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Showing Protein Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial (HMDBP00899)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 8 metabolites
Identification
HMDB Protein ID HMDBP00899
Secondary Accession Numbers
  • 6181
  • HMDBP03648
Name Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial
Synonyms
  1. Isocitric dehydrogenase subunit alpha
  2. NAD(+)-specific ICDH subunit alpha
Gene Name IDH3A
Protein Type Unknown
Biological Properties
General Function Involved in magnesium ion binding
Specific Function Not Available
Pathways
  • 2-ketoglutarate dehydrogenase complex deficiency
  • 2-Oxocarboxylic acid metabolism
  • Citrate cycle (TCA cycle)
  • Citric Acid Cycle
  • Congenital lactic acidosis
  • Fumarase deficiency
  • Glutaminolysis and Cancer
  • Mitochondrial complex II deficiency
  • Pyruvate dehydrogenase deficiency (E2)
  • Pyruvate dehydrogenase deficiency (E3)
  • The oncogenic action of 2-hydroxyglutarate
  • The oncogenic action of D-2-hydroxyglutarate in Hydroxygluaricaciduria
  • The Oncogenic Action of Fumarate
  • The oncogenic action of L-2-hydroxyglutarate in Hydroxygluaricaciduria
  • The Oncogenic Action of Succinate
  • Warburg Effect
Reactions
Isocitric acid + NAD → Oxoglutaric acid + CO(2) + NADH details
Isocitric acid + NAD → Oxoglutaric acid + Carbon dioxide + NADH + Hydrogen Ion details
GO Classification
Biological Process
small molecule metabolic process
NADH metabolic process
2-oxoglutarate metabolic process
tricarboxylic acid cycle
isocitrate metabolic process
carbohydrate metabolic process
Cellular Component
mitochondrial matrix
Component
mitochondrion
organelle
membrane-bounded organelle
intracellular membrane-bounded organelle
Function
ion binding
cation binding
metal ion binding
binding
nucleotide binding
catalytic activity
isocitrate dehydrogenase activity
isocitrate dehydrogenase (nad+) activity
magnesium ion binding
nad or nadh binding
oxidoreductase activity, acting on the ch-oh group of donors, nad or nadp as acceptor
oxidoreductase activity, acting on ch-oh group of donors
oxidoreductase activity
Molecular Function
NAD binding
magnesium ion binding
isocitrate dehydrogenase (NAD+) activity
Process
metabolic process
cellular metabolic process
oxidation reduction
cofactor metabolic process
coenzyme metabolic process
acetyl-coa metabolic process
acetyl-coa catabolic process
tricarboxylic acid cycle
Cellular Location
  1. Mitochondrion
Gene Properties
Chromosome Location 15
Locus 15q25.1-q25.2
SNPs IDH3A
Gene Sequence 
>1101 bp
ATGGCTGGGCCCGCGTGGATCTCCAAGGTCTCTCGGCTGCTGGGGGCATTCCACAACCCA
AAACAGGTGACCAGAGGTTTTACTGGTGGTGTTCAGACAGTAACTTTAATTCCAGGAGAT
GGTATTGGCCCAGAAATTTCAGCTGCAGTTATGAAGATTTTTGATGCTGCCAAAGCACCT
ATTCAGTGGGAGGAGCGGAACGTCACTGCCATTCAAGGACCTGGAGGAAAGTGGATGATC
CCTTCAGAGGCTAAAGAGTCCATGGATAAGAACAAGATGGGCTTGAAAGGCCCTTTGAAG
ACCCCAATAGCAGCCGGTCACCCATCTATGAATTTACTGCTGCGCAAAACATTTGACCTT
TACGCGAATGTCCGACCATGTGTCTCTATCGAAGGCTATAAAACCCCTTACACCGATGTA
AATATTGTGACCATTCGAGAGAACACAGAAGGAGAATACAGTGGAATTGAGCATGTGATT
GTTGATGGAGTCGTGCAGAGTATCAAGCTCATCACCGAGGGGGCGAGCAAGCGCATTGCT
GAGTTTGCCTTTGAGTATGCCCGGAACAACCACCGGAGCAACGTCACGGCGGTGCACAAA
GCCAACATCATGCGGATGTCAGATGGGCTTTTTCTACAAAAATGCAGGGAAGTTGCAGAA
AGCTGTAAAGATATTAAATTTAATGAGATGTACCTTGATACAGTATGTTTGAATATGGTA
CAAGATCCTTCCCAATTTGATGTTCTTGTTATGCCAAATTTGTATGGAGACATCCTTAGT
GACTTGTGTGCAGGATTGATCGGAGGTCTCGGTGTGACACCAAGTGGCAACATTGGAGCC
AATGGGGTTGCAATTTTTGAGTCGGTTCATGGGACGGCTCCAGACATTGCAGGCAAGGAC
ATGGCGAATCCCACAGCCCTCCTGCTCAGTGCCGTGATGATGCTGCGCCACATGGGACTT
TTTGACCATGCTGCAAGAATTGAGGCTGCGTGTTTTGCTACAATTAAGGACGGAAAGAGC
TTGACAAAAGATTTGGGAGGCAATGCAAAATGCTCAGACTTCACAGAGGAAATCTGTCGC
CGAGTAAAAGATTTAGATTAA
Protein Properties
Number of Residues 366
Molecular Weight 39591.365
Theoretical pI 6.924
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial
MAGPAWISKVSRLLGAFHNPKQVTRGFTGGVQTVTLIPGDGIGPEISAAVMKIFDAAKAP
IQWEERNVTAIQGPGGKWMIPSEAKESMDKNKMGLKGPLKTPIAAGHPSMNLLLRKTFDL
YANVRPCVSIEGYKTPYTDVNIVTIRENTEGEYSGIEHVIVDGVVQSIKLITEGASKRIA
EFAFEYARNNHRSNVTAVHKANIMRMSDGLFLQKCREVAESCKDIKFNEMYLDTVCLNMV
QDPSQFDVLVMPNLYGDILSDLCAGLIGGLGVTPSGNIGANGVAIFESVHGTAPDIAGKD
MANPTALLLSAVMMLRHMGLFDHAARIEAACFATIKDGKSLTKDLGGNAKCSDFTEEICR
RVKDLD
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P50213
UniProtKB/Swiss-Prot Entry Name IDH3A_HUMAN
PDB IDs Not Available
GenBank Gene ID U07681
GeneCard ID IDH3A
GenAtlas ID IDH3A
HGNC ID HGNC:5384
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. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed:17974005 ]
  4. Kim YO, Oh IU, Park HS, Jeng J, Song BJ, Huh TL: Characterization of a cDNA clone for human NAD(+)-specific isocitrate dehydrogenase alpha-subunit and structural comparison with its isoenzymes from different species. Biochem J. 1995 May 15;308 ( Pt 1):63-8. [PubMed:7755589 ]