MUT
entrez
4594
canonical
uniprot
P22033
canonical
ensembl
ENSG00000146085
resolver
ensp
ENSP00000274813
resolver
ensp
ENSP00000548119
resolver
ensp
ENSP00000548121
resolver
ensp
ENSP00000548123
resolver
ensp
ENSP00000548124
resolver
ensp
ENSP00000548126
resolver
ensp
ENSP00000548127
resolver
ensp
ENSP00000548129
resolver
ensp
ENSP00000548132
resolver
ensp
ENSP00000623813
resolver
ensp
ENSP00000623814
resolver
ensp
ENSP00000623816
resolver
ensp
ENSP00000623817
resolver
enst
ENST00000274813
resolver
enst
ENST00000878060
resolver
enst
ENST00000878062
resolver
enst
ENST00000878064
resolver
enst
ENST00000878065
resolver
enst
ENST00000878067
resolver
enst
ENST00000878068
resolver
enst
ENST00000878070
resolver
enst
ENST00000878073
resolver
enst
ENST00000953754
resolver
enst
ENST00000953755
resolver
enst
ENST00000953757
resolver
enst
ENST00000953758
resolver
genesymbol
MMUT
resolver
genesymbol
MUT
resolver
genesymbol_syn
MUT
resolver
hgnc
HGNC:7526
resolver
uniprot
A0A024RD82
resolver
uniprot
A8K953
resolver
uniprot
B2R6K1
resolver
uniprot
Q5SYZ3
resolver
uniprot
Q96B11
resolver
uniprot
Q9UD64
resolver
uniprot_entry
A0A024RD82_HUMAN
resolver
uniprot_entry
B2R6K1_HUMAN
resolver
uniprot_entry
MUTA_HUMAN
resolver
uniprot_sec
A8K953
resolver
uniprot_sec
Q5SYZ3
resolver
uniprot_sec
Q96B11
resolver
uniprot_sec
Q9UD64
resolver
activity_regulation
ACTIVITY REGULATION: During catalysis, accumulation of oxidized inactive cofactor hydroxocobalamin (OH2Cbl) leads to loss of MMUT activity (PubMed:21138732, PubMed:28943303). Interaction with MMAA decreases the rate of OH2Cbl formation and promotes the replacement of OH2Cbl by the active cofactor adenosylcobalamin (AdoCbl), thereby restoring MMUT activity (PubMed:21138732, PubMed:28943303). Inhibited by itaconyl-CoA, a metabolite that inactivates the coenzyme B12 cofactor (PubMed:29056341). Inhibited by malyl-coA (PubMed:40108300). Inhibited at high concentration of substrate (PubMed:28943303). {ECO:0000269|PubMed:28943303, ECO:0000269|PubMed:29056341}.
uniprot
proteins
amino_acid_sequence
MLRAKNQLFLLSPHYLRQVKESSGSRLIQQRLLHQQQPLHPEWAALAKKQLKGKNPEDLIWHTPEGISIKPLYSKRDTMDLPEELPGVKPFTRGPYPTMYTFRPWTIRQYAGFSTVEESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPVLANFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAILELAYTLADGLEYSRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKMFQPKNSKSLLLRAHCQTSGWSLTEQDPYNNIVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLTNDVYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKYQLEKEDAVEVLAIDNTSVRNRQIEKLKKIKSSRDQALAERCLAALTECAASGDGNILALAVDASRARCTVGEITDALKKVFGEHKANDRMVSGAYRQEFGESKEITSAIKRVHKFMEREGRRPRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGISTLAAGHKTLVPELIKELNSLGRPDILVMCGGVIPPQDYEFLFEVGVSNVFGPGTRIPKAAVQVLDDIEKCLEKKQQSV
uniprot
proteins
disease_involvement
DISEASE: Methylmalonic aciduria due to methylmalonyl-CoA mutase deficiency (MAMM) [MIM:251000]: An 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. MAMM is unresponsive to vitamin B12 therapy. {ECO:0000269|PubMed:10923046, ECO:0000269|PubMed:11350191, ECO:0000269|PubMed:1346616, ECO:0000269|PubMed:1351030, ECO:0000269|PubMed:15643616, ECO:0000269|PubMed:15781192, ECO:0000269|PubMed:16281286, ECO:0000269|PubMed:1670635, ECO:0000269|PubMed:17113806, ECO:0000269|PubMed:17957493, ECO:0000269|PubMed:19588269, ECO:0000269|PubMed:1977311, ECO:0000269|PubMed:1980486, ECO:0000269|PubMed:22727635, ECO:0000269|PubMed:25125334, ECO:0000269|PubMed:26615597, ECO:0000269|PubMed:27167370, ECO:0000269|PubMed:28101778, ECO:0000269|PubMed:7909321, ECO:0000269|PubMed:7912889, ECO:0000269|PubMed:8990001, ECO:0000269|PubMed:9285782, ECO:0000269|PubMed:9452100, ECO:0000269|PubMed:9554742}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
5.4.99.2
uniprot
proteins
function
FUNCTION: Catalyzes the reversible isomerization of methylmalonyl-CoA (MMCoA) (generated from branched-chain amino acid metabolism and degradation of dietary odd chain fatty acids and cholesterol) to succinyl-CoA (3-carboxypropionyl-CoA), a key intermediate of the tricarboxylic acid cycle. {ECO:0000269|PubMed:1346616, ECO:0000269|PubMed:1978672, ECO:0000269|PubMed:21138732, ECO:0000269|PubMed:24458, ECO:0000269|PubMed:2453061, ECO:0000269|PubMed:25125334, ECO:0000269|PubMed:27167370, ECO:0000269|PubMed:28101778, ECO:0000269|PubMed:28943303, ECO:0000269|PubMed:29056341}.
uniprot
proteins
mass_dalton
83134
uniprot
proteins
protein_family
Methylmalonyl-CoA mutase family
uniprot
proteins
pubmed
10923046
uniprot
proteins
pubmed
11350191
uniprot
proteins
pubmed
1346616
uniprot
proteins
pubmed
1351030
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15643616
uniprot
proteins
pubmed
15781192
uniprot
proteins
pubmed
16281286
uniprot
proteins
pubmed
1670635
uniprot
proteins
pubmed
17113806
uniprot
proteins
pubmed
17957493
uniprot
proteins
pubmed
19588269
uniprot
proteins
pubmed
1977311
uniprot
proteins
pubmed
1978672
uniprot
proteins
pubmed
1980486
uniprot
proteins
pubmed
20876572
uniprot
proteins
pubmed
21138732
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22727635
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24458
uniprot
proteins
pubmed
2453061
uniprot
proteins
pubmed
25125334
uniprot
proteins
pubmed
2567699
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26615597
uniprot
proteins
pubmed
27167370
uniprot
proteins
pubmed
28101778
uniprot
proteins
pubmed
28943303
uniprot
proteins
pubmed
29056341
uniprot
proteins
pubmed
40108300
uniprot
proteins
pubmed
7909321
uniprot
proteins
pubmed
7912889
uniprot
proteins
pubmed
8990001
uniprot
proteins
pubmed
9285782
uniprot
proteins
pubmed
9452100
uniprot
proteins
pubmed
9554742
uniprot
proteins
sequence_length
750
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:24458}. Mitochondrion {ECO:0000269|PubMed:28943303}. Cytoplasm {ECO:0000269|PubMed:28943303}.
uniprot
proteins