CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004449
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Methylmalonyl-CoA mutase, mitochondrial 
Protein Synonyms/Alias
 MCM; Methylmalonyl-CoA isomerase 
Gene Name
 Mut 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
46PEWAVLAKKQLKGKNacetylation[1]
52AKKQLKGKNPEDLIWacetylation[1, 2, 3, 4]
52AKKQLKGKNPEDLIWsuccinylation[3]
87PEELPGVKPFTRGPYacetylation[1, 2, 4, 5]
87PEELPGVKPFTRGPYubiquitination[6]
119STVEESNKFYKDNIKacetylation[2, 4]
210EQGVPKEKLTGTIQNacetylation[1, 2, 3, 4, 5]
210EQGVPKEKLTGTIQNsuccinylation[3]
210EQGVPKEKLTGTIQNubiquitination[6]
221TIQNDILKEFMVRNTubiquitination[6]
333LWAHLIEKMFQPKNSacetylation[1]
341MFQPKNSKSLLLRAHacetylation[1, 3, 5]
341MFQPKNSKSLLLRAHsuccinylation[3]
575KKVFGEHKANDRMVSacetylation[1, 2]
593RQEFGESKEITSAIKacetylation[1, 2, 3]
593RQEFGESKEITSAIKsuccinylation[3]
600KEITSAIKRVNKFMEacetylation[1]
604SAIKRVNKFMEREGRacetylation[2, 3, 4, 5]
604SAIKRVNKFMEREGRsuccinylation[3]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [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] 
Functional Description
 Involved in the degradation of several amino acids, odd- chain fatty acids and cholesterol via propionyl-CoA to the tricarboxylic acid cycle (By similarity). 
Sequence Annotation
 DOMAIN 612 744 B12-binding.
 METAL 625 625 Cobalt (cobalamin axial ligand) (By  
Keyword
 Cobalamin; Cobalt; Complete proteome; Isomerase; Metal-binding; Mitochondrion; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 748 AA 
Protein Sequence
MLRAKNQLFL LSPHYLKQLN IPSASRWKRL LHQQQPLHPE WAVLAKKQLK GKNPEDLIWH 60
TPEGISIKPL YSRADTLDLP EELPGVKPFT RGPYPTMYTY RPWTIRQYAG FSTVEESNKF 120
YKDNIKAGQQ GLSVAFDLAT HRGYDSDNPR VRGDVGMAGV AIDTVEDTKI LFDGIPLEKM 180
SVSMTMNGAV IPVLATFIVT GEEQGVPKEK LTGTIQNDIL KEFMVRNTYI FPPEPSMKII 240
ADIFQYTAQH MPKFNSISIS GYHMQEAGAD AILELAYTIA DGLEYCRTGL QAGLTIDEFA 300
PRLSFFWGIG MNFYMEIAKM RAGRRLWAHL IEKMFQPKNS KSLLLRAHCQ TSGWSLTEQD 360
PYNNIVRTAI EAMAAVFGGT QSLHTNSFDE ALGLPTVKSA RIARNTQIII QEESGIPKVA 420
DPWGGSYMME SLTNDVYEAA LKLIYEVEEM GGMAKAVAEG IPKLRIEECA ARRQARIDSG 480
SEVIVGVNKY QLEKEDSVEV LAIDNTSVRK KQIEKLKKIK SSRDQALAEQ CLSALTQCAA 540
SGDGNILALA VDAARARCTV GEITDALKKV FGEHKANDRM VSGAYRQEFG ESKEITSAIK 600
RVNKFMEREG RRPRLLVAKM GQDGHDRGAK VIATGFADLG FDVDIGPLFQ TPREVAQQAV 660
DADVHAVGVS TLAAGHKTLV PELIKELTAL GRPDILVMCG GVIPPQDYEF LYEVGVSNVF 720
GPGTRIPRAA VQVLDDIEKC LAEKQQSV 748 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004494; F:methylmalonyl-CoA mutase activity; IDA:MGI.
 GO:0072341; F:modified amino acid binding; IEA:Compara.
 GO:0050667; P:homocysteine metabolic process; IEA:Compara.
 GO:0009791; P:post-embryonic development; IMP:MGI. 
Interpro
 IPR006159; Acid_CoA_mut_C.
 IPR016176; Cbl-dep_enz_cat.
 IPR014348; Cbl-dep_enz_cat-sub.
 IPR006158; Cobalamin-bd.
 IPR006099; MeMalonylCoA_mutase_a/b_cat.
 IPR006098; MMCoA_mutase_a_cat. 
Pfam
 PF02310; B12-binding
 PF01642; MM_CoA_mutase 
SMART
  
PROSITE
 PS51332; B12_BINDING
 PS00544; METMALONYL_COA_MUTASE 
PRINTS