Homoisocitrate dehydrogenase, mitochondrial (P40495)

Identification
NameHomoisocitrate dehydrogenase, mitochondrial
SynonymsNot Available
Gene NameLYS12
Enzyme Class
Biological Properties
General FunctionInvolved in magnesium ion binding
Specific FunctionCatalyzes the NAD(+)-dependent conversion of homoisocitrate to alpha-ketoadipate
Cellular LocationMitochondrion
SMPDB Pathways
Citric Acid Cycle 1434561204PW000970 ThumbThumb?image type=greyscaleThumb?image type=simple
TCA CyclePW002377 ThumbThumb?image type=greyscaleThumb?image type=simple
lysine metabolismPW002420 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Lysine biosynthesisec00300 Map00300
SMPDB Reactions
Isocitric acid + NAD → Oxoglutaric acid + Carbon dioxide + NADH + hydron
Isocitric acid + NAD → Oxoglutaric acid + Carbon dioxide + NADH + hydron
(1R,2S)-homoisocitrate + NAD → Carbon dioxide + NADH + Oxoadipic acid
KEGG Reactions
NAD + Homoisocitric acid ↔ NADH + 2-Oxaloglutaric acid + hydron
Metabolites
YMDB IDNameView
YMDB00026Isocitric acidShow
YMDB00110NADShow
YMDB00142Oxoadipic acidShow
YMDB00143NADHShow
YMDB00144Homoisocitric acidShow
YMDB00153Oxoglutaric acidShow
YMDB00412NAD(+)Show
YMDB007052-Oxaloglutaric acidShow
YMDB00862hydronShow
YMDB00912Carbon dioxideShow
YMDB16305(1R,2S)-homoisocitrateShow
GO Classification
Component
Not Available
Function
magnesium ion binding
oxidoreductase activity, acting on CH-OH group of donors
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
NAD or NADH binding
catalytic activity
binding
nucleotide binding
ion binding
cation binding
metal ion binding
oxidoreductase activity
Process
metabolic process
oxidation reduction
Gene Properties
Chromosome Locationchromosome 9
LocusYIL094C
Gene Sequence>1116 bp ATGTTTAGATCTGTTGCTACTAGATTATCTGCCTGCCGTGGGTTAGCATCTAACGCTGCT CGCAAATCACTCACTATTGGTCTTATCCCCGGTGACGGTATCGGTAAGGAAGTCATTCCT GCTGGTAAGCAAGTTTTGGAAAACCTTAACTCCAAGCACGGCCTAAGCTTCAACTTTATT GATCTCTACGCCGGTTTCCAAACATTCCAAGAAACAGGAAAGGCGTTGCCTGATGAGACT GTTAAAGTGTTGAAGGAACAATGTCAAGGTGCTCTTTTCGGTGCAGTTCAGTCTCCAACT ACTAAGGTGGAAGGTTACTCCTCACCAATTGTTGCTCTAAGGAGGGAAATGGGCCTTTTC GCTAATGTTCGTCCTGTTAAGTCTGTAGAGGGAGAAAAGGGTAAACCAATTGACATGGTT ATCGTCAGAGAAAATACTGAGGACCTGTACATTAAAATTGAAAAAACATACATTGACAAG GCCACAGGTACAAGAGTTGCTGATGCCACAAAGAGAATATCCGAAATTGCAACAAGAAGA ATTGCAACCATTGCATTAGATATTGCCTTGAAAAGATTACAAACAAGAGGCCAAGCCACT TTGACAGTGACTCATAAATCAAATGTTCTATCTCAAAGTGATGGTCTATTCAGAGAAATC TGTAAGGAAGTCTACGAATCTAACAAGGACAAGTACGGTCAAATCAAATATAACGAACAA ATTGTGGATTCCATGGTTTATAGGCTGTTCAGAGAACCACAATGTTTTGATGTGATAGTG GCACCAAACCTATACGGGGATATATTATCTGACGGTGCTGCTGCTTTAGTCGGTTCATTA GGTGTTGTTCCAAGCGCCAACGTAGGTCCAGAAATTGTCATTGGTGAACCATGCCATGGT TCTGCACCAGATATTGCTGGTAAAGGTATTGCTAACCCAATCGCCACTATAAGATCTACT GCTTTGATGTTGGAATTCTTGGGCCACAACGAAGCTGCCCAAGATATCTACAAGGCTGTT GATGCTAACTTAAGAGAGGGTTCTATCAAGACACCAGATTTAGGTGGTAAGGCTTCTACT CAACAAGTCGTTGACGACGTTTTGTCGAGATTATAG
Protein Properties
Pfam Domain Function
Protein Residues371
Protein Molecular Weight40068.60156
Protein Theoretical pI8.18
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Homoisocitrate dehydrogenase, mitochondrial MFRSVATRLSACRGLASNAARKSLTIGLIPGDGIGKEVIPAGKQVLENLNSKHGLSFNFI DLYAGFQTFQETGKALPDETVKVLKEQCQGALFGAVQSPTTKVEGYSSPIVALRREMGLF ANVRPVKSVEGEKGKPIDMVIVRENTEDLYIKIEKTYIDKATGTRVADATKRISEIATRR IATIALDIALKRLQTRGQATLTVTHKSNVLSQSDGLFREICKEVYESNKDKYGQIKYNEQ IVDSMVYRLFREPQCFDVIVAPNLYGDILSDGAAALVGSLGVVPSANVGPEIVIGEPCHG SAPDIAGKGIANPIATIRSTALMLEFLGHNEAAQDIYKAVDANLREGSIKTPDLGGKAST QQVVDDVLSRL
References
External Links
ResourceLink
Saccharomyces Genome Database LYS12
Uniprot IDP40495
Uniprot NameLYS12_YEAST
GenBank Gene IDZ46728
Genebank Protein ID577120
General Reference
  • Churcher, C., Bowman, S., Badcock, K., Bankier, A., Brown, D., Chillingworth, T., Connor, R., Devlin, K., Gentles, S., Hamlin, N., Harris, D., Horsnell, T., Hunt, S., Jagels, K., Jones, M., Lye, G., Moule, S., Odell, C., Pearson, D., Rajandream, M., Rice, P., Rowley, N., Skelton, J., Smith, V., Barrell, B., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX." Nature 387:84-87.9169870
  • Strassman, M., Ceci, L. N. (1965). "Enzymatic formation of alpha-ketoadipic acid from homoisocitric acid." J Biol Chem 240:4357-4361.4284830
  • Rowley, B., Tucci, A. F. (1970). "Homoisocitric dehydrogenase from yeast." Arch Biochem Biophys 141:499-510.4395693
  • Urrestarazu, L. A., Borell, C. W., Bhattacharjee, J. K. (1985). "General and specific controls of lysine biosynthesis in Saccharomyces cerevisiae." Curr Genet 9:341-344.3939712
  • Shevchenko, A., Jensen, O. N., Podtelejnikov, A. V., Sagliocco, F., Wilm, M., Vorm, O., Mortensen, P., Shevchenko, A., Boucherie, H., Mann, M. (1996). "Linking genome and proteome by mass spectrometry: large-scale identification of yeast proteins from two dimensional gels." Proc Natl Acad Sci U S A 93:14440-14445.8962070
  • Huh, W. K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., O'Shea, E. K. (2003). "Global analysis of protein localization in budding yeast." Nature 425:686-691.14562095
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Sickmann, A., Reinders, J., Wagner, Y., Joppich, C., Zahedi, R., Meyer, H. E., Schonfisch, B., Perschil, I., Chacinska, A., Guiard, B., Rehling, P., Pfanner, N., Meisinger, C. (2003). "The proteome of Saccharomyces cerevisiae mitochondria." Proc Natl Acad Sci U S A 100:13207-13212.14576278
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956