ACADM
entrez
34
canonical
uniprot
P11310
canonical
ensembl
ENSG00000117054
resolver
ensp
ENSP00000359871
resolver
ensp
ENSP00000359878
resolver
ensp
ENSP00000409612
resolver
ensp
ENSP00000506598
resolver
ensp
ENSP00000679097
resolver
enst
ENST00000370834
resolver
genesymbol
ACADM
resolver
hgnc
HGNC:89
resolver
uniprot
A0A0S2Z366
resolver
uniprot
B4DJE7
resolver
uniprot
B7Z9I1
resolver
uniprot
Q5T4U4
resolver
uniprot
Q5T4U5
resolver
uniprot
Q9NYF1
resolver
uniprot_entry
A0A0S2Z366_HUMAN
resolver
uniprot_entry
ACADM_HUMAN
resolver
uniprot_entry
B4DJE7_HUMAN
resolver
uniprot_entry
B7Z9I1_HUMAN
resolver
uniprot_entry
Q5T4U5_HUMAN
resolver
uniprot_sec
Q5T4U4
resolver
uniprot_sec
Q9NYF1
resolver
amino_acid_sequence
MAAGFGRCCRVLRSISRFHWRSQHTKANRQREPGLGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDKYKN
uniprot
proteins
disease_involvement
DISEASE: Acyl-CoA dehydrogenase medium-chain deficiency (ACADMD) [MIM:201450]: An inborn error of mitochondrial fatty acid beta-oxidation which causes fasting hypoglycemia, hepatic dysfunction and encephalopathy, often resulting in death in infancy. {ECO:0000269|PubMed:10767181, ECO:0000269|PubMed:11349232, ECO:0000269|PubMed:11409868, ECO:0000269|PubMed:11486912, ECO:0000269|PubMed:1363805, ECO:0000269|PubMed:1671131, ECO:0000269|PubMed:1684086, ECO:0000269|PubMed:1902818, ECO:0000269|PubMed:2251268, ECO:0000269|PubMed:2393404, ECO:0000269|PubMed:2394825, ECO:0000269|PubMed:7603790, ECO:0000269|PubMed:7929823, ECO:0000269|PubMed:8198141, ECO:0000269|PubMed:9158144, ECO:0000269|PubMed:9882619}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
1.3.8.7
uniprot
proteins
function
FUNCTION: Medium-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation (FAO), breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats (PubMed:1970566, PubMed:21237683, PubMed:2251268, PubMed:8823175). The first step of FAO consists in the proR-proR stereospecific alpha, beta-dehydrogenation of fatty acyl-CoA thioesters using the electron transfer flavoprotein (ETF) as their physiologic electron acceptor, resulting in the formation of trans-2-enoyl-CoA ((2E)-enoyl-CoA) (PubMed:2251268). ETF is the electron acceptor that transfers electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (PubMed:15159392, PubMed:25416781). Among the different mitochondrial acyl-CoA dehydrogenases, medium-chain specific acyl-CoA dehydrogenase has preference for fatty acyl-CoAs with saturated 6 to 12 carbons long primary chains, making it but can also catalyze longer chains such as C14 and C16 (PubMed:1970566, PubMed:21237683, PubMed:2251268, PubMed:8823175). {ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:1970566, ECO:0000269|PubMed:21237683, ECO:0000269|PubMed:2251268, ECO:0000269|PubMed:25416781, ECO:0000269|PubMed:8823175}.
uniprot
proteins
mass_dalton
46588
uniprot
proteins
mutagenesis
MUTAGEN 86; /note="L->M: Strongly reduced rate of electron transfer to ETF."; /evidence="ECO:0000269|PubMed:15159392"; MUTAGEN 98; /note="L->W: Strongly reduced rate of electron transfer to ETF."; /evidence="ECO:0000269|PubMed:15159392"; MUTAGEN 100; /note="L->Y: Strongly reduced rate of electron transfer to ETF."; /evidence="ECO:0000269|PubMed:15159392"; MUTAGEN 108; /note="I->M: Strongly reduced rate of electron transfer to ETF."; /evidence="ECO:0000269|PubMed:15159392"; MUTAGEN 191; /note="W->A: Loss of electron transfer to ETF."; /evidence="ECO:0000269|PubMed:15975918"; MUTAGEN 191; /note="W->F: Reduces rate of electron transfer to ETF about six-fold."; /evidence="ECO:0000269|PubMed:15975918"; MUTAGEN 237; /note="E->A: Strongly reduced rate of electron transfer to ETF."; /evidence="ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918"; MUTAGEN 280; /note="T->E: Narrower substrate specificity. Changed substrate specificity towards longer acyl chains; when associated with G-401. Loss of acyl-CoA dehydrogenase activity; when associated with T-410."; /evidence="ECO:0000269|PubMed:8823175"; MUTAGEN 384; /note="E->A: Reduces rate of electron transfer to ETF three-fold."; /evidence="ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918"; MUTAGEN 384; /note="E->Q: Reduces rate of electron transfer to ETF two-fold."; /evidence="ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918"; MUTAGEN 401; /note="E->G: Changed substrate specificity towards longer acyl chains; when associated with E-280."; /evidence="ECO:0000269|PubMed:8823175"; MUTAGEN 401; /note="E->Q: Loss of acyl-CoA dehydrogenase activity."; /evidence="ECO:0000269|PubMed:1970566"; MUTAGEN 401; /note="E->T: Loss of acyl-CoA dehydrogenase activity; when associated with E-280."; /evidence="ECO:0000269|PubMed:8823175
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation. {ECO:0000269|PubMed:2251268}.
uniprot
proteins
post_translational_modification
PTM: Acetylated. Could occur at proximity of the cofactor-binding sites and reduce the catalytic activity. Could be deacetylated by SIRT3. {ECO:0000269|PubMed:24121500}.
uniprot
proteins
protein_family
Acyl-CoA dehydrogenase family
uniprot
proteins
pubmed
10767181
uniprot
proteins
pubmed
11349232
uniprot
proteins
pubmed
11409868
uniprot
proteins
pubmed
11486912
uniprot
proteins
pubmed
1363805
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15159392
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15975918
uniprot
proteins
pubmed
16020546
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
1671131
uniprot
proteins
pubmed
1684086
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
1731887
uniprot
proteins
pubmed
17564966
uniprot
proteins
pubmed
1902818
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
1970566
uniprot
proteins
pubmed
21237683
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
2251268
uniprot
proteins
pubmed
2393404
uniprot
proteins
pubmed
2394825
uniprot
proteins
pubmed
24121500
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25416781
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
3035565
uniprot
proteins
pubmed
7603790
uniprot
proteins
pubmed
7929823
uniprot
proteins
pubmed
8198141
uniprot
proteins
pubmed
8823175
uniprot
proteins
pubmed
8823176
uniprot
proteins
pubmed
9158144
uniprot
proteins
pubmed
9882619
uniprot
proteins
sequence_length
421
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:16020546}.
uniprot
proteins