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Protein

Methylmalonyl-CoA mutase, mitochondrial

Gene

MMUT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

adenosylcob(III)alamin1 Publication

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by itaconyl-CoA, a metabolite that inactivates the coenzyme B12 cofactor (PubMed:29056341).

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=4.7 nM for adenosylcob(III)alamin1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei50malonyl-CoA1 Publication1
    Binding sitei228malonyl-CoA1 Publication1
    Binding sitei255malonyl-CoA1 Publication1
    Binding sitei265malonyl-CoA1 Publication1
    <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi627Cobalt (cobalamin 2 axial ligand)1 Publication1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    • cobalamin binding Source: UniProtKB
    • GTPase activity Source: UniProtKB
    • identical protein binding Source: UniProtKB
    • metal ion binding Source: UniProtKB-KW
    • methylmalonyl-CoA mutase activity Source: UniProtKB
    • modified amino acid binding Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionIsomerase
    LigandCobalamin, Cobalt, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:HS07322-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    5.4.99.2 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-196741 Cobalamin (Cbl, vitamin B12) transport and metabolism
    R-HSA-3359475 Defective MMAA causes methylmalonic aciduria type cblA
    R-HSA-3359478 Defective MUT causes methylmalonic aciduria mut type
    R-HSA-71032 Propionyl-CoA catabolism

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P22033

    Chemistry databases

    SwissLipids knowledge resource for lipid biology

    More...
    SwissLipidsi
    SLP:000001254

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Methylmalonyl-CoA mutase, mitochondrialCurated (EC:5.4.99.22 Publications)
    Short name:
    MCM
    Alternative name(s):
    Methylmalonyl-CoA isomerase
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:MMUTImported
    Synonyms:MUTImported
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000146085.7

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:7526 MMUT

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    609058 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_P22033

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Mitochondrion

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

    Methylmalonic aciduria type mut (MMAM)23 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionAn often fatal disorder of organic acid metabolism. Common clinical features include lethargy, vomiting, failure to thrive, hypotonia, neurological deficit and early death. Two forms of the disease are distinguished by the presence (mut-) or absence (mut0) of residual enzyme activity. Mut0 patients have more severe neurological manifestations of the disease than do MUT- patients. MMAM is unresponsive to vitamin B12 therapy.
    See also OMIM:251000
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_0800317 – 750Missing in MMAM; mut-. 1 PublicationAdd BLAST744
    Natural variantiVAR_02347269I → V in MMAM; mut0. 3 PublicationsCorresponds to variant dbSNP:rs115923556EnsemblClinVar.1
    Natural variantiVAR_02659286P → L in MMAM; mut0 and mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability. 2 PublicationsCorresponds to variant dbSNP:rs769348060EnsemblClinVar.1
    Natural variantiVAR_02659387G → E in MMAM; mut0. 1 Publication1
    Natural variantiVAR_00440993R → H in MMAM; mut0; decreased methylmalonyl-CoA mutase activity. 4 PublicationsCorresponds to variant dbSNP:rs121918251EnsemblClinVar.1
    Natural variantiVAR_02659494G → R in MMAM; mut0. 1 PublicationCorresponds to variant dbSNP:rs727504022EnsemblClinVar.1
    Natural variantiVAR_02239394G → V in MMAM; mut- and mut0. 2 PublicationsCorresponds to variant dbSNP:rs535411418Ensembl.1
    Natural variantiVAR_02659595P → R in MMAM; mut0. 1 PublicationCorresponds to variant dbSNP:rs190834116EnsemblClinVar.1
    Natural variantiVAR_075379100Y → C in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability. 2 PublicationsCorresponds to variant dbSNP:rs864309735EnsemblClinVar.1
    Natural variantiVAR_004410105W → R in MMAM; mut0. 2 PublicationsCorresponds to variant dbSNP:rs121918249EnsemblClinVar.1
    Natural variantiVAR_026596108R → C in MMAM; mut0. 2 PublicationsCorresponds to variant dbSNP:rs121918257EnsemblClinVar.1
    Natural variantiVAR_026597108R → G in MMAM; mut-. 1 Publication1
    Natural variantiVAR_022394108R → H in MMAM; mut0. 3 PublicationsCorresponds to variant dbSNP:rs483352778EnsemblClinVar.1
    Natural variantiVAR_023473109Q → R in MMAM; mut0. 2 PublicationsCorresponds to variant dbSNP:rs1461110052Ensembl.1
    Natural variantiVAR_075380110Y → C in MMAM. 1 PublicationCorresponds to variant dbSNP:rs796052005EnsemblClinVar.1
    Natural variantiVAR_077210126N → K in MMAM. 1 PublicationCorresponds to variant dbSNP:rs879253827EnsemblClinVar.1
    Natural variantiVAR_077211133G → R in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity. 1 PublicationCorresponds to variant dbSNP:rs879253828EnsemblClinVar.1
    Natural variantiVAR_075381137A → G in MMAM. 1 PublicationCorresponds to variant dbSNP:rs941483851EnsemblClinVar.1
    Natural variantiVAR_022395137A → V in MMAM; mut0. 2 PublicationsCorresponds to variant dbSNP:rs941483851EnsemblClinVar.1
    Natural variantiVAR_077212139D → N in MMAM; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs879253829EnsemblClinVar.1
    Natural variantiVAR_078342140L → P in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity. 2 Publications1
    Natural variantiVAR_078343141A → T in MMAM; decreased protein expression. 1 Publication1
    Natural variantiVAR_075382143H → Y in MMAM; mut0. 1 Publication1
    Natural variantiVAR_026598145G → S in MMAM; mut0. 1 Publication1
    Natural variantiVAR_022396148S → L in MMAM; mut0. 2 PublicationsCorresponds to variant dbSNP:rs1300547552Ensembl.1
    Natural variantiVAR_080032152 – 750Missing in MMAM; mut0. 1 PublicationAdd BLAST599
    Natural variantiVAR_022397156D → N in MMAM; mut-. 1 Publication1
    Natural variantiVAR_077213156D → V in MMAM. 1 PublicationCorresponds to variant dbSNP:rs757000253EnsemblClinVar.1
    Natural variantiVAR_022398158G → V in MMAM; mut0. 1 Publication1
    Natural variantiVAR_077214161G → R in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity. 2 Publications1
    Natural variantiVAR_078344161G → V in MMAM; decreased protein expression. 1 Publication1
    Natural variantiVAR_022399174F → S in MMAM; mut0. 3 PublicationsCorresponds to variant dbSNP:rs864309733EnsemblClinVar.1
    Natural variantiVAR_026599186M → V in MMAM; mut-. 1 PublicationCorresponds to variant dbSNP:rs148331800EnsemblClinVar.1
    Natural variantiVAR_077215187T → S in MMAM; mut0. 1 PublicationCorresponds to variant dbSNP:rs879253830EnsemblClinVar.1
    Natural variantiVAR_077216189N → I in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity. 1 PublicationCorresponds to variant dbSNP:rs200908035EnsemblClinVar.1
    Natural variantiVAR_026600189N → K in MMAM; mut-. 1 Publication1
    Natural variantiVAR_004411191A → E in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity. 8 PublicationsCorresponds to variant dbSNP:rs760782399EnsemblClinVar.1
    Natural variantiVAR_026601197A → E in MMAM; mut0. 1 Publication1
    Natural variantiVAR_022400203G → R in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity. 6 PublicationsCorresponds to variant dbSNP:rs778702777EnsemblClinVar.1
    Natural variantiVAR_077217205Missing in MMAM; mut0. 1 Publication1
    Natural variantiVAR_026602215G → C in MMAM; mut- and mut0. 1 PublicationCorresponds to variant dbSNP:rs121918258EnsemblClinVar.1
    Natural variantiVAR_022401215G → S in MMAM; mut0. 3 PublicationsCorresponds to variant dbSNP:rs121918258EnsemblClinVar.1
    Natural variantiVAR_022402218Q → H in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability. 4 PublicationsCorresponds to variant dbSNP:rs1446389693Ensembl.1
    Natural variantiVAR_022403219N → Y in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity. 8 PublicationsCorresponds to variant dbSNP:rs121918256EnsemblClinVar.1
    Natural variantiVAR_080033228 – 750Missing in MMAM; mut0. 1 PublicationAdd BLAST523
    Natural variantiVAR_004412228R → Q in MMAM; mut0. 2 PublicationsCorresponds to variant dbSNP:rs770810987Ensembl.1
    Natural variantiVAR_026603230T → I in MMAM; mut-. 1 Publication1
    Natural variantiVAR_077218230T → R in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity. 1 PublicationCorresponds to variant dbSNP:rs879253833EnsemblClinVar.1
    Natural variantiVAR_004413231Y → N in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; strong decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability. 5 PublicationsCorresponds to variant dbSNP:rs864309736EnsemblClinVar.1
    Natural variantiVAR_022404262S → N in MMAM; mut0. 2 Publications1
    Natural variantiVAR_026604265H → Y in MMAM; mut-. 1 Publication1
    Natural variantiVAR_077219276E → D in MMAM; mut-; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs12175488EnsemblClinVar.1
    Natural variantiVAR_026605281L → S in MMAM; mut0. 1 PublicationCorresponds to variant dbSNP:rs796052007EnsemblClinVar.1
    Natural variantiVAR_077220284G → E in MMAM; mut0. 1 PublicationCorresponds to variant dbSNP:rs879253835EnsemblClinVar.1
    Natural variantiVAR_077221284G → R in MMAM; mut0. 1 PublicationCorresponds to variant dbSNP:rs761477436EnsemblClinVar.1
    Natural variantiVAR_075383288S → P in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity. 2 PublicationsCorresponds to variant dbSNP:rs1179778233Ensembl.1
    Natural variantiVAR_026606291G → E in MMAM; mut0. 1 Publication1
    Natural variantiVAR_022405293Q → P in MMAM; mut0. 1 Publication1
    Natural variantiVAR_026607305L → S in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity. 3 Publications1
    Natural variantiVAR_026608306S → F in MMAM; mut0. 1 Publication1
    Natural variantiVAR_078345309W → G in MMAM; decreased protein expression. 1 Publication1
    Natural variantiVAR_004414312G → V in MMAM; mut0. 2 PublicationsCorresponds to variant dbSNP:rs864309734EnsemblClinVar.1
    Natural variantiVAR_026609316Y → C in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; no decreased affinity for adenosylcob(III)alamin. 2 PublicationsCorresponds to variant dbSNP:rs781474200Ensembl.1
    Natural variantiVAR_023474324A → T in MMAM; mut-. 3 PublicationsCorresponds to variant dbSNP:rs780387525EnsemblClinVar.1
    Natural variantiVAR_077222325G → D in MMAM. 1 PublicationCorresponds to variant dbSNP:rs879253837EnsemblClinVar.1
    Natural variantiVAR_077223326R → K in MMAM; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs758577372EnsemblClinVar.1
    Natural variantiVAR_022406328L → F in MMAM; mut0; affects proper folding; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity. 4 PublicationsCorresponds to variant dbSNP:rs796052002EnsemblClinVar.1
    Natural variantiVAR_023475328L → P in MMAM; mut0. 2 PublicationsCorresponds to variant dbSNP:rs965316043EnsemblClinVar.1
    Natural variantiVAR_075384344S → F in MMAM; mut-; affects proper folding; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin. 2 Publications1
    Natural variantiVAR_004415346Missing in MMAM; mut0. 2 Publications1
    Natural variantiVAR_026610347L → R in MMAM; mut0. 1 Publication1
    Natural variantiVAR_026611350H → Y in MMAM; mut0. 1 PublicationCorresponds to variant dbSNP:rs1407914109Ensembl.1
    Natural variantiVAR_077224358L → P in MMAM; mut0. 1 Publication1
    Natural variantiVAR_075385364Y → S in MMAM. 1 PublicationCorresponds to variant dbSNP:rs563776413Ensembl.1
    Natural variantiVAR_075386366N → S in MMAM; mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability. 2 PublicationsCorresponds to variant dbSNP:rs864309737EnsemblClinVar.1
    Natural variantiVAR_004416368V → D in MMAM. 1
    Natural variantiVAR_026612369R → C in MMAM; mut0. 2 PublicationsCorresponds to variant dbSNP:rs772552898EnsemblClinVar.1
    Natural variantiVAR_004417369R → H in MMAM; mut- and mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability. 4 PublicationsCorresponds to variant dbSNP:rs564069299EnsemblClinVar.1
    Natural variantiVAR_026613370T → P in MMAM; mut0. 1 PublicationCorresponds to variant dbSNP:rs368790885EnsemblClinVar.1
    Natural variantiVAR_004418377A → E in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity. 3 PublicationsCorresponds to variant dbSNP:rs121918250EnsemblClinVar.1
    Natural variantiVAR_026614383Q → H in MMAM; mut0. 1 Publication1
    Natural variantiVAR_026615383Q → P in MMAM; mut0. 1 Publication1
    Natural variantiVAR_026616386H → N in MMAM; mut0. 1 Publication1
    Natural variantiVAR_077225386H → R in MMAM; mut0. 1 PublicationCorresponds to variant dbSNP:rs866933356Ensembl.1
    Natural variantiVAR_075387387T → I in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability. 3 Publications1
    Natural variantiVAR_026617388N → H in MMAM; mut0. 1 PublicationCorresponds to variant dbSNP:rs766010704Ensembl.1
    Natural variantiVAR_077226388N → K in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity. 1 PublicationCorresponds to variant dbSNP:rs879253840EnsemblClinVar.1
    Natural variantiVAR_026618389Missing in MMAM; mut0. 1 Publication1
    Natural variantiVAR_026619412Missing in MMAM; mut0. 1 Publication1
    Natural variantiVAR_077227424P → L in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity. 1 PublicationCorresponds to variant dbSNP:rs879253842EnsemblClinVar.1
    Natural variantiVAR_077228426G → E in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity. 1 PublicationCorresponds to variant dbSNP:rs533755473EnsemblClinVar.1
    Natural variantiVAR_026620426G → R in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; strong decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability. 2 PublicationsCorresponds to variant dbSNP:rs769922244Ensembl.1
    Natural variantiVAR_026621427G → D in MMAM; mut0. 1 PublicationCorresponds to variant dbSNP:rs753288303EnsemblClinVar.1
    Natural variantiVAR_075388454G → E in MMAM; mut0. 2 Publications1
    Natural variantiVAR_078346505I → T in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity. 1 Publication1
    Natural variantiVAR_075389514Q → E in MMAM; unknown pathological significance. 1 Publication1
    Natural variantiVAR_078347514Q → K in MMAM; decreased protein expression. 1 Publication1
    Natural variantiVAR_026622518L → P in MMAM; mut0. 1 PublicationCorresponds to variant dbSNP:rs864309738EnsemblClinVar.1
    Natural variantiVAR_022408535A → P in MMAM; mut0. 1 PublicationCorresponds to variant dbSNP:rs760183775Ensembl.1
    Natural variantiVAR_077229552A → V in MMAM; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs879253845EnsemblClinVar.1
    Natural variantiVAR_026623560C → Y in MMAM; mut0. 1 PublicationCorresponds to variant dbSNP:rs1238333040Ensembl.1
    Natural variantiVAR_026624566T → R in MMAM; mut0. 1 Publication1
    Natural variantiVAR_026625573F → S in MMAM; mut-; affects proper folding; no effect on protein abundance; no effect on methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; does not alter thermodynamic stability. 2 PublicationsCorresponds to variant dbSNP:rs775593146EnsemblClinVar.1
    Natural variantiVAR_022409587Y → C in MMAM; mut-. 1 Publication1
    Natural variantiVAR_078348597I → R in MMAM; no changed in protein expression; decreased methylmalonyl-CoA mutase activity. 1 Publication1
    Natural variantiVAR_075390615P → L in MMAM; mut0; affects proper folding; reduced strongly protein level. 3 Publications1
    Natural variantiVAR_026626615P → R in MMAM; mut0. 1 Publication1
    Natural variantiVAR_022410615P → T in MMAM; mut0; affects proper folding; reduced strongly protein level; loss of methylmalonyl-CoA mutase activity. 5 PublicationsCorresponds to variant dbSNP:rs1302409621Ensembl.1
    Natural variantiVAR_023476616R → C in MMAM; mut0. 3 PublicationsCorresponds to variant dbSNP:rs765284825EnsemblClinVar.1
    Natural variantiVAR_023477617L → R in MMAM; mut0. 2 Publications1
    Natural variantiVAR_077230618L → P in MMAM. 1 PublicationCorresponds to variant dbSNP:rs879253846EnsemblClinVar.1
    Natural variantiVAR_022411621K → N in MMAM; mut0. 1 Publication1
    Natural variantiVAR_004420623G → R in MMAM; mut0. 4 PublicationsCorresponds to variant dbSNP:rs121918254EnsemblClinVar.1
    Natural variantiVAR_022412624Q → R in MMAM; no effect on protein abundance. 2 PublicationsCorresponds to variant dbSNP:rs768521956Ensembl.1
    Natural variantiVAR_077231625D → G in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity. 1 PublicationCorresponds to variant dbSNP:rs879253847EnsemblClinVar.1
    Natural variantiVAR_075391625D → V in MMAM; mut0; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity. 2 Publications1
    Natural variantiVAR_004421626G → C in MMAM; mut-. 1 PublicationCorresponds to variant dbSNP:rs982110849Ensembl.1
    Natural variantiVAR_022413627H → R in MMAM; mut0. 2 PublicationsCorresponds to variant dbSNP:rs372486357EnsemblClinVar.1
    Natural variantiVAR_004422630G → E in MMAM; mut0. 3 PublicationsCorresponds to variant dbSNP:rs143023066EnsemblClinVar.1
    Natural variantiVAR_004423633V → G in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; does not alter thermodynamic stability. 4 PublicationsCorresponds to variant dbSNP:rs200055428EnsemblClinVar.1
    Natural variantiVAR_022414637G → E in MMAM; mut-. 1 Publication1
    Natural variantiVAR_026627637G → R in MMAM; mut0. 1 PublicationCorresponds to variant dbSNP:rs781501004Ensembl.1
    Natural variantiVAR_022415638F → I in MMAM; mut0. 1 Publication1
    Natural variantiVAR_022416640D → Y in MMAM; mut0. 1 PublicationCorresponds to variant dbSNP:rs865815395Ensembl.1
    Natural variantiVAR_022417642G → R in MMAM; mut-. 2 PublicationsCorresponds to variant dbSNP:rs747897332EnsemblClinVar.1
    Natural variantiVAR_004424648G → D in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; strong decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability. 2 PublicationsCorresponds to variant dbSNP:rs766721811Ensembl.1
    Natural variantiVAR_004425669V → E in MMAM; mut0. Corresponds to variant dbSNP:rs1360470463Ensembl.1
    Natural variantiVAR_075392674L → F in MMAM; decreased protein abundance; decreased methylmalonyl-CoA mutase activity. 2 PublicationsCorresponds to variant dbSNP:rs1164271240Ensembl.1
    Natural variantiVAR_004427678H → R in MMAM; mut-. 2 PublicationsCorresponds to variant dbSNP:rs147094927Ensembl.1
    Natural variantiVAR_004428684E → EL in MMAM; mut-. 1 Publication1
    Natural variantiVAR_004429685L → R in MMAM; mut-. 2 PublicationsCorresponds to variant dbSNP:rs864309739EnsemblClinVar.1
    Natural variantiVAR_075393692L → P in MMAM. 1 Publication1
    Natural variantiVAR_075394694R → L in MMAM; mut-; decreased protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability. 3 Publications1
    Natural variantiVAR_004430694R → W in MMAM; mut- and mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability. 8 PublicationsCorresponds to variant dbSNP:rs777758903EnsemblClinVar.1
    Natural variantiVAR_022418700M → K in MMAM; mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability. 4 PublicationsCorresponds to variant dbSNP:rs140600746EnsemblClinVar.1
    Natural variantiVAR_004431703G → R in MMAM; mut0. 2 PublicationsCorresponds to variant dbSNP:rs121918255EnsemblClinVar.1
    Natural variantiVAR_004432717G → V in MMAM; mut-; no effect on protein abundance; interfers with the binding of the cofactor to the apoenzyme; decreased methylmalonyl-CoA mutase activity; strong decreased affinity for adenosylcob(III)alamin; decreased thermodynamic stability. 6 PublicationsCorresponds to variant dbSNP:rs121918252EnsemblClinVar.1
    Natural variantiVAR_078349723G → D in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity. 1 PublicationCorresponds to variant dbSNP:rs755077681Ensembl.1
    Natural variantiVAR_077232736L → F in MMAM. 1 PublicationCorresponds to variant dbSNP:rs753461919EnsemblClinVar.1

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    4594

    GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

    More...
    GeneReviewsi
    MUT

    MalaCards human disease database

    More...
    MalaCardsi
    MUT
    MIMi251000 phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000146085

    Orphanet; a database dedicated to information on rare diseases and orphan drugs

    More...
    Orphaneti
    79312 Vitamin B12-unresponsive methylmalonic acidemia type mut-
    289916 Vitamin B12-unresponsive methylmalonic acidemia type mut0

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA31327

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB00115 Cyanocobalamin
    DB00200 Hydroxocobalamin

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    MUT

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    317373575

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 32MitochondrionAdd BLAST32
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001929333 – 750Methylmalonyl-CoA mutase, mitochondrialAdd BLAST718

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei89N6-acetyllysineBy similarity1
    Modified residuei212N6-acetyllysineBy similarity1
    Modified residuei335N6-acetyllysineBy similarity1
    Modified residuei343N6-succinyllysineBy similarity1
    Modified residuei481PhosphoserineCombined sources1
    Modified residuei595N6-succinyllysineBy similarity1
    Modified residuei602N6-acetyllysineBy similarity1

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P22033

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P22033

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P22033

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P22033

    PeptideAtlas

    More...
    PeptideAtlasi
    P22033

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P22033

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    53953

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P22033

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    P22033

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000146085 Expressed in 232 organ(s), highest expression level in liver

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_MUT

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P22033 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P22033 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    HPA035971
    HPA035972

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer (PubMed:20876572). Interacts (the apoenzyme form) with MMAA; the interaction is GTP dependent (PubMed:20876572).1 Publication

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    110680, 14 interactors

    CORUM comprehensive resource of mammalian protein complexes

    More...
    CORUMi
    P22033

    Protein interaction database and analysis system

    More...
    IntActi
    P22033, 5 interactors

    Molecular INTeraction database

    More...
    MINTi
    P22033

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000274813

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1750
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2XIJX-ray1.95A12-750[»]
    2XIQX-ray1.95A/B12-750[»]
    3BICX-ray2.60A/B12-750[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P22033

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P22033

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P22033

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini614 – 746B12-bindingPROSITE-ProRule annotationAdd BLAST133

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni96 – 99malonyl-CoA binding1 Publication4
    Regioni106 – 110malonyl-CoA binding1 Publication5
    Regioni216 – 218malonyl-CoA binding1 Publication3
    Regioni304 – 306malonyl-CoA binding1 Publication3

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the methylmalonyl-CoA mutase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG410IE7I Eukaryota
    COG1884 LUCA
    COG2185 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00390000011892

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000003917

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG006423

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P22033

    KEGG Orthology (KO)

    More...
    KOi
    K01847

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    DRMSVSM

    Database of Orthologous Groups

    More...
    OrthoDBi
    347581at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P22033

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF313557

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR006159 Acid_CoA_mut_C
    IPR016176 Cbl-dep_enz_cat
    IPR006158 Cobalamin-bd
    IPR036724 Cobalamin-bd_sf
    IPR006099 MeMalonylCoA_mutase_a/b_cat
    IPR006098 MMCoA_mutase_a_cat

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02310 B12-binding, 1 hit
    PF01642 MM_CoA_mutase, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51703 SSF51703, 1 hit
    SSF52242 SSF52242, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00640 acid_CoA_mut_C, 1 hit
    TIGR00641 acid_CoA_mut_N, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51332 B12_BINDING, 1 hit
    PS00544 METMALONYL_COA_MUTASE, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P22033-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MLRAKNQLFL LSPHYLRQVK ESSGSRLIQQ RLLHQQQPLH PEWAALAKKQ
    60 70 80 90 100
    LKGKNPEDLI WHTPEGISIK PLYSKRDTMD LPEELPGVKP FTRGPYPTMY
    110 120 130 140 150
    TFRPWTIRQY AGFSTVEESN KFYKDNIKAG QQGLSVAFDL ATHRGYDSDN
    160 170 180 190 200
    PRVRGDVGMA GVAIDTVEDT KILFDGIPLE KMSVSMTMNG AVIPVLANFI
    210 220 230 240 250
    VTGEEQGVPK EKLTGTIQND ILKEFMVRNT YIFPPEPSMK IIADIFEYTA
    260 270 280 290 300
    KHMPKFNSIS ISGYHMQEAG ADAILELAYT LADGLEYSRT GLQAGLTIDE
    310 320 330 340 350
    FAPRLSFFWG IGMNFYMEIA KMRAGRRLWA HLIEKMFQPK NSKSLLLRAH
    360 370 380 390 400
    CQTSGWSLTE QDPYNNIVRT AIEAMAAVFG GTQSLHTNSF DEALGLPTVK
    410 420 430 440 450
    SARIARNTQI IIQEESGIPK VADPWGGSYM MECLTNDVYD AALKLINEIE
    460 470 480 490 500
    EMGGMAKAVA EGIPKLRIEE CAARRQARID SGSEVIVGVN KYQLEKEDAV
    510 520 530 540 550
    EVLAIDNTSV RNRQIEKLKK IKSSRDQALA ERCLAALTEC AASGDGNILA
    560 570 580 590 600
    LAVDASRARC TVGEITDALK KVFGEHKAND RMVSGAYRQE FGESKEITSA
    610 620 630 640 650
    IKRVHKFMER EGRRPRLLVA KMGQDGHDRG AKVIATGFAD LGFDVDIGPL
    660 670 680 690 700
    FQTPREVAQQ AVDADVHAVG ISTLAAGHKT LVPELIKELN SLGRPDILVM
    710 720 730 740 750
    CGGVIPPQDY EFLFEVGVSN VFGPGTRIPK AAVQVLDDIE KCLEKKQQSV
    Length:750
    Mass (Da):83,134
    Last modified:January 11, 2011 - v4
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB5909729C08B562F
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti153V → L in AAA99226 (PubMed:1980486).Curated1
    Sequence conflicti236E → D in AAA99226 (PubMed:1980486).Curated1
    Sequence conflicti274 – 277ILEL → FWSW in AAA99226 (PubMed:1980486).Curated4
    Sequence conflicti316Y → H in AAA99226 (PubMed:1980486).Curated1
    Sequence conflicti516E → G in AAA99226 (PubMed:1980486).Curated1
    Sequence conflicti591F → Y in AAA99226 (PubMed:1980486).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_0800317 – 750Missing in MMAM; mut-. 1 PublicationAdd BLAST744
    Natural variantiVAR_02347269I → V in MMAM; mut0. 3 PublicationsCorresponds to variant dbSNP:rs115923556EnsemblClinVar.1
    Natural variantiVAR_02659286P → L in MMAM; mut0 and mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability. 2 PublicationsCorresponds to variant dbSNP:rs769348060EnsemblClinVar.1
    Natural variantiVAR_02659387G → E in MMAM; mut0. 1 Publication1
    Natural variantiVAR_00440993R → H in MMAM; mut0; decreased methylmalonyl-CoA mutase activity. 4 PublicationsCorresponds to variant dbSNP:rs121918251EnsemblClinVar.1
    Natural variantiVAR_02659494G → R in MMAM; mut0. 1 PublicationCorresponds to variant dbSNP:rs727504022EnsemblClinVar.1
    Natural variantiVAR_02239394G → V in MMAM; mut- and mut0. 2 PublicationsCorresponds to variant dbSNP:rs535411418Ensembl.1
    Natural variantiVAR_02659595P → R in MMAM; mut0. 1 PublicationCorresponds to variant dbSNP:rs190834116EnsemblClinVar.1
    Natural variantiVAR_075379100Y → C in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability. 2 Publications