Mlycd
entrez
56690
canonical
uniprot
Q99J39
canonical
ensembl
ENSMUSG00000074064
resolver
ensp
ENSMUSP00000095970
resolver
ensp
ENSMUSP00000166693
resolver
ensp
ENSMUSP00000166705
resolver
genesymbol
Mlycd
resolver
uniprot
Q7TNL6
resolver
uniprot_entry
DCMC_MOUSE
resolver
uniprot_sec
Q7TNL6
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
MRGLGPGLRARRLLPLRSPPRPPGPRGRRLCGGLAASAMDELLRRAVPPTPAYELREKTPAPAEGQCADFVSFYGGLAEASQRAELLGRLAQGFGVDHGQVAEQSAGVLQLRQQAREAAVLLQAEDRLRYALVPRYRGLFHHISKLDGGVRFLVQLRADLLEAQALKLVEGPHVREMNGVLKSMLSEWFSSGFLNLERVTWHSPCEVLQKISECEAVHPVKNWMDMKRRVGPYRRCYFFSHCSTPGEPLVVLHVALTGDISNNIQGIVKECPPTETEERNRIAAAIFYSISLTQQGLQGVELGTFLIKRVVKELQKEFPQLGAFSSLSPIPGFTKWLLGLLNVQGKEHGRNELFTDSECQEISAVTGNPVHESLKGFLSSGEWVKSEKLTQALQGPLMRLCAWYLYGEKHRGYALNPVANFHLQNGAVMWRINWMADSSLKGLTSSCGLMVNYRYYLEETGPNSISYLGSKNIKASEQILSLVAQFQNNSKL
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. Plays a role in controlling the extent of ischemic injury by promoting glucose oxidation. {ECO:0000269|PubMed:17030679, ECO:0000269|PubMed:23746352}.
uniprot
proteins
mass_dalton
54736
uniprot
proteins
mutagenesis
MUTAGEN 471; /note="K->Q: Mimicks constitutive acetylation, leading to increased malonyl-CoA decarboxylase activity."; /evidence="ECO:0000269|PubMed:23746352"; MUTAGEN 471; /note="K->R: Decreased acetylation, leading to reduced malonyl-CoA decarboxylase activity."; /evidence="ECO:0000269|PubMed:23746352
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: 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}.; PTM: Acetylation at Lys-471 activates malonyl-CoA decarboxylase activity. Deacetylation at Lys-471 by SIRT4 represses activity, leading to promote lipogenesis. {ECO:0000269|PubMed:23746352}.
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17030679
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23576753
uniprot
proteins
pubmed
23746352
uniprot
proteins
pubmed
23806337
uniprot
proteins
sequence_length
492
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95822}. Mitochondrion matrix {ECO:0000269|PubMed:23746352}. Peroxisome {ECO:0000250|UniProtKB:O95822}. Peroxisome matrix {ECO:0000250|UniProtKB:Q920F5}. Note=Enzymatically active in all three subcellular compartments. {ECO:0000250|UniProtKB:Q920F5}.
uniprot
proteins