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Literature summary for 1.6.5.2 extracted from

  • Ramos, A.R.; Grein, F.; Oliveira, G.P.; Venceslau, S.S.; Keller, K.L.; Wall, J.D.; Pereira, I.A.
    The FlxABCD-HdrABC proteins correspond to a novel NADH dehydrogenase/heterodisulfide reductase widespread in anaerobic bacteria and involved in ethanol metabolism in Desulfovibrio vulgaris Hildenborough (2015), Environ. Microbiol., 17, 2288-2305 .
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Desulfovibrio vulgaris Q729F2 and Q729F1 and Q729F0 Q729F2 i.e. subunit FlxA, Q729F1 i.e. subunit FlxB, Q729F0 i.e. subunits FlxCD
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Desulfovibrio vulgaris Hildenborough Q729F2 and Q729F1 and Q729F0 Q729F2 i.e. subunit FlxA, Q729F1 i.e. subunit FlxB, Q729F0 i.e. subunits FlxCD
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Synonyms

Synonyms Comment Organism
DVU_2399 locus name, subunit FlxA Desulfovibrio vulgaris
DVU_2400 locus name, subunit FlxB Desulfovibrio vulgaris
DVU_2401 locus name, subunit FlxCD Desulfovibrio vulgaris
FlxABCD
-
Desulfovibrio vulgaris

Cofactor

Cofactor Comment Organism Structure
FAD flavoprotein subunit FlxA is involved in oxidation/reduction of NAD(P)H/NAD(P)+ Desulfovibrio vulgaris

Expression

Organism Comment Expression
Desulfovibrio vulgaris expression increases during growth in ethanol-sulfate, and to a less extent during pyruvate fermentation up

General Information

General Information Comment Organism
physiological function a gene disruption strain is unable to grow with ethanol-sulfate. The FlxABCD-HdrABC (heterodisulfide reductase) proteins are essential for NADH oxidation during growth on ethanol, while in fermentation they operate in reverse, reducing NAD+ for ethanol production Desulfovibrio vulgaris