
Family Accession:
11441193
Method:
Sparcle
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