CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019839
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Malonyl-CoA decarboxylase, mitochondrial 
Protein Synonyms/Alias
 MCD 
Gene Name
 Mlycd 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
58PAYELREKTPAPAEGacetylation[1]
167LLEAQALKLVEGPHVacetylation[2, 3, 4]
167LLEAQALKLVEGPHVsuccinylation[4]
221CEAVHPVKNWMDMKRacetylation[2, 4]
221CEAVHPVKNWMDMKRsuccinylation[4]
227VKNWMDMKRRVGPYRacetylation[2]
346GLLNVQGKEHGRNELacetylation[3, 4]
346GLLNVQGKEHGRNELsuccinylation[4]
385LSSGEWVKSEKLTQAacetylation[1, 2, 3, 4, 5]
385LSSGEWVKSEKLTQAsuccinylation[4]
388GEWVKSEKLTQALQGubiquitination[6]
471SISYLGSKNIKASEQacetylation[7]
Reference
 [1] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [3] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [4] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [5] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [6] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [7] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 
Functional Description
 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 (By similarity). Plays a role in controlling the extent of ischemic injury by promoting glucose oxidation. 
Sequence Annotation
 REGION 298 304 Malonyl-CoA binding (By similarity).
 MOTIF 490 492 Microbody targeting signal (Potential).
 BINDING 328 328 Malonyl-CoA (By similarity).
 BINDING 422 422 Malonyl-CoA (By similarity).
 DISULFID 205 205 Interchain (Potential).  
Keyword
 Alternative initiation; Complete proteome; Cytoplasm; Decarboxylase; Disulfide bond; Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Lyase; Mitochondrion; Peroxisome; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 492 AA 
Protein Sequence
MRGLGPGLRA RRLLPLRSPP RPPGPRGRRL CGGLAASAMD ELLRRAVPPT PAYELREKTP 60
APAEGQCADF VSFYGGLAEA SQRAELLGRL AQGFGVDHGQ VAEQSAGVLQ LRQQAREAAV 120
LLQAEDRLRY ALVPRYRGLF HHISKLDGGV RFLVQLRADL LEAQALKLVE GPHVREMNGV 180
LKSMLSEWFS SGFLNLERVT WHSPCEVLQK ISECEAVHPV KNWMDMKRRV GPYRRCYFFS 240
HCSTPGEPLV VLHVALTGDI SNNIQGIVKE CPPTETEERN RIAAAIFYSI SLTQQGLQGV 300
ELGTFLIKRV VKELQKEFPQ LGAFSSLSPI PGFTKWLLGL LNVQGKEHGR NELFTDSECQ 360
EISAVTGNPV HESLKGFLSS GEWVKSEKLT QALQGPLMRL CAWYLYGEKH RGYALNPVAN 420
FHLQNGAVMW RINWMADSSL KGLTSSCGLM VNYRYYLEET GPNSISYLGS KNIKASEQIL 480
SLVAQFQNNS KL 492 
Gene Ontology
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
 GO:0050080; F:malonyl-CoA decarboxylase activity; IEA:EC.
 GO:0006085; P:acetyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
 GO:0019395; P:fatty acid oxidation; IEA:Compara.
 GO:2001294; P:malonyl-CoA catabolic process; IEA:Compara.
 GO:0046321; P:positive regulation of fatty acid oxidation; IEA:Compara.
 GO:0031998; P:regulation of fatty acid beta-oxidation; IEA:Compara.
 GO:0010906; P:regulation of glucose metabolic process; IEA:Compara. 
Interpro
 IPR007956; Malonyl_CoA_deC. 
Pfam
 PF05292; MCD 
SMART
  
PROSITE
  
PRINTS