Protein Family Models for Protein (Select 447201309) - Protein Family Models

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Select item 4296531.

Electron transfer flavoprotein-ubiquinone oxidoreductase (ETF-QO) is a a 4Fe4S flavoprotein located in the inner mitochondrial membrane and catalyses ubiquinone (UQ) reduction. It forms a single structural domain with three functional regions (that bind FAD, the 4Fe4S cluster, and UQ) which are closely packed and share structural elements [1]. This domain includes the residues involved in UQ binding [1]. This domain is also found in FixC proteins from bacteria, which share similarities with ETF-QO [2]. Paper describing PDB structure 2gmh. [1]. 17050691. Structure of electron transfer flavoprotein-ubiquinone oxidoreductase and electron transfer to the mitochondrial ubiquinone pool. Zhang J, Frerman FE, Kim JJ;. Proc Natl Acad Sci U S A. 2006;103:16212-16217. [2]. 15386115. The electron transfer flavoprotein fixABCX gene products from Azospirillum brasilense show a NifA-dependent promoter regulation. Sperotto RA, Gross J, Vedoy C, Passaglia LM, Schrank IS;. Curr Microbiol. 2004;49:267-273. (from Pfam)

Date:: 2024-10-16

Family Accession:: NF045305.2
Method:: HMM

Select item 4240322.

NAD(P)-binding protein

Date:: 2024-08-14

Family Accession:: NF024842.5
Method:: HMM

Select item 4214943.

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 4133084.

Thi4 family

This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme. [1]. 7961415. Cloning, nucleotide sequence, and regulation of Schizosaccharomyces pombe thi4, a thiamine biosynthetic gene. Zurlinden A, Schweingruber ME;. J Bacteriol 1994;176:6631-6635. (from Pfam)

Date:: 2024-10-16

Family Accession:: NF014053.5
Method:: HMM

Select item 4125315.

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

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:: 2024-10-16

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:: 2024-10-16

Family Accession:: NF013086.5
Method:: HMM

Select item 4083068.