Isocitrate dehydrogenase [NADP]
Details
- Name
- Isocitrate dehydrogenase [NADP]
- Synonyms
- 1.1.1.42
- icdA
- icdE
- IDH
- IDP
- NADP(+)-specific ICDH
- Oxalosuccinate decarboxylase
- Gene Name
- icd
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0020518|Isocitrate dehydrogenase [NADP] MESKVVVPAQGKKITLQNGKLNVPENPIIPYIEGDGIGVDVTPAMLKVVDAAVEKAYKGE RKISWMEIYTGEKSTQVYGQDVWLPAETLDLIREYRVAIKGPLTTPVGGGIRSLNVALRQ ELDLYICLRPVRYYQGTPSPVKHPELTDMVIFRENSEDIYAGIEWKADSADAEKVIKFLR EEMGVKKIRFPEHCGIGIKPCSEEGTKRLVRAAIEYAIANDRDSVTLVHKGNIMKFTEGA FKDWGYQLAREEFGGELIDGGPWLKVKNPNTGKEIVIKDVIADAFLQQILLRPAEYDVIA CMNLNGDYISDALAAQVGGIGIAPGANIGDECALFEATHGTAPKYAGQDKVNPGSIILSA EMMLRHMGWTEAADLIVKGMEGAINAKTVTYDFERLMDGAKLLKCSEFGDAIIENM
- Number of residues
- 416
- Molecular Weight
- 45756.335
- Theoretical pI
- 4.9
- GO Classification
- Functionsisocitrate dehydrogenase (NADP+) activity / magnesium ion binding / NAD bindingProcesseselectron transport chain / glyoxylate cycle / response to oxidative stress / tricarboxylic acid cycleComponentscytoplasm / cytosol
- General Function
- Nad binding
- Specific Function
- Not Available
- Pfam Domain Function
- Iso_dh (PF00180)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0020519|Isocitrate dehydrogenase [NADP] (icd) ATGGAAAGTAAAGTAGTTGTTCCGGCACAAGGCAAGAAGATCACCCTGCAAAACGGCAAA CTCAACGTTCCTGAAAATCCGATTATCCCTTACATTGAAGGTGATGGAATCGGTGTAGAT GTAACCCCAGCCATGCTGAAAGTGGTCGACGCTGCAGTCGAGAAAGCCTATAAAGGCGAG CGTAAAATCTCCTGGATGGAAATTTACACCGGTGAAAAATCCACACAGGTTTATGGTCAG GACGTCTGGCTGCCTGCTGAAACTCTTGATCTGATTCGTGAATATCGCGTTGCCATTAAA GGTCCGCTGACCACTCCGGTTGGTGGCGGTATTCGCTCTCTGAACGTTGCCCTGCGCCAG GAACTGGATCTCTACATCTGCCTGCGTCCGGTACGTTACTATCAGGGCACTCCAAGCCCG GTTAAACACCCTGAACTGACCGATATGGTTATCTTCCGTGAAAACTCGGAAGACATTTAT GCGGGTATCGAATGGAAAGCAGACTCTGCCGACGCCGAGAAAGTGATTAAATTCCTGCGT GAAGAGATGGGGGTGAAGAAAATTCGCTTCCCGGAACATTGTGGTATCGGTATTAAGCCG TGTTCGGAAGAAGGCACCAAACGTCTGGTTCGTGCAGCGATCGAATACGCAATTGCTAAC GATCGTGACTCTGTGACTCTGGTGCACAAAGGCAACATCATGAAGTTCACCGAAGGAGCG TTTAAAGACTGGGGCTACCAGCTGGCGCGTGAAGAGTTTGGCGGTGAACTGATCGACGGT GGCCCGTGGCTGAAAGTTAAAAACCCGAACACTGGCAAAGAGATCGTCATTAAAGACGTG ATTGCTGATGCATTCCTGCAACAGATCCTGCTGCGTCCGGCTGAATATGATGTTATCGCC TGTATGAACCTGAACGGTGACTACATTTCTGACGCCCTGGCAGCGCAGGTTGGCGGTATC GGTATCGCCCCTGGTGCAAACATCGGTGACGAATGCGCCCTGTTTGAAGCCACCCACGGT ACTGCGCCGAAATATGCCGGTCAGGACAAAGTAAATCCTGGCTCTATTATTCTCTCCGCT GAGATGATGCTGCGCCACATGGGTTGGACCGAAGCGGCTGACTTAATTGTTAAAGGTATG GAAGGCGCAATCAACGCGAAAACCGTAACCTATGACTTCGAGCGTCTGATGGATGGCGCT AAACTGCTGAAATGTTCAGAGTTTGGTGACGCGATCATCGAAAACATGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P08200 UniProtKB Entry Name IDH_ECOLI GenBank Protein ID 146432 GenBank Gene ID J02799 - General References
- Thorsness PE, Koshland DE Jr: Inactivation of isocitrate dehydrogenase by phosphorylation is mediated by the negative charge of the phosphate. J Biol Chem. 1987 Aug 5;262(22):10422-5. [Article]
- Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Wang FS, Whittam TS, Selander RK: Evolutionary genetics of the isocitrate dehydrogenase gene (icd) in Escherichia coli and Salmonella enterica. J Bacteriol. 1997 Nov;179(21):6551-9. [Article]
- Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [Article]
- Lee ME, Dyer DH, Klein OD, Bolduc JM, Stoddard BL, Koshland DE Jr: Mutational analysis of the catalytic residues lysine 230 and tyrosine 160 in the NADP(+)-dependent isocitrate dehydrogenase from Escherichia coli. Biochemistry. 1995 Jan 10;34(1):378-84. [Article]
- VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
- Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y: Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli. Mol Cell Proteomics. 2009 Feb;8(2):215-25. doi: 10.1074/mcp.M800187-MCP200. Epub 2008 Aug 23. [Article]
- Zhang Z, Tan M, Xie Z, Dai L, Chen Y, Zhao Y: Identification of lysine succinylation as a new post-translational modification. Nat Chem Biol. 2011 Jan;7(1):58-63. doi: 10.1038/nchembio.495. Epub 2010 Dec 12. [Article]
- Hurley JH, Dean AM, Sohl JL, Koshland DE Jr, Stroud RM: Regulation of an enzyme by phosphorylation at the active site. Science. 1990 Aug 31;249(4972):1012-6. [Article]
- Bolduc JM, Dyer DH, Scott WG, Singer P, Sweet RM, Koshland DE Jr, Stoddard BL: Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase. Science. 1995 Jun 2;268(5215):1312-8. [Article]
- Hurley JH, Thorsness PE, Ramalingam V, Helmers NH, Koshland DE Jr, Stroud RM: Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase. Proc Natl Acad Sci U S A. 1989 Nov;86(22):8635-9. [Article]
- Cherbavaz DB, Lee ME, Stroud RM, Koshland DE Jr: Active site water molecules revealed in the 2.1 A resolution structure of a site-directed mutant of isocitrate dehydrogenase. J Mol Biol. 2000 Jan 21;295(3):377-85. [Article]
- Doyle SA, Beernink PT, Koshland DE Jr: Structural basis for a change in substrate specificity: crystal structure of S113E isocitrate dehydrogenase in a complex with isopropylmalate, Mg2+, and NADP. Biochemistry. 2001 Apr 10;40(14):4234-41. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01727 Isocitric Acid experimental unknown Details DB02190 (S)-oxalosuccinic acid experimental unknown Details DB03461 Nicotinamide adenine dinucleotide phosphate experimental unknown Details DB04279 3-Isopropylmalic Acid experimental unknown Details