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Links from Protein

Items: 17

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:
2024-08-14
Family Accession:
NF026042.5
Method:
HMM
2.

NAD(P)-binding protein

Date:
2024-08-14
Family Accession:
NF024842.5
Method:
HMM
3.

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
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:
2024-08-14
Family Accession:
NF013646.5
Method:
HMM
5.

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
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.

glutamate synthase subunit beta

beta subunit of the glutamate synthase that catalyzes the formation of L-glutamate from 2-oxoglutarate and L-glutamine, as part of the L-glutamate biosynthesis GLT pathway

Date:
2017-02-27
Family Accession:
11486208
Method:
Sparcle
17.

glutamate synthase small subunit

This HMM represents one of three built for the NADPH-dependent or NADH-dependent glutamate synthase (EC 1.4.1.13 and 1.4.1.14, respectively) small subunit or homologous region. TIGR01316 describes a family in several archaeal and deeply branched bacterial lineages of a homotetrameric form for which there is no large subunit. Another model describes glutamate synthase small subunit from gamma and some alpha subdivision Proteobacteria plus paralogs of unknown function. This model describes the small subunit, or homologous region of longer forms proteins, of eukaryotes, Gram-positive bacteria, cyanobacteria, and some other lineages. All members with known function participate in NADH or NADPH-dependent reactions to interconvert between glutamine plus 2-oxoglutarate and two molecules of glutamate.

Gene:
gltD
GO Terms:
Biological Process:
glutamate biosynthetic process (GO:0006537)
Cellular Component:
glutamate synthase complex (NADPH) (GO:0009342)
Molecular Function:
glutamate synthase activity, NAD(P)H as acceptor (GO:0045181)
Date:
2021-04-27
Family Accession:
TIGR01317.1
Method:
HMM
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