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Fumarate reductase flavoprotein C-term
This family contains fumarate reductases, succinate dehydrogenases and L-aspartate oxidases. [1]. 10373108. Structure of the Escherichia coli fumarate reductase respiratory complex. Iverson TM, Luna-Chavez C, Cecchini G, Rees DC;. Science 1999;284:1961-1966. (from Pfam)
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)
succinate dehydrogenase flavoprotein subunit
Succinate dehydrogenase and fumarate reductase are homologous enzymes reversible in principle but favored under different circumstances. This HMM represents a narrowly defined clade of the succinate dehydrogenase flavoprotein subunit as found in mitochondria, in Rickettsia, in E. coli and other Proteobacteria, and in a few other lineages. However, this HMM excludes all known fumarate reductases. It also excludes putative succinate dehydrogenases that appear to diverged before the split between E. coli succinate dehydrogenase and fumarate reductase.
succinate dehydrogenase or fumarate reductase, flavoprotein subunit
This HMM represents the succinate dehydrogenase flavoprotein subunit as found in Gram-negative bacteria, mitochondria, and some Archaea. Mitochondrial forms interact with ubiquinone and are designated EC 1.3.5.1, but can be degraded to 1.3.99.1. Some isozymes in E. coli and other species run primarily in the opposite direction and are designated fumarate reductase.
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