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uncharacterized protein [Oryza sativa Japonica Group]
malonyl-CoA decarboxylase( domain architecture ID 13603468)
malonyl-CoA decarboxylase (MCD) is a key intermediate in the biosynthesis of long-chain and very long-chain fatty acids, and also has a crucial role in the regulation of fatty acid oxidation through its potent inhibition of carnitine palmitoyltransferase I
List of domain hits
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Name | Accession | Description | Interval | E-value | |||||
MCD super family | cl09364 | Malonyl-CoA decarboxylase C-terminal domain; This family consists of several eukaryotic ... |
206-485 | 6.73e-118 | |||||
Malonyl-CoA decarboxylase C-terminal domain; This family consists of several eukaryotic malonyl-CoA decarboxylase (MLYCD) proteins. Malonyl-CoA, in addition to being an intermediate in the de novo synthesis of fatty acids, is an inhibitor of carnitine palmitoyltransferase I, the enzyme that regulates the transfer of long-chain fatty acyl-CoA into mitochondria, where they are oxidized. After exercise, malonyl-CoA decarboxylase participates with acetyl-CoA carboxylase in regulating the concentration of malonyl-CoA in liver and adipose tissue, as well as in muscle. Malonyl-CoA decarboxylase is regulated by AMP-activated protein kinase (AMPK). The actual alignment was detected with superfamily member pfam05292: Pssm-ID: 461613 Cd Length: 245 Bit Score: 346.86 E-value: 6.73e-118
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MCD_N super family | cl38688 | Malonyl-CoA decarboxylase N-terminal domain; This family consists of several eukaryotic ... |
137-200 | 3.63e-07 | |||||
Malonyl-CoA decarboxylase N-terminal domain; This family consists of several eukaryotic malonyl-CoA decarboxylase (MLYCD) proteins. Malonyl-CoA, in addition to being an intermediate in the de novo synthesis of fatty acids, is an inhibitor of carnitine palmitoyltransferase I, the enzyme that regulates the transfer of long-chain fatty acyl-CoA into mitochondria, where they are oxidized. After exercise, malonyl-CoA decarboxylase participates with acetyl-CoA carboxylase in regulating the concentration of malonyl-CoA in liver and adipose tissue, as well as in muscle. Malonyl-CoA decarboxylase is regulated by AMP-activated protein kinase (AMPK). The actual alignment was detected with superfamily member pfam17408: Pssm-ID: 465421 Cd Length: 85 Bit Score: 47.96 E-value: 3.63e-07
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Name | Accession | Description | Interval | E-value | |||||
MCD | pfam05292 | Malonyl-CoA decarboxylase C-terminal domain; This family consists of several eukaryotic ... |
206-485 | 6.73e-118 | |||||
Malonyl-CoA decarboxylase C-terminal domain; This family consists of several eukaryotic malonyl-CoA decarboxylase (MLYCD) proteins. Malonyl-CoA, in addition to being an intermediate in the de novo synthesis of fatty acids, is an inhibitor of carnitine palmitoyltransferase I, the enzyme that regulates the transfer of long-chain fatty acyl-CoA into mitochondria, where they are oxidized. After exercise, malonyl-CoA decarboxylase participates with acetyl-CoA carboxylase in regulating the concentration of malonyl-CoA in liver and adipose tissue, as well as in muscle. Malonyl-CoA decarboxylase is regulated by AMP-activated protein kinase (AMPK). Pssm-ID: 461613 Cd Length: 245 Bit Score: 346.86 E-value: 6.73e-118
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MCD_N | pfam17408 | Malonyl-CoA decarboxylase N-terminal domain; This family consists of several eukaryotic ... |
137-200 | 3.63e-07 | |||||
Malonyl-CoA decarboxylase N-terminal domain; This family consists of several eukaryotic malonyl-CoA decarboxylase (MLYCD) proteins. Malonyl-CoA, in addition to being an intermediate in the de novo synthesis of fatty acids, is an inhibitor of carnitine palmitoyltransferase I, the enzyme that regulates the transfer of long-chain fatty acyl-CoA into mitochondria, where they are oxidized. After exercise, malonyl-CoA decarboxylase participates with acetyl-CoA carboxylase in regulating the concentration of malonyl-CoA in liver and adipose tissue, as well as in muscle. Malonyl-CoA decarboxylase is regulated by AMP-activated protein kinase (AMPK). Pssm-ID: 465421 Cd Length: 85 Bit Score: 47.96 E-value: 3.63e-07
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Name | Accession | Description | Interval | E-value | |||||
MCD | pfam05292 | Malonyl-CoA decarboxylase C-terminal domain; This family consists of several eukaryotic ... |
206-485 | 6.73e-118 | |||||
Malonyl-CoA decarboxylase C-terminal domain; This family consists of several eukaryotic malonyl-CoA decarboxylase (MLYCD) proteins. Malonyl-CoA, in addition to being an intermediate in the de novo synthesis of fatty acids, is an inhibitor of carnitine palmitoyltransferase I, the enzyme that regulates the transfer of long-chain fatty acyl-CoA into mitochondria, where they are oxidized. After exercise, malonyl-CoA decarboxylase participates with acetyl-CoA carboxylase in regulating the concentration of malonyl-CoA in liver and adipose tissue, as well as in muscle. Malonyl-CoA decarboxylase is regulated by AMP-activated protein kinase (AMPK). Pssm-ID: 461613 Cd Length: 245 Bit Score: 346.86 E-value: 6.73e-118
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MCD_N | pfam17408 | Malonyl-CoA decarboxylase N-terminal domain; This family consists of several eukaryotic ... |
137-200 | 3.63e-07 | |||||
Malonyl-CoA decarboxylase N-terminal domain; This family consists of several eukaryotic malonyl-CoA decarboxylase (MLYCD) proteins. Malonyl-CoA, in addition to being an intermediate in the de novo synthesis of fatty acids, is an inhibitor of carnitine palmitoyltransferase I, the enzyme that regulates the transfer of long-chain fatty acyl-CoA into mitochondria, where they are oxidized. After exercise, malonyl-CoA decarboxylase participates with acetyl-CoA carboxylase in regulating the concentration of malonyl-CoA in liver and adipose tissue, as well as in muscle. Malonyl-CoA decarboxylase is regulated by AMP-activated protein kinase (AMPK). Pssm-ID: 465421 Cd Length: 85 Bit Score: 47.96 E-value: 3.63e-07
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