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Identification
HMDB Protein ID HMDBP00051
Secondary Accession Numbers
  • 5280
  • HMDBP04708
Name Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial
Synonyms
  1. Aldehyde dehydrogenase family 6 member A1
  2. MMSDH
  3. Malonate-semialdehyde dehydrogenase [acylating]
Gene Name ALDH6A1
Protein Type Unknown
Biological Properties
General Function Involved in oxidoreductase activity
Specific Function Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA.
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-Alanine Metabolism
  • beta-Alanine metabolism
  • Beta-Ketothiolase Deficiency
  • Carnosinuria, carnosinemia
  • GABA-Transaminase Deficiency
  • Inositol phosphate metabolism
  • Isobutyryl-coa dehydrogenase deficiency
  • Isovaleric acidemia
  • Isovaleric Aciduria
  • Malonic Aciduria
  • Malonyl-coa decarboxylase deficiency
  • Maple Syrup Urine Disease
  • Methylmalonate Semialdehyde Dehydrogenase Deficiency
  • Methylmalonic Aciduria
  • Methylmalonic Aciduria Due to Cobalamin-Related Disorders
  • Propanoate Metabolism
  • Propanoate metabolism
  • Propionic Acidemia
  • Ureidopropionase Deficiency
  • Valine, Leucine and Isoleucine Degradation
  • Valine, leucine and isoleucine degradation
Reactions
2-Methyl-3-oxopropanoic acid + Coenzyme A + Water + NAD → Propionyl-CoA + Carbonic acid + NADH details
Malonic semialdehyde + Coenzyme A + NAD(P)(+) → Acetyl-CoA + CO(2) + NAD(P)H details
Malonic semialdehyde + Coenzyme A + NAD → Acetyl-CoA + Carbon dioxide + NADH + Hydrogen Ion details
Malonic semialdehyde + Coenzyme A + NADP → Acetyl-CoA + Carbon dioxide + NADPH + Hydrogen Ion details
Malonic semialdehyde + Coenzyme A + NADP → Malonyl-CoA + NADPH + Hydrogen Ion details
(S)-Methylmalonic acid semialdehyde + Coenzyme A + NAD → Propionyl-CoA + Carbon dioxide + NADH + Hydrogen Ion details
(S)-Methylmalonic acid semialdehyde + Coenzyme A + NAD → Methylmalonyl-CoA + NADH + Hydrogen Ion details
GO Classification
Biological Process
beta-alanine catabolic process
thymine metabolic process
branched-chain amino acid catabolic process
valine metabolic process
brown fat cell differentiation
thymine catabolic process
valine catabolic process
Cellular Component
mitochondrial matrix
nucleus
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on the aldehyde or oxo group of donors
oxidoreductase activity, acting on the aldehyde or oxo group of donors, nad or nadp as acceptor
methylmalonate-semialdehyde dehydrogenase (acylating) activity
Molecular Function
malonate-semialdehyde dehydrogenase (acetylating) activity
methylmalonate-semialdehyde dehydrogenase (acylating) activity
thiolester hydrolase activity
fatty-acyl-CoA binding
Process
metabolic process
cellular metabolic process
oxidation reduction
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
branched chain family amino acid metabolic process
valine metabolic process
Cellular Location
  1. Mitochondrion
Gene Properties
Chromosome Location 14
Locus 14q24.3
SNPs ALDH6A1
Gene Sequence
>1608 bp
ATGGCGGCGCTATTGGCGGCGGCGGCAGTGCGAGCCCGGATCCTGCAGGTTTCTTCCAAG
GTGAAATCCAGTCCCACCTGGTATTCAGCATCTTCCTTCTCTTCTTCAGTGCCAACTGTA
AAGCTCTTCATTGGTGGGAAATTCGTTGAATCCAAAAGTGACAAATGGATCGATATCCAC
AACCCAGCCACCAATGAGGTCATTGGTCGGGTCCCTCAGGCCACCAAGGCAGAAATGGAT
GCAGCCATTGCTTCCTGCAAACGTGCTTTTCCTGCATGGGCAGACACTTCAGTATTAAGC
CGCCAGCAGGTCTTGCTCCGCTATCAACAACTTATTAAAGAAAACTTGAAAGAAATTGCC
AAGTTAATCACATTGGAACAAGGGAAGACCCTAGCTGATGCTGAAGGAGATGTATTTCGA
GGCCTTCAGGTGGTTGAGCATGCCTGTAGTGTGACATCCCTCATGATGGGAGAGACCATG
CCATCCATCACCAAAGACATGGACCTTTATTCCTACCGTCTGCCTCTGGGAGTGTGTGCA
GGCATTGCTCCATTCAATTTTCCTGCCATGATCCCCCTTTGGATGTTTCCCATGGCCATG
GTGTGTGGAAATACCTTCCTAATGAAACCATCTGAGCGAGTCCCTGGAGCAACTATGCTT
CTTGCTAAGTTGCTCCAGGATTCTGGTGCCCCTGATGGAACATTAAACATCATCCATGGA
CAGCATGAAGCTGTAAATTTTATTTGCGATCATCCGGACATCAAAGCAATCAGCTTTGTG
GGATCCAACAAGGCAGGAGAGTATATCTTCGAGAGAGGATCAAGACATGGCAAGAGGGTT
CAAGCCAATATGGGAGCCAAGAACCATGGGGTAGTCATGCCAGATGCCAATAAGGAAAAT
ACCCTGAACCAGCTGGTTGGGGCAGCATTTGGAGCTGCTGGTCAGCGCTGCATGGCTCTT
TCAACAGCAGTCCTTGTGGGAGAAGCCAAGAAGTGGCTGCCAGAGCTGGTGGAGCATGCC
AAAAACCTGAGAGTCAATGCAGGAGATCAGCCTGGAGCTGATCTTGGCCCTCTGATCACT
CCCCAGGCCAAAGAGCGAGTCTGTAATCTGATTGATAGTGGAACAAAGGAGGGAGCTTCC
ATCCTTCTTGATGGACGAAAAATTAAAGTGAAAGGCTATGAAAATGGCAACTTTGTTGGA
CCAACCATCATCTCGAATGTCAAGCCAAATATGACCTGTTACAAAGAGGAGATTTTTGGT
CCAGTTCTTGTGGTTCTGGAGACAGAAACATTGGATGAAGCCATCCAGATTGTAAATAAC
AACCCATATGGAAATGGAACTGCCATCTTCACCACCAATGGAGCCACTGCTCGGAAATAT
GCCCACTTGGTGGATGTTGGACAGGTGGGAGTGAATGTCCCCATTCCAGTGCCTTTGCCA
ATGTTCTCATTCACCGGCTCTCGATCCTCCTTCAGGGGAGACACCAATTTCTATGGCAAA
CAGGGCATCCAATTCTACACTCAGTTAAAGACCATTACTTCTCAGTGGAAAGAAGAAGAT
GCTACTCTTTCCTCACCTGCTGTTGTCATGCCTACCATGGGCCGTTAG
Protein Properties
Number of Residues 535
Molecular Weight 57839.31
Theoretical pI 8.494
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial
MAALLAAAAVRARILQVSSKVKSSPTWYSASSFSSSVPTVKLFIGGKFVESKSDKWIDIH
NPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIA
KLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCA
GIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHG
QHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKEN
TLNQLVGAAFGAAGQRCMALSTAVLVGEAKKWLPELVEHAKNLRVNAGDQPGADLGPLIT
PQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFG
PVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPLP
MFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQWKEEDATLSSPAVVMPTMGR
GenBank ID Protein 6164678
UniProtKB/Swiss-Prot ID Q02252
UniProtKB/Swiss-Prot Entry Name MMSA_HUMAN
PDB IDs Not Available
GenBank Gene ID AF148505
GeneCard ID ALDH6A1
GenAtlas ID ALDH6A1
HGNC ID HGNC:7179
References
General References
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  2. 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 ]
  3. Chambliss KL, Gray RG, Rylance G, Pollitt RJ, Gibson KM: Molecular characterization of methylmalonate semialdehyde dehydrogenase deficiency. J Inherit Metab Dis. 2000 Jul;23(5):497-504. [PubMed:10947204 ]
  4. Kedishvili NY, Popov KM, Rougraff PM, Zhao Y, Crabb DW, Harris RA: CoA-dependent methylmalonate-semialdehyde dehydrogenase, a unique member of the aldehyde dehydrogenase superfamily. cDNA cloning, evolutionary relationships, and tissue distribution. J Biol Chem. 1992 Sep 25;267(27):19724-9. [PubMed:1527093 ]