Search by BoMiProt ID - Bomi6521


Primary Information

BoMiProt ID Bomi6521
Protein Name Isocitrate dehydrogenase [NAD] subunit alpha/mitochondrial/Isocitrate dehydrogenase subunits 3/4/Isocitric dehydrogenase subunit alpha/NAD(+)-specific ICDH subunit alpha
Organism Bos taurus
Uniprot IdP41563
Milk FractionWhey
Ref Sequence Id NP_777069.1
Aminoacid Length 366
Molecular Weight 39668
Fasta Sequence https://www.uniprot.org/uniprot/P41563.fasta
Gene Name IDH3A
Gene Id 282446
Protein Existence Status reviewed

Secondary Information

Protein Function participate in Krebs cycle.Catalytic subunit of Isocitrate dehydrogenase which catalyzes the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate.
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.
PTMs Acetylation and phosphorylation
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
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
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.