MLYCD
entrez
23417
canonical
uniprot
O95822
canonical
ensembl
ENSG00000103150
resolver
ensp
ENSP00000262430
resolver
genesymbol
MLYCD
resolver
hgnc
HGNC:7150
resolver
uniprot
Q9UNU5
resolver
uniprot
Q9Y3F2
resolver
uniprot_entry
DCMC_HUMAN
resolver
uniprot_sec
Q9UNU5
resolver
uniprot_sec
Q9Y3F2
resolver
activity_regulation
ACTIVITY REGULATION: Malonyl-CoA decarboxylase activity does not require any cofactors or divalent metal ions. Formation of interchain disulfide bonds leads to positive cooperativity between active sites and increases the affinity for malonyl-CoA and the catalytic efficiency (in vitro). {ECO:0000269|PubMed:15003260, ECO:0000269|PubMed:23482565}.
uniprot
proteins
amino_acid_sequence
MRGFGPGLTARRLLPLRLPPRPPGPRLASGQAAGALERAMDELLRRAVPPTPAYELREKTPAPAEGQCADFVSFYGGLAETAQRAELLGRLARGFGVDHGQVAEQSAGVLHLRQQQREAAVLLQAEDRLRYALVPRYRGLFHHISKLDGGVRFLVQLRADLLEAQALKLVEGPDVREMNGVLKGMLSEWFSSGFLNLERVTWHSPCEVLQKISEAEAVHPVKNWMDMKRRVGPYRRCYFFSHCSTPGEPLVVLHVALTGDISSNIQAIVKEHPPSETEEKNKITAAIFYSISLTQQGLQGVELGTFLIKRVVKELQREFPHLGVFSSLSPIPGFTKWLLGLLNSQTKEHGRNELFTDSECKEISEITGGPINETLKLLLSSSEWVQSEKLVRALQTPLMRLCAWYLYGEKHRGYALNPVANFHLQNGAVLWRINWMADVSLRGITGSCGLMANYRYFLEETGPNSTSYLGSKIIKASEQVLSLVAQFQKNSKL
uniprot
proteins
disease_involvement
DISEASE: Malonyl-CoA decarboxylase deficiency (MLYCD deficiency) [MIM:248360]: Autosomal recessive disease characterized by abdominal pain, chronic constipation, episodic vomiting, metabolic acidosis and malonic aciduria. {ECO:0000269|PubMed:10417274}. Note=The disease is caused by variants affecting the gene represented in this entry.
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:10455107, ECO:0000269|PubMed:15003260, ECO:0000269|PubMed:18314420, ECO:0000269|PubMed:23482565}.
uniprot
proteins
mass_dalton
55003
uniprot
proteins
mutagenesis
MUTAGEN 206; /note="C->S: Abolishes formation of disulfide-linked homotetramers. Abolishes the cooperative enzyme kinetics that are seen under oxidative conditions."; /evidence="ECO:0000269|PubMed:23482565"; MUTAGEN 243; /note="C->S: Does not abolish formation of disulfide-linked homotetramers. No effect on development of cooperative enzyme kinetics in response to oxidative conditions."; /evidence="ECO:0000269|PubMed:23482565"; MUTAGEN 290; /note="S->F: 2-fold reduction in catalytic activity."; /evidence="ECO:0000269|PubMed:23791943"; MUTAGEN 302; /note="E->G: Decreases catalytic activity. Increases affinity for malonyl-CoA."; /evidence="ECO:0000269|PubMed:23482565"; MUTAGEN 329; /note="S->A: 110-fold reduction in catalytic activity."; /evidence="ECO:0000269|PubMed:23791943"; MUTAGEN 423; /note="H->N: 7-fold reduction in catalytic activity."; /evidence="ECO:0000269|PubMed:23791943"; MUTAGEN 456; /note="Y->S: 3.5-fold reduction in catalytic activity."; /evidence="ECO:0000269|PubMed:23791943
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-472 activates malonyl-CoA decarboxylase activity. Deacetylation at Lys-472 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
10417274
uniprot
proteins
pubmed
10455107
uniprot
proteins
pubmed
15003260
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
18314420
uniprot
proteins
pubmed
20178365
uniprot
proteins
pubmed
23482565
uniprot
proteins
pubmed
23791943
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
9869665
uniprot
proteins
sequence_length
493
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10417274}. Mitochondrion matrix {ECO:0000269|PubMed:10417274}. Peroxisome {ECO:0000269|PubMed:10417274}. Peroxisome matrix {ECO:0000250|UniProtKB:Q920F5}. Note=Enzymatically active in all three subcellular compartments. {ECO:0000250|UniProtKB:Q920F5}.
uniprot
proteins