P08200 · IDH_ECOLI
- ProteinIsocitrate dehydrogenase [NADP]
- Geneicd
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids416 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the oxidative decarboxylation of isocitrate to 2-oxoglutarate and carbon dioxide with the concomitant reduction of NADP+.
Catalytic activity
- D-threo-isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Activity regulation
Inhibition of this enzyme by phosphorylation regulates the branch point between the Krebs cycle and the glyoxylate bypass, which is an alternate route that accumulates carbon for biosynthesis when acetate is the sole carbon source for growth.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
11.4 μM | isocitrate | |||||
13 μM | isocitrate |
pH Dependence
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 104 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 113 | D-threo-isocitrate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 115 | D-threo-isocitrate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 119 | D-threo-isocitrate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 129 | D-threo-isocitrate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 153 | D-threo-isocitrate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Site | 160 | Critical for catalysis | ||||
Sequence: Y | ||||||
Site | 230 | Critical for catalysis | ||||
Sequence: K | ||||||
Binding site | 307 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 307 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 311 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 339-345 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: HGTAPKY | ||||||
Binding site | 352 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 391 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 395 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Molecular Function | guanosine tetraphosphate binding | |
Molecular Function | isocitrate dehydrogenase (NADP+) activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | NAD binding | |
Biological Process | electron transport chain | |
Biological Process | glyoxylate cycle | |
Biological Process | response to oxidative stress | |
Biological Process | tricarboxylic acid cycle |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameIsocitrate dehydrogenase [NADP]
- EC number
- Short namesIDH
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP08200
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 100 | Abolishes enzymatic activity. | ||||
Sequence: K → R or E | ||||||
Mutagenesis | 113 | Decreased enzyme activity. Loss of phosphorylation. | ||||
Sequence: S → A or T | ||||||
Mutagenesis | 113 | Reduced affinity for isocitrate. | ||||
Sequence: S → D or E | ||||||
Mutagenesis | 113 | Loss of enzyme activity. | ||||
Sequence: S → D | ||||||
Mutagenesis | 160 | Nearly abolishes enzyme activity. No significant effect on substrate affinity. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 230 | Nearly abolishes enzyme activity and strongly reduces substrate affinity. | ||||
Sequence: K → M | ||||||
Mutagenesis | 242 | Strongly impairs enzymatic activity. | ||||
Sequence: K → E | ||||||
Mutagenesis | 242 | Impairs enzymatic activity. | ||||
Sequence: K → R |
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000083551 | 1-416 | Isocitrate dehydrogenase [NADP] | |||
Sequence: MESKVVVPAQGKKITLQNGKLNVPENPIIPYIEGDGIGVDVTPAMLKVVDAAVEKAYKGERKISWMEIYTGEKSTQVYGQDVWLPAETLDLIREYRVAIKGPLTTPVGGGIRSLNVALRQELDLYICLRPVRYYQGTPSPVKHPELTDMVIFRENSEDIYAGIEWKADSADAEKVIKFLREEMGVKKIRFPEHCGIGIKPCSEEGTKRLVRAAIEYAIANDRDSVTLVHKGNIMKFTEGAFKDWGYQLAREEFGGELIDGGPWLKVKNPNTGKEIVIKDVIADAFLQQILLRPAEYDVIACMNLNGDYISDALAAQVGGIGIAPGANIGDECALFEATHGTAPKYAGQDKVNPGSIILSAEMMLRHMGWTEAADLIVKGMEGAINAKTVTYDFERLMDGAKLLKCSEFGDAIIENM | ||||||
Modified residue | 100 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 113 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 142 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 242 | N6-succinyllysine | ||||
Sequence: K |
Post-translational modification
Phosphorylation state of this enzyme is controlled by isocitrate dehydrogenase kinase/phosphatase (AceK).
Succinylation probably inhibits enzymatic activity.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Homodimer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P08200 | aceK P11071 | 5 | EBI-369069, EBI-1112800 |
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length416
- Mass (Da)45,757
- Last updated1988-08-01 v1
- Checksum9A02E707C3B4FDD9
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J02799 EMBL· GenBank· DDBJ | AAA24006.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC74220.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAA35958.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF017587 EMBL· GenBank· DDBJ | AAC45887.1 EMBL· GenBank· DDBJ | Genomic DNA |