Reviewed,
UniProtKB/Swiss-Prot Q01205 (ODO2_RAT)
Last modified
June 16, 2009.
Version 89.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial EC=2.3.1.61 Alternative name(s): Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex Short name=E2 E2K | ||
| 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 | 454 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3). |
| Catalytic activity | Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine. |
| Cofactor | Binds 1 lipoyl cofactor covalently. |
| Pathway | |
| Subunit structure | Forms a 24-polypeptide structural core with octahedral symmetry. |
| Subcellular location | |
| Sequence similarities | Belongs to the 2-oxoacid dehydrogenase family. Contains 1 lipoyl-binding domain. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 68 | 68 | Mitochondrion Ref.2 Ref.3 | ||||||
| Chain | 69 – 454 | 386 | Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial | PRO_0000020475 | |||||
Regions | |||||||||
| Domain | 72 – 144 | 73 | Lipoyl-binding | ||||||
Sites | |||||||||
| Active site | 425 | 1 | Potential | ||||||
| Active site | 429 | 1 | Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 111 | 1 | N6-lipoyllysine Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 13 | 1 | S → M in BAA14397. Ref.2 | ||||||
| Sequence conflict | 52 – 54 | 3 | NSS → TVA in BAA14397. Ref.2 | ||||||
| Sequence conflict | 164 | 1 | Y → H in BAA14397. Ref.2 | ||||||
| Sequence conflict | 281 | 1 | F → L in BAA14397. Ref.2 | ||||||
| Sequence conflict | 448 | 1 | R → A in BAA14397. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung. |
| [2] | "Purification and molecular cloning of succinyltransferase of the rat alpha-ketoglutarate dehydrogenase complex. Absence of a sequence motif of the putative E3 and/or E1 binding site." Nakano K., Matuda S., Yamanaka T., Tsubouchi H., Nakagawa S., Titani K., Ohta S., Miyata T. J. Biol. Chem. 266:19013-19017(1991) [PubMed: 1918017] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-454, PROTEIN SEQUENCE OF 69-83. Tissue: Heart. |
| [3] | Lubec G., Chen W.-Q., Afjehi-Sadat L., Diao W. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 69-89; 135-145; 262-308 AND 314-326, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus and Spinal cord. |
Cross-references
Sequence databases | |
|---|---|
| BC083858 mRNA. Translation: AAH83858.1. D90401 mRNA. Translation: BAA14397.1. | |
| IPI | IPI00551702. |
| PIR | A41015. |
| RefSeq | NP_001006982.2. |
| UniGene | Rn.99702 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1C4T based on UniProtKB P07016. |
| ModBase | Search... |
Genome annotation databases | |
| Ensembl | ENSRNOG00000005061. Rattus norvegicus. [Contig view] |
| GeneID | 299201. |
| KEGG | rno:299201. |
Organism-specific databases | |
| RGD | 1359615. Dlst. |
Phylogenomic databases | |
| HOVERGEN | Q01205. |
Enzyme and pathway databases | |
| BRENDA | 2.3.1.61. 248. |
Gene expression databases | |
| ArrayExpress | Q01205. |
| GermOnline | ENSRNOG00000005061. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR000089. Biotin_lipoyl. IPR006255. SucB. [Graphical view] |
| Pfam | PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 1 hit. [Graphical view] |
| ProDom | PD001115. 2Oxoacid_dh. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR01347. sucB. 1 hit. |
| PROSITE | PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 644993. |
Entry information
| Entry name | ODO2_RAT | ||||||||
| Accession | Primary (citable) accession number: Q01205 Secondary accession number(s): Q5XI35 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


