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Showing Protein Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial (HMDBP00381)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 26 metabolites
Identification
HMDB Protein ID HMDBP00381
Secondary Accession Numbers
  • 5618
  • HMDBP05824
Name Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
Synonyms
  1. HCDH
  2. Medium and short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase
  3. Short-chain 3-hydroxyacyl-CoA dehydrogenase
Gene Name HADH
Protein Type Unknown
Biological Properties
General Function Involved in 3-hydroxyacyl-CoA dehydrogenase activity
Specific Function Plays an essential role in the mitochondrial beta-oxidation of short chain fatty acids. Exerts it highest activity toward 3-hydroxybutyryl-CoA.
Pathways
  • 2-aminoadipic 2-oxoadipic aciduria
  • Butanoate metabolism
  • Butyrate Metabolism
  • fatty acid beta-oxidation
  • Fatty acid elongation
  • fatty acid metabolism
  • Glutaric Aciduria Type I
  • Hyperlysinemia I, Familial
  • Hyperlysinemia II or Saccharopinuria
  • Lysine degradation
  • Lysine degradation
  • Mitochondrial Beta-Oxidation of Long Chain Saturated Fatty Acids
  • Mitochondrial Beta-Oxidation of Medium Chain Saturated Fatty Acids
  • Mitochondrial Beta-Oxidation of Short Chain Saturated Fatty Acids
  • Pyridoxine dependency with seizures
  • Saccharopinuria/Hyperlysinemia II
  • Short-chain 3-hydroxyacyl-CoA dehydrogenase deficiency (SCHAD)
  • Tryptophan metabolism
  • Valine, leucine and isoleucine degradation
Reactions
(S)-3-hydroxyacyl-CoA + NAD → 3-oxoacyl-CoA + NADH details
(3S)-3-Hydroxyacyl-CoA + NAD → 3-Oxoacyl-CoA + NADH + Hydrogen Ion details
3-Hydroxybutyryl-CoA + NAD → Acetoacetyl-CoA + NADH + Hydrogen Ion details
2-Methyl-3-hydroxybutyryl-CoA + NAD → 2-Methylacetoacetyl-CoA + NADH + Hydrogen Ion details
(S)-3-Hydroxyhexadecanoyl-CoA + NAD → 3-Oxohexadecanoyl-CoA + NADH + Hydrogen Ion details
(S)-3-Hydroxytetradecanoyl-CoA + NAD → 3-Oxotetradecanoyl-CoA + NADH details
(S)-3-Hydroxydodecanoyl-CoA + NAD → 3-Oxododecanoyl-CoA + NADH + Hydrogen Ion details
(S)-Hydroxydecanoyl-CoA + NAD → 3-Oxodecanoyl-CoA + NADH + Hydrogen Ion details
(S)-Hydroxyoctanoyl-CoA + NAD → 3-Oxooctanoyl-CoA + NADH + Hydrogen Ion details
(S)-Hydroxyhexanoyl-CoA + NAD → 3-Oxohexanoyl-CoA + NADH + Hydrogen Ion details
(S)-3-Hydroxyisobutyric acid + NAD → (S)-Methylmalonic acid semialdehyde + NADH + Hydrogen Ion details
(3S)-3-Hydroxyadipyl-CoA + NAD → 3-Oxoadipyl-CoA + NADH + Hydrogen Ion details
3-Hydroxy-5-methylhex-4-enoyl-CoA + NAD → 5-Methyl-3-oxo-4-hexenoyl-CoA + NADH + Hydrogen Ion details
GO Classification
Biological Process
response to insulin stimulus
response to drug
negative regulation of insulin secretion
response to activity
fatty acid beta-oxidation
Cellular Component
mitochondrial matrix
nucleus
mitochondrial inner membrane
Function
binding
nucleotide binding
catalytic activity
nad or nadh binding
oxidoreductase activity, acting on the ch-oh group of donors, nad or nadp as acceptor
coenzyme binding
cofactor binding
nad binding
3-hydroxyacyl-coa dehydrogenase activity
oxidoreductase activity, acting on ch-oh group of donors
oxidoreductase activity
Molecular Function
3-hydroxyacyl-CoA dehydrogenase activity
NAD+ binding
Process
metabolic process
cellular metabolic process
organic acid metabolic process
oxoacid metabolic process
carboxylic acid metabolic process
monocarboxylic acid metabolic process
fatty acid metabolic process
Cellular Location
  1. Mitochondrion matrix
Gene Properties
Chromosome Location 4
Locus 4q22-q26
SNPs HADH
Gene Sequence 
>945 bp
ATGGCCTTCGTCACCAGGCAGTTCATGCGTTCCGTGTCCTCCTCGTCCACCGCCTCGGCC
TCGGCCAAGAAGATAATCGTCAAGCACGTGACGGTCATCGGCGGCGGGCTGATGGGCGCC
GGCATTGCCCAGGTTGCTGCAGCAACTGGTCACACAGTAGTGTTGGTAGACCAGACAGAG
GACATCCTGGCAAAATCCAAAAAGGGAATTGAGGAAAGCCTTAGGAAAGTGGCAAAGAAG
AAGTTTGCAGAAAACCCTAAGGCCGGCGATGAATTTGTGGAGAAGACCCTGAGCACCATA
GCGACCAGCACGGATGCAGCCTCCGTTGTCCACAGCACAGACTTGGTGGTGGAAGCCATC
GTGGAGAATCTGAAGGTGAAAAACGAGCTCTTCAAAAGGCTGGACAAGTTTGCTGCTGAA
CATACAATCTTTGCCAGCAACACTTCCTCCTTGCATATTACAAGCATAGCTAATGCCACC
ACCAGACAAGACCGATTCGCTGGCCTCCATTTCTTCAACCCAGTGCCTGTCATGAAACTT
GTGGAGGTCATTAAAACACCAATGACCAGCCAGAAGACATTTGAATCTTTGGTAGACTTT
AGCAAAGCCCTAGGAAAGCATCCTGTTTCTTGCAAGGACACTCCTGGGTTTATTGTGAAC
CGCCTCCTGGTTCCATACCTCATGGAAGCAATCAGGCTGTATGAACGAGGTGACGCATCC
AAAGAAGACATTGACACTGCTATGAAATTAGGAGCCGGTTACCCCATGGGCCCATTTGAG
CTTCTAGATTATGTCGGACTGGATACTACGAAGTTCATCGTGGATGGGTGGCATGAAATG
GATGCAGAGAACCCATTACATCAGCCCAGCCCATCCTTAAATAAGCTGGTAGCAGAGAAC
AAGTTCGGCAAGAAGACTGGAGAAGGATTTTACAAATACAAGTGA
Protein Properties
Number of Residues 314
Molecular Weight 36035.11
Theoretical pI 8.535
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
MAFVTRQFMRSVSSSSTASASAKKIIVKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTE
DILAKSKKGIEESLRKVAKKKFAENPKAGDEFVEKTLSTIATSTDAASVVHSTDLVVEAI
VENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKL
VEVIKTPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDAS
KEDIDTAMKLGAGYPMGPFELLDYVGLDTTKFIVDGWHEMDAENPLHQPSPSLNKLVAEN
KFGKKTGEGFYKYK
GenBank ID Protein 1483511
UniProtKB/Swiss-Prot ID Q16836
UniProtKB/Swiss-Prot Entry Name HCDH_HUMAN
PDB IDs
GenBank Gene ID X96752
GeneCard ID HADH
GenAtlas ID HADH
HGNC ID HGNC:4799
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. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Vredendaal PJ, van den Berg IE, Malingre HE, Stroobants AK, Olde Weghuis DE, Berger R: Human short-chain L-3-hydroxyacyl-CoA dehydrogenase: cloning and characterization of the coding sequence. Biochem Biophys Res Commun. 1996 Jun 25;223(3):718-23. [PubMed:8687463 ]
  4. Barycki JJ, O'Brien LK, Bratt JM, Zhang R, Sanishvili R, Strauss AW, Banaszak LJ: Biochemical characterization and crystal structure determination of human heart short chain L-3-hydroxyacyl-CoA dehydrogenase provide insights into catalytic mechanism. Biochemistry. 1999 May 4;38(18):5786-98. [PubMed:10231530 ]
  5. Barycki JJ, O'Brien LK, Strauss AW, Banaszak LJ: Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase. J Biol Chem. 2000 Sep 1;275(35):27186-96. [PubMed:10840044 ]
  6. Yang SY, He XY, Schulz H: 3-Hydroxyacyl-CoA dehydrogenase and short chain 3-hydroxyacyl-CoA dehydrogenase in human health and disease. FEBS J. 2005 Oct;272(19):4874-83. [PubMed:16176262 ]
  7. Clayton PT, Eaton S, Aynsley-Green A, Edginton M, Hussain K, Krywawych S, Datta V, Malingre HE, Berger R, van den Berg IE: Hyperinsulinism in short-chain L-3-hydroxyacyl-CoA dehydrogenase deficiency reveals the importance of beta-oxidation in insulin secretion. J Clin Invest. 2001 Aug;108(3):457-65. [PubMed:11489939 ]