O13285 (IDH1_CANTR) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 75.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Isocitrate dehydrogenase [NADP], mitochondrial Short name=IDH EC=1.1.1.42 Alternative name(s): CtIDP1 IDP NADP(+)-specific ICDH Oxalosuccinate decarboxylase | ||
| Gene names |
| ||
| Organism | Candida tropicalis (Yeast) | ||
| Taxonomic identifier | 5482 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida![]() |
Protein attributes
| Sequence length | 430 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 | Mitochondrial IDP1 may regulate flux through the tricarboxylic acid cycle and respiration. Its probably critical function is the production of NADPH. |
| Catalytic activity | Isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH. |
| Cofactor | Binds 1 magnesium or manganese ion per subunit By similarity. |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | |
| Sequence similarities | Belongs to the isocitrate and isopropylmalate dehydrogenases family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glyoxylate bypass Tricarboxylic acid cycle |
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | Magnesium Manganese Metal-binding NADP |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Biological_process | glyoxylate cycle Inferred from electronic annotation. Source: UniProtKB-KW isocitrate metabolic processInferred from electronic annotation. Source: InterPro tricarboxylic acid cycleInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | NAD binding Inferred from electronic annotation. Source: InterPro isocitrate dehydrogenase (NADP+) activityInferred from electronic annotation. Source: EC magnesium ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 27 | 27 | Mitochondrion By similarity | ||||||
| Chain | 28 – 430 | 403 | Isocitrate dehydrogenase [NADP], mitochondrial | PRO_0000014424 | |||||
Regions | |||||||||
| Nucleotide binding | 101 – 103 | 3 | NADP By similarity | ||||||
| Nucleotide binding | 335 – 340 | 6 | NADP By similarity | ||||||
| Region | 120 – 126 | 7 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Metal binding | 277 | 1 | Magnesium or manganese By similarity | ||||||
| Metal binding | 300 | 1 | Magnesium or manganese By similarity | ||||||
| Binding site | 103 | 1 | Substrate By similarity | ||||||
| Binding site | 108 | 1 | NADP By similarity | ||||||
| Binding site | 135 | 1 | Substrate By similarity | ||||||
| Binding site | 158 | 1 | Substrate By similarity | ||||||
| Binding site | 285 | 1 | NADP By similarity | ||||||
| Binding site | 353 | 1 | NADP; via amide nitrogen and carbonyl oxygen By similarity | ||||||
| Site | 165 | 1 | Critical for catalysis By similarity | ||||||
| Site | 237 | 1 | Critical for catalysis By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Immunochemically distinct NADP-linked isocitrate dehydrogenase isozymes in mitochondria and peroxisomes of Candida tropicalis." Imajo T., Kawachi H., Atomi H., Sanuki S., Yamamoto S., Ueda M., Tanaka A. Arch. Microbiol. 168:389-395(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 20336 / pK233 / NCYC 997. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB004556 Genomic DNA. Translation: BAA22945.1. |
3D structure databases | |
| ProteinModelPortal | O13285. |
| SMR | O13285. Positions 29-430. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | O13285. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| Gene3D | 3.40.718.10. 1 hit. |
| InterPro | IPR019818. IsoCit/isopropylmalate_DH_CS. IPR004790. Isocitrate_DH_NADP. IPR024084. IsoPropMal-DH-like_dom. [Graphical view] |
| PANTHER | PTHR11822. PTHR11822. 1 hit. |
| Pfam | PF00180. Iso_dh. 1 hit. [Graphical view] |
| PIRSF | PIRSF000108. IDH_NADP. 1 hit. |
| TIGRFAMs | TIGR00127. nadp_idh_euk. 1 hit. |
| PROSITE | PS00470. IDH_IMDH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | IDH1_CANTR | ||||||||
| Accession | Primary (citable) accession number: O13285 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
