Primary Information |
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BoMiProt ID | Bomi6521 |
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Protein Name | Isocitrate dehydrogenase [NAD] subunit alpha/mitochondrial/Isocitrate dehydrogenase subunits 3/4/Isocitric dehydrogenase subunit alpha/NAD(+)-specific ICDH subunit alpha |
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Organism | Bos taurus |
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Uniprot ID | P41563 |
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Milk Fraction | Whey |
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Ref Sequence ID | NP_777069.1 |
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Aminoacid Length | 366 |
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Molecular Weight | 39668 |
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FASTA Sequence |
Download |
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Gene Name | IDH3A |
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Gene ID | 282446 |
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Protein Existence Status | reviewed |
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Secondary Information |
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Protein Function | participate in Krebs cycle.Catalytic subunit of Isocitrate dehydrogenase which catalyzes the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. |
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Biochemical Properties | NAD-dependent isocitrate dehydrogenase (NAD-IDH) exists as the α2βγ heterotetramer composed of the αβ and αγ heterodimers.Uses NAD as cofactor and divalent metal cations; Mn2+ or Mg2+. Activity higher in presence of Mn2+ than of Mg2+. Binds 1 Mg2+ or Mn2+ ion per subunit.can be allosterically activated by citrate and ADP.Inhibited by ATP. NADH can compete with NAD to bind to the active site and inhibits the activity of the αβ heterodimer.Alpha subunit consists of 10 α-helices and 12 β-strands, which fold into a large domain, a small domain, and a clasp domain. |
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PTMs | Acetylation and phosphorylation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|P41563|IDH3A_BOVIN Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial OS=Bos taurus OX=9913 GN=IDH3A PE=1 SV=1
MAGPAWISKVSRLLGAFHNQKQVTRGFAGGVKTVTLIPGDGIGPEISAAVMKIFDAAKAP
IQWEERNVAAIQGPGGKWMIPPEAKESMDKNKMGLKGPLKT*101PIAAGHPSMNLLLRKTFDL
YANVRPCVSIEGYKTPYHDVNIVTIRENTEGEYSGIEHVIVDGVVQSIKLITEAASKRIA
EFAFEYARNNHRSNVTAVHKANIMRMSDGLFLQKCREVAENCKDIKFNEMYLDTVCLNMV
QDPSQFDVLVMPNLYGDILSDLCAGLIGGLGVTPSGNIGANGVAIFESVHGTAPDIAGKD
MANPTALLLSAVMMLRHMGLFDHAAKIETACFATIKDGKSLTKDLGGNSKCSDFTEEICR
RVKDLD
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Predicted Disorder Regions | NA |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Bibliography | Sun P, Ma T, Zhang T, Zhu H, Zhang J, Liu Y, Ding J. Molecular basis for the function of the αβ heterodimer of human NAD-dependent isocitrate dehydrogenase. J Biol Chem. 2019 Nov 1;294(44):16214-16227. doi: 10.1074/jbc.RA119.010099. Epub 2019 Sep 12. PMID: 31515270; PMCID: PMC6827300. |