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
binding
nucleotide binding
ion binding
cation binding
metal ion binding
oxidoreductase activity
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
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