MMUT

Protein identityUniProt · HPA

UniProt accession

P22033

Gene

MMUT

Ensembl

ENSG00000146085

Chromosome

6

Canonical length

750 aa

Protein class

Disease related genes, Enzymes, FDA approved drug targets, Human disease related genes, Metabolic proteins, Plasma proteins, Predicted intracellular proteins

Subcellular location

Mitochondria,Cytosol

Quaternary structure

Homodimer

OverviewNCBI Gene

This gene encodes the mitochondrial enzyme methylmalonyl Coenzyme A mutase. In humans, the product of this gene is a vitamin B12-dependent enzyme which catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA, while in other species this enzyme may have different functions. Mutations in this gene may lead to various types of methylmalonic aciduria. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

750 residues, UniProt reviewed canonical sequence.

>P22033|MMUT
     1  MLRAKNQLFL LSPHYLRQVK ESSGSRLIQQ RLLHQQQPLH PEWAALAKKQ LKGKNPEDLI
    61  WHTPEGISIK PLYSKRDTMD LPEELPGVKP FTRGPYPTMY TFRPWTIRQY AGFSTVEESN
   121  KFYKDNIKAG QQGLSVAFDL ATHRGYDSDN PRVRGDVGMA GVAIDTVEDT KILFDGIPLE
   181  KMSVSMTMNG AVIPVLANFI VTGEEQGVPK EKLTGTIQND ILKEFMVRNT YIFPPEPSMK
   241  IIADIFEYTA KHMPKFNSIS ISGYHMQEAG ADAILELAYT LADGLEYSRT GLQAGLTIDE
   301  FAPRLSFFWG IGMNFYMEIA KMRAGRRLWA HLIEKMFQPK NSKSLLLRAH CQTSGWSLTE
   361  QDPYNNIVRT AIEAMAAVFG GTQSLHTNSF DEALGLPTVK SARIARNTQI IIQEESGIPK
   421  VADPWGGSYM MECLTNDVYD AALKLINEIE EMGGMAKAVA EGIPKLRIEE CAARRQARID
   481  SGSEVIVGVN KYQLEKEDAV EVLAIDNTSV RNRQIEKLKK IKSSRDQALA ERCLAALTEC
   541  AASGDGNILA LAVDASRARC TVGEITDALK KVFGEHKAND RMVSGAYRQE FGESKEITSA
   601  IKRVHKFMER EGRRPRLLVA KMGQDGHDRG AKVIATGFAD LGFDVDIGPL FQTPREVAQQ
   661  AVDADVHAVG ISTLAAGHKT LVPELIKELN SLGRPDILVM CGGVIPPQDY EFLFEVGVSN
   721  VFGPGTRIPK AAVQVLDDIE KCLEKKQQSV

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against MMUT can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Intracellular

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.23

Highest tissue expression

186 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about MMUT.

Disease | AllUniProt

Conditions MMUT is implicated in, by any mechanism.

• Methylmalonic aciduria due to methylmalonyl-CoA mutase deficiency (MAMM) MIM:251000

Disease | GeneticClinVar

412 pathogenic / likely-pathogenic of 1,234 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Methylmalonic aciduria due to methylmalonyl-CoA mutase deficiency
• Methylmalonic aciduria due to complete methylmalonyl-CoA mutase deficiency
• Methylmalonic acidemia
• METHYLMALONIC ACIDURIA, mut(0) TYPE
• MMUT-related disorder

Disease | ImmuneIEDB

Conditions an epitope on MMUT was assayed in.

• berylliosis T cell

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

1.23

gnomAD pLI

0

DepMap mean gene effect

-0.07

DepMap dependency class

selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 7% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• homocysteine metabolic process
• positive regulation of GTPase activity
• post-embryonic development
• succinyl-CoA biosynthetic process
• propionate metabolic process, methylmalonyl pathway

Molecular functions

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

Cellular components

• cytoplasm
• mitochondrial matrix
• mitochondrion

Protein domainsUniProt · Pfam · InterPro

• Cobalamin (vitamin B12)-binding domain
• Cobalamin-binding domain superfamily
• B12 binding domain
• Methylmalonyl-CoA mutase, alpha chain, catalytic
• Methylmalonyl-CoA mutase, alpha/beta chain, catalytic
• Methylmalonyl-CoA mutase, C-terminal
• Cobalamin (vitamin B12)-dependent enzyme, catalytic
• Methylmalonyl-CoA mutase, alpha/beta chain, conserved site
• Methylmalonyl-CoA mutase

KeywordsUniProt

• Acetylation
• Cobalamin
• Cobalt
• Cytoplasm
• Isomerase
• Metal-binding
• Mitochondrion
• Phosphoprotein
• Transit peptide

InteractionsUniProt · HPA

Protein binding partners of MMUT in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• MMAA