UniProt Accession

 MUTA_HUMAN; P22033; A8K953; Q5SYZ3; Q96B11; Q9UD64 

Genbank Protein ID

 M65131; M37510; M37499; M37500; M37501; M37503; M37504; M37505; M37506; M37507; M37508; M37509; AK292568; BT007434; AL590668; BC016282 

Genbank Nucleotide ID

 AAA59569.1; AAA99226.1; AAA99226.1; AAA99226.1; AAA99226.1; AAA99226.1; AAA99226.1; AAA99226.1; AAA99226.1; AAA99226.1; AAA99226.1; AAA99226.1; BAF85257.1; AAP36102.1; CAI14311.1; AAH16282.1 

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

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
89	PEELPGVKPFTRGPY	ubiquitination	[1]
223	TIQNDILKEFMVRNT	ubiquitination	[1]
335	LWAHLIEKMFQPKNS	acetylation	[2]
343	MFQPKNSKSLLLRAH	acetylation	[3]
343	MFQPKNSKSLLLRAH	ubiquitination	[4]
400	ALGLPTVKSARIARN	ubiquitination	[1]

Reference

 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [2] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [3] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961] 

Functional Description

 Involved in the degradation of several amino acids, odd- chain fatty acids and cholesterol via propionyl-CoA to the tricarboxylic acid cycle. MCM has different functions in other species. 

Sequence Annotation

 DOMAIN 614 746 B12-binding.
 METAL 627 627 Cobalt (cobalamin axial ligand) (By  

Keyword

 3D-structure; Cobalamin; Cobalt; Complete proteome; Direct protein sequencing; Disease mutation; Isomerase; Metal-binding; Mitochondrion; Polymorphism; Reference proteome; Transit peptide. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 750 AA 

Protein Sequence

Gene Ontology

 GO:0005759; C:mitochondrial matrix; TAS:Reactome.
 GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004494; F:methylmalonyl-CoA mutase activity; TAS:ProtInc.
 GO:0072341; F:modified amino acid binding; IDA:UniProtKB.
 GO:0006635; P:fatty acid beta-oxidation; TAS:Reactome.
 GO:0050667; P:homocysteine metabolic process; IDA:UniProtKB.
 GO:0009791; P:post-embryonic development; IEA:Compara.
 GO:0019626; P:short-chain fatty acid catabolic process; TAS:Reactome. 

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