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Links from Protein

Items: 19

1.

Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster

Domain II of the enzyme dihydroprymidine dehydrogenase binds FAD. Dihydroprymidine dehydrogenase catalyses the first and rate-limiting step of pyrimidine degradation by converting pyrimidines to the corresponding 5,6- dihydro compounds [1]. This domain carries two Fe4-S4 clusters. [1]. 11796730. Crystal structure of the productive ternary complex of dihydropyrimidine dehydrogenase with NADPH and 5-iodouracil. Implications for mechanism of inhibition and electron transfer. Dobritzsch D, Ricagno S, Schneider G, Schnackerz KD, Lindqvist Y;. J Biol Chem. 2002;277:13155-13166. (from Pfam)

Date:
2024-10-16
Family Accession:
NF026042.5
Method:
HMM
2.

NAD(P)-binding domain-containing protein

Date:
2024-08-14
Family Accession:
NF025114.5
Method:
HMM
3.

NAD(P)-binding protein

Date:
2024-08-14
Family Accession:
NF024842.5
Method:
HMM
4.

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
5.

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
6.

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
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.
new record, indexing in progress
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18.

Se_ygfK family protein

Se_ygfK family protein

Date:
2017-03-02
Family Accession:
11496600
Method:
Sparcle
19.

putative selenate reductase subunit YgfK

Members of this protein family are YgfK, predicted to be one subunit of a three-subunit, molybdopterin-containing selenate reductase. This enzyme is found, typically, in genomic regions associated with xanthine dehydrogenase homologs predicted to belong to the selenium-dependent molybdenum hydroxylases (SDMH). Therefore, the selenate reductase is suggested to play a role in furnishing selenide for SelD, the selenophosphate synthase.

Gene:
ygfK
GO Terms:
Molecular Function:
oxidoreductase activity (GO:0016491)
Molecular Function:
iron-sulfur cluster binding (GO:0051536)
Date:
2021-09-15
Family Accession:
TIGR03315.1
Method:
HMM
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