Primary Information |
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| BoMiProt ID | Bomi7052 |
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| Protein Name | Methylmalonyl-CoA epimerase, mitochondrial/DL-methylmalonyl-CoA racemase |
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| Organism | Bos taurus |
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| Uniprot ID | Q2KIZ3 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_001039460.1 |
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| Aminoacid Length | 175 |
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| Molecular Weight | 18514 |
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| FASTA Sequence |
Download |
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| Gene Name | MCEE |
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| Gene ID | 508170 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | Methylmalonyl-CoA epimerase (MCE) is an enzyme involved in the propionyl-CoA metabolism that is responsible for the degradation of branched amino acids and odd-chain fatty acids. |
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| Biochemical Properties | This protein is involved in the flow of D-methylmalonyl-CoA to L-methylmalonyl-CoA----tricarboxylic acid cycle |
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| PTMs | Acetylation at Lys |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| NA |
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| Predicted Disorder Regions | 1-6, 21-37, 108-114 |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Additional Comments | The sequence similarity to an MCE of known structure was high enough to permit a three-dimensional model to be built, suggesting conservation of ligand and metal binding sites. Comparison with corresponding sequences from a variety of organisms shows more than 1/6 of the sequence is completely conserved. |
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| Bibliography | 1.Stabler SP, Marcell PD, Allen RH. Isolation and characterization of DL-methylmalonyl-coenzyme A racemase from rat liver. Arch Biochem Biophys. 1985 Aug 15;241(1):252-64. doi: 10.1016/0003-9861(85)90381-9. PMID: 2862845. 2.Kühnl J, Bobik T, Procter JB, Burmeister C, Höppner J, Wilde I, Lüersen K, Torda AE, Walter RD, Liebau E. Functional analysis of the methylmalonyl-CoA epimerase from Caenorhabditis elegans. FEBS J. 2005 Mar;272(6):1465-77. doi: 10.1111/j.1742-4658.2005.04579.x. PMID: 15752362. |
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