Mlycd
entrez
85239
canonical
uniprot
Q920F5
canonical
ensembl
ENSRNOG00000014522
resolver
ensembl
ENSRNOG00055020693
resolver
ensembl
ENSRNOG00060023704
resolver
ensp
ENSRNOP00000019923
resolver
genesymbol
Mlycd
resolver
uniprot
Q9WUY2
resolver
uniprot_entry
DCMC_RAT
resolver
uniprot_sec
Q9WUY2
resolver
activity_regulation
ACTIVITY REGULATION: Malonyl-CoA decarboxylase activity does not require any cofactors or divalent metal ions. {ECO:0000250|UniProtKB:O95822}.
uniprot
proteins
amino_acid_sequence
MRGLGPSLRARRLLPLRYPPRPPGPRGPRLCSGLTASAMDELLRRAVPPTPAYELREKTPAPAEGQCADFVSFYGGLAEAAQRAELLGRLAQGFGVDHGQVAEQSAGVLQLRQQSREAAVLLQAEDRLRYALVPRYRGLFHHISKLDGGVRFLVQLRADLLEAQALKLVEGPHVREMNGVLKSMLSEWFSSGFLNLERVTWHSPCEVLQKISECEAVHPVKNWMDMKRRVGPYRRCYFFSHCSTPGDPLVVLHVALTGDISNNIQSIVKECPPSETEEKNRIAAAVFYSISLTQQGLQGVELGTFLIKRVVKELQKEFPHLGAFSSLSPIPGFTKWLLGLLNVQGKEYGRNELFTDSECKEIAEVTGDPVHESLKGLLSSGEWAKSEKLAQALQGPLMRLCAWYLYGEKHRGYALNPVANFHLQNGAVMWRINWMADSSLKGLTSSCGLMVNYRYYLEETGPNSISYLGSKNIKASEQILSLVAQFQSNSKL
uniprot
proteins
ec_number
4.1.1.9
uniprot
proteins
function
FUNCTION: Catalyzes the conversion of malonyl-CoA to acetyl-CoA. In the fatty acid biosynthesis MCD selectively removes malonyl-CoA and thus assures that methyl-malonyl-CoA is the only chain elongating substrate for fatty acid synthase and that fatty acids with multiple methyl side chains are produced. In peroxisomes it may be involved in degrading intraperoxisomal malonyl-CoA, which is generated by the peroxisomal beta-oxidation of odd chain-length dicarboxylic fatty acids. Plays a role in the metabolic balance between glucose and lipid oxidation in muscle independent of alterations in insulin signaling. May play a role in controlling the extent of ischemic injury by promoting glucose oxidation. {ECO:0000269|PubMed:10947976, ECO:0000269|PubMed:15105298, ECO:0000269|PubMed:16298369}.
uniprot
proteins
mass_dalton
54762
uniprot
proteins
mutagenesis
MUTAGEN 210; /note="K->M: Abolishes catalytic activity."; /evidence="ECO:0000269|PubMed:16739991"; MUTAGEN 308; /note="K->M: 40% reduction in catalytic activity."; /evidence="ECO:0000269|PubMed:16739991"; MUTAGEN 388; /note="K->M: 40% reduction in catalytic activity."; /evidence="ECO:0000269|PubMed:16739991
uniprot
proteins
pathway_participation
PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from malonyl-CoA: step 1/1.
uniprot
proteins
post_translational_modification
PTM: Acetylation at Lys-471 activates malonyl-CoA decarboxylase activity. Deacetylation at Lys-471 by SIRT4 represses activity, leading to promote lipogenesis (By similarity). {ECO:0000250|UniProtKB:Q99J39}.; PTM: Interchain disulfide bonds may form in peroxisomes (Potential). Interchain disulfide bonds are not expected to form in the reducing environment of the cytoplasm and mitochondria. {ECO:0000305}.
uniprot
proteins
pubmed
10229677
uniprot
proteins
pubmed
10455107
uniprot
proteins
pubmed
10947976
uniprot
proteins
pubmed
12297032
uniprot
proteins
pubmed
15105298
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16298369
uniprot
proteins
pubmed
16739991
uniprot
proteins
sequence_length
492
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16298369}. Mitochondrion matrix {ECO:0000269|PubMed:16298369}. Peroxisome {ECO:0000250}. Peroxisome matrix {ECO:0000269|PubMed:16298369}. Note=Enzymatically active in all three subcellular compartments.
uniprot
proteins