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Links from Protein

Items: 10

1.

NAD(P)-binding protein

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

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
3.

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
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
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.

FAD-dependent urate hydroxylase HpxO

HpxO is an FAD-dependent urate hydroxylase (EC 1.14.13.113). Like the factor independent urate hydroxylase (EC 1.7.3.3), it consumes O2 and converts urate to 5-hydroxyisourate, which decomposes spontaneously to allantoin and CO2. However, HpxO oxidizes NADH to NAD(+), and produces H20, while EC 1.7.3.3 produces H202 as a byproduct.

Gene:
hpxO
GO Terms:
Molecular Function:
urate oxidase activity (GO:0004846)
Biological Process:
urate catabolic process (GO:0019628)
Molecular Function:
FAD binding (GO:0071949)
Date:
2024-05-30
Family Accession:
NF033623.1
Method:
HMM
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