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Identification
HMDB Protein ID HMDBP00103
Secondary Accession Numbers
  • 5335
  • HMDBP04489
Name Short-chain specific acyl-CoA dehydrogenase, mitochondrial
Synonyms
  1. Butyryl-CoA dehydrogenase
  2. SCAD
Gene Name ACADS
Protein Type Unknown
Biological Properties
General Function Involved in acyl-CoA dehydrogenase activity
Specific Function Not Available
Pathways
  • 2-Methyl-3-Hydroxybutryl CoA Dehydrogenase Deficiency
  • 3-Hydroxy-3-Methylglutaryl-CoA Lyase Deficiency
  • 3-hydroxyisobutyric acid dehydrogenase deficiency
  • 3-hydroxyisobutyric aciduria
  • 3-Methylcrotonyl Coa Carboxylase Deficiency Type I
  • 3-Methylglutaconic Aciduria Type I
  • 3-Methylglutaconic Aciduria Type III
  • 3-Methylglutaconic Aciduria Type IV
  • Beta-Ketothiolase Deficiency
  • Butanoate metabolism
  • Butyrate Metabolism
  • Carnitine palmitoyl transferase deficiency (I)
  • Carnitine palmitoyl transferase deficiency (II)
  • Ethylmalonic Encephalopathy
  • Fatty acid Metabolism
  • fatty acid metabolism
  • Glutaric Aciduria Type I
  • Isobutyryl-coa dehydrogenase deficiency
  • Isovaleric acidemia
  • Isovaleric Aciduria
  • Long chain acyl-CoA dehydrogenase deficiency (LCAD)
  • Maple Syrup Urine Disease
  • Medium chain acyl-coa dehydrogenase deficiency (MCAD)
  • Methylmalonate Semialdehyde Dehydrogenase Deficiency
  • Methylmalonic Aciduria
  • Mitochondrial Beta-Oxidation of Short Chain Saturated Fatty Acids
  • mitochondrial fatty acid beta-oxidation
  • Propionic Acidemia
  • Short Chain Acyl CoA Dehydrogenase Deficiency (SCAD Deficiency)
  • Short-chain 3-hydroxyacyl-CoA dehydrogenase deficiency (SCHAD)
  • Trifunctional protein deficiency
  • Valine, Leucine and Isoleucine Degradation
  • Valine, leucine and isoleucine degradation
  • Very-long-chain acyl coa dehydrogenase deficiency (VLCAD)
Reactions
Butyryl-CoA + electron-transfer flavoprotein → Crotonoyl-CoA + reduced electron-transfer flavoprotein details
Butyryl-CoA + NAD → (E)-but-2-enoyl-CoA + NADH + Hydrogen Ion details
Butyryl-CoA + FAD → FADH + (E)-but-2-enoyl-CoA details
Isobutyryl-CoA + Acceptor → Methacrylyl-CoA + Reduced acceptor details
(S)-2-Methylbutanoyl-CoA + Acceptor → Tiglyl-CoA + Reduced acceptor details
Hexanoyl-CoA + FAD → trans-2-Hexenoyl-CoA + FADH details
GO Classification
Biological Process
response to starvation
response to glucocorticoid stimulus
protein homotetramerization
fatty acid beta-oxidation using acyl-CoA dehydrogenase
butyrate catabolic process
fatty acid beta-oxidation
Cellular Component
mitochondrial matrix
Function
oxidoreductase activity, acting on the ch-ch group of donors
acyl-coa dehydrogenase activity
binding
catalytic activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
oxidoreductase activity
fad or fadh2 binding
Molecular Function
acyl-CoA dehydrogenase activity
flavin adenine dinucleotide binding
fatty-acyl-CoA binding
butyryl-CoA dehydrogenase activity
Process
metabolic process
oxidation reduction
Cellular Location
  1. Mitochondrion matrix
Gene Properties
Chromosome Location 12
Locus 12q24.31
SNPs ACADS
Gene Sequence
>1239 bp
ATGGCCGCCGCGCTGCTCGCCCGGGCCTCGGGCCCTGCCCGCAGAGCTCTCTGTCCTAGG
GCCTGGCGGCAGTTACACACCATCTACCAGTCTGTGGAACTGCCCGAGACACACCAGATG
TTGCTCCAGACATGCCGGGACTTTGCCGAGAAGGAGTTGTTTCCCATTGCAGCCCAGGTG
GATAAGGAACATCTCTTCCCAGCGGCTCAGGTGAAGAAGATGGGCGGGCTTGGGCTTCTG
GCCATGGACGTGCCCGAGGAGCTTGGCGGTGCTGGCCTCGATTACCTGGCCTACGCCATC
GCCATGGAGGAGATCAGCCGTGGCTGCGCCTCCACCGGAGTCATCATGAGTGTCAACAAC
TCTCTCTACCTGGGGCCCATCTTGAAGTTTGGCTCCAAGGAGCAGAAGCAGGCGTGGGTC
ACGCCTTTCACCAGTGGTGACAAAATTGGCTGCTTTGCCCTCAGCGAACCAGGGAACGGC
AGTGATGCAGGAGCTGCGTCCACCACCGCCCGGGCCGAGGGCGACTCATGGGTTCTGAAT
GGAACCAAAGCCTGGATCACCAATGCCTGGGAGGCTTCGGCTGCCGTGGTCTTTGCCAGC
ACGGACAGAGCCCTGCAAAACAAGGGCATCAGTGCCTTCCTGGTCCCCATGCCAACGCCT
GGGCTCACGTTGGGGAAGAAAGAAGACAAGCTGGGCATCCGGGGCTCATCCACGGCCAAC
CTCATCTTTGAGGACTGTCGCATCCCCAAGGACAGCATCCTGGGGGAGCCAGGGATGGGC
TTCAAGATAGCCATGCAAACCCTGGACATGGGCCGCATCGGCATCGCCTCCCAGGCCCTG
GGCATTGCCCAGACCGCCCTCGATTGTGCTGTGAACTACGCTGAGAATCGCATGGCCTTC
GGGGCGCCCCTCACCAAGCTCCAGGTCATCCAGTTCAAGTTGGCAGACATGGCCCTGGCC
CTGGAGAGTGCCCGGCTGCTGACCTGGCGCGCTGCCATGCTGAAGGATAACAAGAAGCCT
TTCATCAAGGAGGCAGCCATGGCCAAGCTGGCCGCCTCGGAGGCCGCGACCGCCATCAGC
CACCAGGCCATCCAGATCCTGGGCGGCATGGGCTACGTGACAGAGATGCCGGCAGAGCGG
CACTACCGCGACGCCCGCATCACTGAGATCTACGAGGGCACCAGCGAAATCCAGCGGCTG
GTGATCGCCGGGCATCTGCTCAGGAGCTACCGGAGCTGA
Protein Properties
Number of Residues 412
Molecular Weight 44296.705
Theoretical pI 7.987
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Short-chain specific acyl-CoA dehydrogenase, mitochondrial
MAAALLARASGPARRALCPRAWRQLHTIYQSVELPETHQMLLQTCRDFAEKELFPIAAQV
DKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSVNN
SLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLN
GTKAWITNAWEASAAVVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTAN
LIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAF
GAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLAASEAATAIS
HQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYRS
GenBank ID Protein 337928
UniProtKB/Swiss-Prot ID P16219
UniProtKB/Swiss-Prot Entry Name ACADS_HUMAN
PDB IDs
GenBank Gene ID M26393
GeneCard ID ACADS
GenAtlas ID ACADS
HGNC ID HGNC:90
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed:1286669 ]
  3. Naito E, Ozasa H, Ikeda Y, Tanaka K: Molecular cloning and nucleotide sequence of complementary DNAs encoding human short chain acyl-coenzyme A dehydrogenase and the study of the molecular basis of human short chain acyl-coenzyme A dehydrogenase deficiency. J Clin Invest. 1989 May;83(5):1605-13. [PubMed:2565344 ]
  4. Corydon MJ, Andresen BS, Bross P, Kjeldsen M, Andreasen PH, Eiberg H, Kolvraa S, Gregersen N: Structural organization of the human short-chain acyl-CoA dehydrogenase gene. Mamm Genome. 1997 Dec;8(12):922-6. [PubMed:9383286 ]
  5. Naito E, Indo Y, Tanaka K: Identification of two variant short chain acyl-coenzyme A dehydrogenase alleles, each containing a different point mutation in a patient with short chain acyl-coenzyme A dehydrogenase deficiency. J Clin Invest. 1990 May;85(5):1575-82. [PubMed:1692038 ]
  6. Gregersen N, Winter VS, Corydon MJ, Corydon TJ, Rinaldo P, Ribes A, Martinez G, Bennett MJ, Vianey-Saban C, Bhala A, Hale DE, Lehnert W, Kmoch S, Roig M, Riudor E, Eiberg H, Andresen BS, Bross P, Bolund LA, Kolvraa S: Identification of four new mutations in the short-chain acyl-CoA dehydrogenase (SCAD) gene in two patients: one of the variant alleles, 511C-->T, is present at an unexpectedly high frequency in the general population, as was the case for 625G-->A, together conferring susceptibility to ethylmalonic aciduria. Hum Mol Genet. 1998 Apr;7(4):619-27. [PubMed:9499414 ]
  7. Corydon MJ, Vockley J, Rinaldo P, Rhead WJ, Kjeldsen M, Winter V, Riggs C, Babovic-Vuksanovic D, Smeitink J, De Jong J, Levy H, Sewell AC, Roe C, Matern D, Dasouki M, Gregersen N: Role of common gene variations in the molecular pathogenesis of short-chain acyl-CoA dehydrogenase deficiency. Pediatr Res. 2001 Jan;49(1):18-23. [PubMed:11134486 ]