U.S. flag

An official website of the United States government

Format
Items per page
Sort by

Send to:

Choose Destination

Links from Protein

Items: 1 to 20 of 21

1.

NAD(P)-binding protein

Date:
2024-08-14
Family Accession:
NF024842.5
Method:
HMM
2.

3-hydroxyacyl-CoA dehydrogenase NAD-binding domain-containing protein

The term 3-hydroxyacyl-CoA dehydrogenase, corresponding to EC 1.1.1.35, covers a range of specificities, as the acyl group is not specified. Beta-hydroxyacyl dehydrogenase is a synonym. There may be mulitple members of the family in a single genome, e.g. FadB, FabJ, and PaaH from Escherichia coli K-12.

GO Terms:
Biological Process:
fatty acid metabolic process (GO:0006631)
Molecular Function:
NAD+ binding (GO:0070403)
Date:
2024-10-16
Family Accession:
NF014757.5
Method:
HMM
3.

FAD-dependent oxidoreductase

This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1. [1]. 9153426. Active site plasticity in D-amino acid oxidase: a crystallographic analysis. Todone F, Vanoni MA, Mozzarelli A, Bolognesi M, Coda A, Curti B, Mattevi A;. Biochemistry 1997;36:5853-5860. (from Pfam)

GO Terms:
Molecular Function:
oxidoreductase activity (GO:0016491)
Date:
2024-10-16
Family Accession:
NF013434.5
Method:
HMM
4.

FAD-dependent monooxygenase

This domain is involved in FAD binding in a number of enzymes. [1]. 1409567. Crystal structure of the reduced form of p-hydroxybenzoate hydroxylase refined at 2.3A resolution. Schreuder HA, van der Laan JM, Swarte MB, Kalk KH, Hol WG, Drenth J;. Proteins 1992;14:178-190. (from Pfam)

GO Terms:
Molecular Function:
FAD binding (GO:0071949)
Date:
2024-10-16
Family Accession:
NF013646.5
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:
2024-10-16
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:
2024-10-16
Family Accession:
NF012299.5
Method:
HMM
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.
new record, indexing in progress
Family Accession:
10.
new record, indexing in progress
Family Accession:
11.
new record, indexing in progress
Family Accession:
12.
new record, indexing in progress
Family Accession:
13.
new record, indexing in progress
Family Accession:
14.
new record, indexing in progress
Family Accession:
15.
new record, indexing in progress
Family Accession:
16.
new record, indexing in progress
Family Accession:
17.
new record, indexing in progress
Family Accession:
18.
new record, indexing in progress
Family Accession:
19.
new record, indexing in progress
Family Accession:
20.

glycine oxidase ThiO

glycine oxidase ThiO catalyzes the oxidation of glycine, leading to glyoxyl imine and hydrogen peroxide as primary products; glyoxyl imine is used for the biosynthesis of the thiazole ring of thiamine

Date:
2023-06-15
Family Accession:
11494177
Method:
Sparcle
Format
Items per page
Sort by

Send to:

Choose Destination

Supplemental Content

Find related data

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
Support Center