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mcd

Gene
mcd
Protein
(2S)-methylsuccinyl-CoA dehydrogenase
Organism
Rhodobacter sphaeroides
Length
548 amino acids
Function
Involved in the ethylmalonyl-CoA pathway, a new acetyl-CoA assimilation strategy that operates in a number of bacteria and replaces the glyoxylate cycle. Catalyzes the oxidation of (2S)-methylsuccinyl-CoA to yield mesaconyl-(C1)-CoA. Highly specific for (S)-methylsuccinyl-CoA.
Similarity
Belongs to the acyl-CoA dehydrogenase family.
Mass
59.772 kDa
Sequence
MTGQPLLGDLLTLASDALPEVEALFETARSALKERVTTDGKVSSKALEEEQFAAHALSWLATYVESLRQMRAWAGRLETEGRFGEMEALILQIAFGEYLAQIRGGIPMSQTETARVQDIGIELGHPGEAVRRLIQAGNTPAARARLVALMRDNHGRATFGASGLDEELEMIRDQFRRFADERVAPHAHGWHMRDELIPMEIVEALAEMGVFGLTIPEEFGGFGLSKASMVVVSEELSRGYIGVGSLGTRSEIAAELILCGGTDAQKAAWLPKLASGEILPTAVFTEPNTGSDLGSLRTRAVKDGDEWVVHGNKTWITHAARTHVMTLLARTDLETTDYRGLSMFLAEKVPGTDADPFPTPGMTGGEIEVLGYRGMKEYEIGFDGFRVKAENLLGGVEGQGFKQLMQTFESARIQTAARAIGVAQNALEVGMQYAEERKQFGKALIEFPRVAGKLAMMAVEIMVARQLTYHSAWEKDHGQRCDLEAGMAKLLGARVAWAAADNALQIHGGNGFALEYQISRILCDARILNIFEGAAEIQAQVIARRLLD

Gene
mcd
Protein
(2S)-methylsuccinyl-CoA dehydrogenase
Organism
Rhodobacter sphaeroides
Length
548 amino acids
Function
Involved in the ethylmalonyl-CoA pathway, a new acetyl-CoA assimilation strategy that operates in a number of bacteria and replaces the glyoxylate cycle. Catalyzes the oxidation of (2S)-methylsuccinyl-CoA to yield mesaconyl-(C1)-CoA. Highly specific for (S)-methylsuccinyl-CoA.
Similarity
Belongs to the acyl-CoA dehydrogenase family.
Mass
59.772 kDa
Sequence
MTGQPLLGDLLTLASDALPEVEALFETARSALKERVTTDGKVSSKALEEEQFAAHALSWLATYVESLRQMRAWAGRLETEGRFGEMEALILQIAFGEYLAQIRGGIPMSQTETARVQDIGIELGHPGEAVRRLIQAGNTPAARARLVALMRDNHGRATFGASGLDEELEMIRDQFRRFADERVAPHAHGWHMRDELIPMEIVEALAEMGVFGLTIPEEFGGFGLSKASMVVVSEELSRGYIGVGSLGTRSEIAAELILCGGTDAQKAAWLPKLASGEILPTAVFTEPNTGSDLGSLRTRAVKDGDEWVVHGNKTWITHAARTHVMTLLARTDLETTDYRGLSMFLAEKVPGTDADPFPTPGMTGGEIEVLGYRGMKEYEIGFDGFRVKAENLLGGVEGQGFKQLMQTFESARIQTAARAIGVAQNALEVGMQYAEERKQFGKALIEFPRVAGKLAMMAVEIMVARQLTYHSAWEKDHGQRCDLEAGMAKLLGARVAWAAADNALQIHGGNGFALEYQISRILCDARILNIFEGAAEIQAQVIARRLLD