Reviewed,
UniProtKB/Swiss-Prot P41565 (IDH3G_RAT)
Last modified
November 25, 2008.
Version 69.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial EC=1.1.1.41 Alternative name(s): Isocitric dehydrogenase NAD(+)-specific ICDH | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 393 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Catalytic activity | Isocitrate + NAD(+) = 2-oxoglutarate + CO(2) + NADH. |
| Cofactor | Binds 1 magnesium or manganese ion per subunit By similarity. |
| Enzyme regulation | Activated by increasing ADP/ATP ratios and by Ca(2+). |
| Subunit structure | Heterooligomer of subunits alpha, beta, and gamma in the apparent ratio of 2:1:1. |
| Subcellular location | |
| Sequence similarities | Belongs to the isocitrate and isopropylmalate dehydrogenases family. |
Ontologies
Keywords | |
|---|---|
| Biological process | Tricarboxylic acid cycle |
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | ATP-binding Magnesium Manganese Metal-binding NAD Nucleotide-binding |
| Molecular function | Oxidoreductase |
| PTM | Phosphoprotein |
Gene Ontology (GO) | |
| Biological process | isocitrate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycleInferred from electronic annotation. Source: InterPro |
| Cellular component | mitochondrion Inferred from sequence or structural similarity. Source: UniProtKB |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW isocitrate dehydrogenase (NAD+) activityInferred from sequence or structural similarity. Source: UniProtKB 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 – 39 | 39 | Mitochondrion By similarity | ||||||
| Chain | 40 – 393 | 354 | Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial | PRO_0000014452 | |||||
Regions | |||||||||
| Nucleotide binding | 56 – 84 | 29 | NAD Potential | ||||||
| Nucleotide binding | 309 – 316 | 8 | ATP Potential | ||||||
Sites | |||||||||
| Metal binding | 254 | 1 | Magnesium or manganese By similarity | ||||||
| Binding site | 136 | 1 | Substrate By similarity | ||||||
| Binding site | 167 | 1 | Substrate By similarity | ||||||
| Binding site | 254 | 1 | Substrate By similarity | ||||||
| Site | 174 | 1 | Critical for catalysis By similarity | ||||||
| Site | 221 | 1 | Critical for catalysis By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 363 | 1 | Phosphothreonine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 7 | 1 | I → V in CAA52225. Ref.2 | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Genomic organization of two novel genes on human Xq28: compact head to head arrangement of IDH gamma and TRAP delta is conserved in rat and mouse." Brenner V., Nyakatura G., Rosenthal A., Platzer M. Genomics 44:8-14(1997) [PubMed: 9286695] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24. Strain: HAN/WIST. |
| [2] | "Molecular cloning and deduced amino acid sequences of the gamma-subunits of rat and monkey NAD(+)-isocitrate dehydrogenases." Nichols B.J., Hall L., Perry A.C.F., Denton R.M. Biochem. J. 295:347-350(1993) [PubMed: 8240232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 6-393. Strain: Wistar. Tissue: Epididymis. |
Cross-references
Sequence databases | |
|---|---|
| U63009 Genomic DNA. Translation: AAC53341.1. X74125 mRNA. Translation: CAA52225.1. | |
| PIR | S39064. |
| UniGene | Rn.2837 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1OSJ based on UniProtKB P00351. |
| ModBase | Search... |
Genome annotation databases | |
| Ensembl | ENSRNOG00000037284. Rattus norvegicus. [Contig view] |
Organism-specific databases | |
| RGD | 2863. Idh3g. |
Phylogenomic databases | |
| HOVERGEN | P41565. |
Gene expression databases | |
| ArrayExpress | P41565. |
| GermOnline | ENSRNOG00000037284. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR004434. IsoCit_DHase_NAD_mit. IPR001804. IsoCit_IM_DHase. [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 | IDH3G_RAT | ||||||||
| Accession | Primary (citable) accession number: P41565 Secondary accession number(s): P70577 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


