Reviewed,
UniProtKB/Swiss-Prot O94230 (IDH2_KLULA)
Last modified
June 16, 2009.
Version 59.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Isocitrate dehydrogenase [NAD] subunit 2, mitochondrial EC=1.1.1.41 Alternative name(s): Isocitric dehydrogenase NAD(+)-specific ICDH | ||||
| Gene names |
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| Organism | Kluyveromyces lactis (Yeast) (Candida sphaerica) [Complete proteome] | ||||
| Taxonomic identifier | 28985 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces |
Protein attributes
| Sequence length | 368 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Performs an essential role in the oxidative function of the citric acid cycle By similarity. |
| Catalytic activity | Isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH. |
| Cofactor | Binds 1 magnesium or manganese ion per subunit By similarity. |
| Subunit structure | Octamer of two non-identical subunits IDH1 and IDH2 By similarity. |
| Subcellular location | Mitochondrion By similarity. |
| Sequence similarities | Belongs to the isocitrate and isopropylmalate dehydrogenases family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Tricarboxylic acid cycle |
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | Magnesium Manganese Metal-binding NAD |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycleInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | NAD or NADH binding Inferred from electronic annotation. Source: InterPro isocitrate dehydrogenase (NAD+) 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 14 | 14 | Mitochondrion By similarity | ||||||
| Chain | 15 – 368 | 354 | Isocitrate dehydrogenase [NAD] subunit 2, mitochondrial | PRO_0000014432 | |||||
Sites | |||||||||
| Metal binding | 236 | 1 | Magnesium or manganese By similarity | ||||||
| Metal binding | 262 | 1 | Magnesium or manganese By similarity | ||||||
| Metal binding | 266 | 1 | Magnesium or manganese By similarity | ||||||
| Binding site | 118 | 1 | Substrate By similarity | ||||||
| Binding site | 128 | 1 | Substrate By similarity | ||||||
| Binding site | 149 | 1 | Substrate By similarity | ||||||
| Binding site | 236 | 1 | Substrate By similarity | ||||||
| Site | 156 | 1 | Critical for catalysis By similarity | ||||||
| Site | 203 | 1 | Critical for catalysis By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Isolation and RNA-binding analysis of NAD+ -isocitrate dehydrogenases from Kluyveromyces lactis and Schizosaccharomyces pombe." Elzinga S.D.J., van Oosterum K., Maat C., Grivell L.A., van der Spek H. Curr. Genet. 38:87-94(2000) [PubMed: 10975257] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC MYA-539 / JBD100. |
| [2] | "Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.  Souciet J.-L.Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37. |
Cross-references
Sequence databases | |
|---|---|
| AF045154 Genomic DNA. Translation: AAC69609.1. CR382125 Genomic DNA. Translation: CAG99173.1. | |
| RefSeq | XP_454086.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1XAA based on UniProtKB P00351. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2894289. |
| KEGG | kla:KLLA0E03058g. |
Phylogenomic databases | |
| HOGENOM | O94230. |
| OMA | O94230. GGNSKCS. |
Enzyme and pathway databases | |
| BRENDA | 1.1.1.41. 74088. |
Family and domain databases | |
| InterPro | IPR019818. IsoCit/isopropylmalate_DH_CS. IPR001804. Isocitrate/isopropylmalate_DH. IPR004434. Isocitrate_DH_NAD_mit. [Graphical view] |
| Gene3D | G3DSA:3.40.718.10. IDH_IMDH. 1 hit. |
| PANTHER | PTHR11835. IDH_IMDH_dimeric. 1 hit. |
| Pfam | PF00180. Iso_dh. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00175. mito_nad_idh. 1 hit. |
| PROSITE | PS00470. IDH_IMDH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | IDH2_KLULA | ||||||||
| Accession | Primary (citable) accession number: O94230 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
