P50214 · IDH_NOSS1

Function

function

Catalyzes the oxidative decarboxylation of isocitrate to 2-oxoglutarate and carbon dioxide with the concomitant reduction of NADP+.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Binds 1 Mg2+ or Mn2+ ion per subunit (By similarity).
Mn2+ is the most effective divalent cation in vitro, but the enzyme can also use Mg2+, Co2+ and Ni2+, with lower efficiency (PubMed:8169222).

Activity regulation

Inhibited by either oxaloacetate or glyoxylate (PubMed:8169222).
Also inhibited by the adenine nucleotides AMP, ADP and ATP and by NADPH, which inhibits the activity by 28% when it is added to the assay mixture at 0.25 mM (PubMed:8169222).

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
4.2 μMD,L-isocitratein the presence of Mn2+
61.2 μMD,L-isocitratein the presence of Mg2+
9.3 μMNADP+in the presence of Mn2+
13.6 μMNADP+in the presence of Mg2+

pH Dependence

Optimum pH is 8.5 (PubMed:8169222).
Shows 75% of maximal activity between pH 7.5 and 9.5 (PubMed:8169222).

Features

Showing features for binding site, site.

TypeIDPosition(s)Description
Binding site104NADP+ (UniProtKB | ChEBI)
Binding site113D-threo-isocitrate (UniProtKB | ChEBI)
Binding site115D-threo-isocitrate (UniProtKB | ChEBI)
Binding site119D-threo-isocitrate (UniProtKB | ChEBI)
Binding site129D-threo-isocitrate (UniProtKB | ChEBI)
Binding site153D-threo-isocitrate (UniProtKB | ChEBI)
Site160Critical for catalysis
Site237Critical for catalysis
Binding site362Mg2+ (UniProtKB | ChEBI)
Binding site394-400NADP+ (UniProtKB | ChEBI)
Binding site407NADP+ (UniProtKB | ChEBI)
Binding site446NADP+ (UniProtKB | ChEBI)
Binding site450NADP+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionisocitrate dehydrogenase (NADP+) activity
Molecular Functionmagnesium ion binding
Molecular FunctionNAD binding
Biological Processglyoxylate cycle
Biological Processtricarboxylic acid cycle

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Isocitrate dehydrogenase [NADP]
  • EC number
  • Short names
    IDH
  • Alternative names
    • IDP
    • NADP(+)-isocitrate dehydrogenase
      (NADP(+)-IDH
      )
    • NADP(+)-specific ICDH
    • Oxalosuccinate decarboxylase

Gene names

    • Name
      icd
    • Ordered locus names
      alr1827

Organism names

Accessions

  • Primary accession
    P50214

Proteomes

Phenotypes & Variants

Disruption phenotype

Essential, it cannot be deleted.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000835471-473Isocitrate dehydrogenase [NADP]

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    473
  • Mass (Da)
    52,228
  • Last updated
    1996-10-01 v1
  • Checksum
    D30941B992A38AAB
MYNKITPPTTGEKITFKNGEPVVPDNPIIPFIRGDGTGIDIWPATEKVLDAAVAKAYQGKRKISWFKVYAGDEACDLYGTYQYLPEDTLTAIREYGVAIKGPLTTPVGGGIRSLNVALRQIFDLYACVRPCRYYAGTPSPHKNPEKLDVIVYRENTEDIYLGIEWKQGSEIGDRLISILNKELIPATPEHGKKQIPLDSGIGIKPISKTGSQRLVRRAIKHALTLPKDKQQVTLVHKGNIMKYTEGAFRDWGYELATSEFRQETVTERESWILSNKEKNPNISLEDNARQIDPGFDALTPEKKAQIVKEVETVLNSIWESHGNGKWKEKVLVNDRIADSIFQQIQTRPDEYSILATMNLNGDYLSDAAAAIVGGLGMGPGANIGDSCAVFEATHGTAPKHAGLDRINPGSVILSGVMMLEYMGWQEAADLIKKGLSDAIANSQVTYDLARLLEPPVEPLKCSEFADAIIKHFG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X77654
EMBL· GenBank· DDBJ
CAA54734.1
EMBL· GenBank· DDBJ
Genomic DNA
BA000019
EMBL· GenBank· DDBJ
BAB73526.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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