Gene/Proteome Database (LMPD)
Proteins
malonyl-CoA decarboxylase, mitochondrial | |
---|---|
Refseq ID | NP_064350 |
Protein GI | 56797739 |
UniProt ID | Q99J39 |
mRNA ID | NM_019966 |
Length | 492 |
RefSeq Status | PROVISIONAL |
MRGLGPGLRARRLLPLRSPPRPPGPRGRRLCGGLAASAMDELLRRAVPPTPAYELREKTPAPAEGQCADFVSFYGGLAEASQRAELLGRLAQGFGVDHGQVAEQSAGVLQLRQQAREAAVLLQAEDRLRYALVPRYRGLFHHISKLDGGVRFLVQLRADLLEAQALKLVEGPHVREMNGVLKSMLSEWFSSGFLNLERVTWHSPCEVLQKISECEAVHPVKNWMDMKRRVGPYRRCYFFSHCSTPGEPLVVLHVALTGDISNNIQGIVKECPPTETEERNRIAAAIFYSISLTQQGLQGVELGTFLIKRVVKELQKEFPQLGAFSSLSPIPGFTKWLLGLLNVQGKEHGRNELFTDSECQEISAVTGNPVHESLKGFLSSGEWVKSEKLTQALQGPLMRLCAWYLYGEKHRGYALNPVANFHLQNGAVMWRINWMADSSLKGLTSSCGLMVNYRYYLEETGPNSISYLGSKNIKASEQILSLVAQFQNNSKL |
Gene Information
Gene Ontology (GO Annotations)
GO ID | Source | Type | Description |
---|---|---|---|
GO:0005737 | ISS:UniProtKB | C | cytoplasm |
GO:0005829 | IEA:Ensembl | C | cytosol |
GO:0005759 | IDA:UniProtKB | C | mitochondrial matrix |
GO:0005739 | IDA:MGI | C | mitochondrion |
GO:0005782 | ISS:UniProtKB | C | peroxisomal matrix |
GO:0005777 | ISS:UniProtKB | C | peroxisome |
GO:0050080 | IDA:UniProtKB | F | malonyl-CoA decarboxylase activity |
GO:0006085 | ISS:UniProtKB | P | acetyl-CoA biosynthetic process |
GO:0006633 | ISS:UniProtKB | P | fatty acid biosynthetic process |
GO:0019395 | IEA:Ensembl | P | fatty acid oxidation |
GO:2001294 | IDA:UniProtKB | P | malonyl-CoA catabolic process |
GO:0046321 | IDA:UniProtKB | P | positive regulation of fatty acid oxidation |
GO:0031998 | IEA:Ensembl | P | regulation of fatty acid beta-oxidation |
GO:0010906 | ISS:UniProtKB | P | regulation of glucose metabolic process |
GO:0002931 | ISS:UniProtKB | P | response to ischemia |
KEGG Pathway Links
Domain Information
InterPro Annotations
Accession | Description |
---|---|
IPR007956 | Malonyl-CoA decarboxylase |
UniProt Annotations
Entry Information
Comments
Comment Type | Description |
---|---|
Alternative Products | Event=Alternative initiation; Named isoforms=2; Comment=A single transcription start site has been demonstrated in Rat.; Name=Mitochondrial; IsoId=Q99J39-1; Sequence=Displayed; Name=Cytoplasmic+peroxisomal; IsoId=Q99J39-2; Sequence=VSP_018817; Note=May be produced by alternative initiation at Met-39 of isoform mitochondrial. Alternatively, represents a proteolytic processed form of the mitochondrial form.; |
Catalytic Activity | Malonyl-CoA = acetyl-CoA + CO(2). {ECO:0000269|PubMed:17030679}. |
Disruption Phenotype | Mice show an increased expression of genes regulating fatty acid utilization and likely contributes to the absence of changes in energy metabolism in the aerobic heart. Display a preference for glucose utilization after ischemia and improve functional recovery of the heart. {ECO:0000269|PubMed:17030679}. |
Enzyme Regulation | Malonyl-CoA decarboxylase activity does not require any cofactors or divalent metal ions. {ECO:0000250}. |
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}. |
Pathway | Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from malonyl-CoA: step 1/1. |
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:23576753, ECO:0000269|PubMed:23746352}. |
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}. |
Subcellular Location | Cytoplasm {ECO:0000250}. Mitochondrion matrix {ECO:0000269|PubMed:23746352}. Peroxisome {ECO:0000250}. Peroxisome matrix {ECO:0000250}. Note=Enzymatically active in all three subcellular compartments. {ECO:0000250}. |
Subunit | Homotetramer. Dimer of dimers. The two subunits within a dimer display conformational differences suggesting that at any given moment, only one of the two subunits is competent for malonyl-CoA binding and catalytic activity. Under oxidizing conditions, can form disulfide-linked homotetramers (in vitro). Associates with the peroxisomal targeting signal receptor PEX5 (By similarity). {ECO:0000250}. |
Identical and Related Proteins
Unique RefSeq proteins for LMP000544 (as displayed in Record Overview)
Protein GI | Database | Accession | Length | Protein Name |
---|---|---|---|---|
56797739 | RefSeq | NP_064350 | 492 | malonyl-CoA decarboxylase, mitochondrial |
Identical Sequences to LMP000544 proteins
Reference | Database | Accession | Length | Protein Name |
---|---|---|---|---|
GI:56797739 | DBBJ | BAC38505.1 | 492 | unnamed protein product [Mus musculus] |
GI:56797739 | GenBank | AAH04764.1 | 492 | Malonyl-CoA decarboxylase [Mus musculus] |
GI:56797739 | SwissProt | Q99J39.1 | 492 | RecName: Full=Malonyl-CoA decarboxylase, mitochondrial; Short=MCD; Flags: Precursor [Mus musculus] |
Related Sequences to LMP000544 proteins
Reference | Database | Accession | Length | Protein Name |
---|---|---|---|---|
GI:56797739 | GenBank | AAL09352.1 | 492 | malonyl-CoA decarboxylase [Rattus norvegicus] |
GI:56797739 | GenBank | AAH61845.1 | 492 | Malonyl-CoA decarboxylase [Rattus norvegicus] |
GI:56797739 | GenBank | EDL92663.1 | 492 | malonyl-CoA decarboxylase [Rattus norvegicus] |
GI:56797739 | RefSeq | NP_445929.1 | 491 | malonyl-CoA decarboxylase, mitochondrial [Rattus norvegicus] |
GI:56797739 | RefSeq | XP_006531281.1 | 474 | PREDICTED: malonyl-CoA decarboxylase, mitochondrial isoform X1 [Mus musculus] |
GI:56797739 | SwissProt | Q920F5.1 | 492 | RecName: Full=Malonyl-CoA decarboxylase, mitochondrial; Short=MCD; Flags: Precursor [Rattus norvegicus] |