Protein Family Models for Protein (Select 503766215) - Protein Family Models

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Select item 4240321.

NAD(P)-binding protein

Date:: 2024-08-14

Family Accession:: NF024842.5
Method:: HMM

Select item 4214942.

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

Select item 4169533.

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

Select item 4159574.

lycopene cyclase family protein

This family consists of lycopene beta and epsilon cyclase proteins. Carotenoids with cyclic end groups are essential components of the photosynthetic membranes in all plants, algae, and cyanobacteria. These lipid-soluble compounds protect against photo-oxidation, harvest light for photosynthesis, and dissipate excess light energy absorbed by the antenna pigments. The cyclisation of lycopene (psi, psi-carotene) is a key branch point in the pathway of carotenoid biosynthesis. Two types of cyclic end groups are found in higher plant carotenoids: the beta and epsilon rings. Carotenoids with two beta rings are ubiquitous, and those with one beta and one epsilon ring are common; however, carotenoids with two epsilon rings are rare [1,2]. [1]. 8837512. Functional analysis of the beta and epsilon lycopene cyclase. enzymes of Arabidopsis reveals a mechanism for control of cyclic. carotenoid formation.. Cunningham FX Jr, Pogson B, Sun Z, McDonald KA, DellaPenna D,. Gantt E;. Plant Cell 1996;8:1613-1626.. [2]. 11226339. One ring or two? Determination of ring number in carotenoids by. lycopene epsilon-cyclases.. Cunningham FX Jr, Gantt E;. Proc Natl Acad Sci U S A 2001;98:2905-2910. (from Pfam)

Date:: 2024-08-14

Family Accession:: NF017634.5
Method:: HMM

Select item 4120295.

FAD-dependent oxidoreductase

Date:: 2024-08-14

Family Accession:: NF013314.5
Method:: HMM

Select item 4115806.

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

Select item 4111767.

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

Select item 4101348.

menaquinone reductase

Gene:: menJ

GO Terms:

Biological Process:: menaquinone biosynthetic process (GO:0009234)

Molecular Function:: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627)

Molecular Function:: oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor (GO:0016628)

Date:: 2024-02-01

Family Accession:: NF045655.1
Method:: HMM

Select item 4001159.