Reviewed,
UniProtKB/Swiss-Prot Q59985 (IDH_STRSL)
Last modified
June 16, 2009.
Version 50.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Isocitrate dehydrogenase [NADP] Short name=IDH EC=1.1.1.42 Alternative name(s): Oxalosuccinate decarboxylase NADP(+)-specific ICDH IDP | ||
| Gene names |
| ||
| Organism | Streptococcus salivarius | ||
| Taxonomic identifier | 1304 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus |
Protein attributes
| Sequence length | 391 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | Isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH. Oxalosuccinate + NADP+ = 2-oxoglutarate + CO2 + NADPH. |
| Cofactor | Binds 1 magnesium or manganese ion per subunit By similarity. |
| Subunit structure | Homodimer By similarity. |
| Sequence similarities | Belongs to the isocitrate and isopropylmalate dehydrogenases family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glyoxylate bypass Tricarboxylic acid cycle |
| Ligand | Magnesium Manganese Metal-binding NADP |
| Molecular function | Oxidoreductase |
| PTM | Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | glyoxylate cycle Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycleInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | NAD or NADH binding Inferred from electronic annotation. Source: InterPro isocitrate dehydrogenase (NADP+) activityInferred from electronic annotation. Source: EC magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW manganese ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 391 | 391 | Isocitrate dehydrogenase [NADP] | PRO_0000083569 | |||||
Sites | |||||||||
| Metal binding | 283 | 1 | Magnesium or manganese By similarity | ||||||
| Binding site | 102 | 1 | Substrate By similarity | ||||||
| Binding site | 104 | 1 | Substrate By similarity | ||||||
| Binding site | 108 | 1 | Substrate By similarity | ||||||
| Binding site | 118 | 1 | Substrate By similarity | ||||||
| Binding site | 142 | 1 | Substrate By similarity | ||||||
| Site | 149 | 1 | Critical for catalysis By similarity | ||||||
| Site | 219 | 1 | Critical for catalysis By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 102 | 1 | Phosphoserine By similarity | ||||||
Sequences
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References
| [1] | Desgagnes R., Gagnon G., Frenette M. Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 25975. |
Cross-references
Sequence databases | |
|---|---|
| L14780 Genomic DNA. Translation: AAA98355.1. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 1HQS based on UniProtKB P39126. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 1.1.1.42. 39093. |
Family and domain databases | |
| InterPro | IPR019818. IsoCit/isopropylmalate_DH_CS. IPR001804. Isocitrate/isopropylmalate_DH. IPR004439. Isocitrate_DH_NADP_prok. [Graphical view] |
| Gene3D | G3DSA:3.40.718.10. IDH_IMDH. 1 hit. |
| PANTHER | PTHR11835. IDH_IMDH_dimeric. 1 hit. PTHR11835:SF1. NADP_IDH_prok. 1 hit. |
| Pfam | PF00180. Iso_dh. 1 hit. [Graphical view] |
| PROSITE | PS00470. IDH_IMDH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | IDH_STRSL | ||||||||
| Accession | Primary (citable) accession number: Q59985 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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