P86197 (ODP2_MESAU) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 13.
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: Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial EC=2.3.1.12 Alternative name(s): Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex Pyruvate dehydrogenase complex component E2 Short name=PDC-E2 Short name=PDCE2 | ||
| Gene names |
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| Organism | Mesocricetus auratus (Golden hamster) | ||
| Taxonomic identifier | 10036 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Mesocricetus![]() |
Protein attributes
| Sequence length | 219 AA. |
| Sequence status | Fragments. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2, and thereby links the glycolytic pathway to the tricarboxylic cycle By similarity. UniProtKB P08461 |
| Catalytic activity | Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine. UniProtKB P08461 |
| Cofactor | Binds 1 lipoyl cofactor covalently By similarity. UniProtKB P08461 |
| Subunit structure | Part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules. Interacts with PDK2 and PDK3 By similarity. |
| Subcellular location | Mitochondrion matrix By similarity UniProtKB P08461. |
| Tissue specificity | Detected at higher levels in cauda epididymal spermatazoa than in caput epididymal spermatazoa (at protein level). Ref.1 |
| Sequence similarities | Belongs to the 2-oxoacid dehydrogenase family. Contains 2 lipoyl-binding domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Glucose metabolism Tricarboxylic acid cycle |
| Cellular component | Mitochondrion |
| Domain | Lipoyl Repeat |
| Molecular function | Acyltransferase Transferase |
| Gene Ontology (GO) | |
| Biological_process | glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycleInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | dihydrolipoyllysine-residue acetyltransferase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | ‹1 – 219 | ›219 | Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial | PRO_0000394399 | |||||
Regions | |||||||||
| Domain | ‹1 – ›17 | ›17 | Lipoyl-binding 1 UniProtKB P08461 | ||||||
| Domain | ‹18 – 28 | ›11 | Lipoyl-binding 2 UniProtKB P08461 | ||||||
| Region | 37 – 57 | 21 | E3- and/or E1-component binding domain Potential UniProtKB P08461 | ||||||
| Region | 187 – 198 | 12 | CoA-binding By similarity UniProtKB P08461 | ||||||
Sites | |||||||||
| Active site | 192 | 1 | Potential UniProtKB P08461 | ||||||
| Active site | 196 | 1 | Potential UniProtKB P08461 | ||||||
Experimental info | |||||||||
| Non-adjacent residues | 17 – 18 | 2 | |||||||
| Non-adjacent residues | 31 – 32 | 2 | |||||||
| Non-adjacent residues | 40 – 41 | 2 | |||||||
| Non-adjacent residues | 55 – 56 | 2 | |||||||
| Non-adjacent residues | 63 – 64 | 2 | |||||||
| Non-adjacent residues | 121 – 122 | 2 | |||||||
| Non-terminal residue | 1 | 1 | |||||||
Sequences
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References
| [1] | "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen (GP96) are unique to hamster caput epididymal spermatozoa." Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S. Asian J. Androl. 12:344-355(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY. |
Cross-references
3D structure databases | |
|---|---|
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P86197. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| Gene3D | 3.30.559.10. 1 hit. 4.10.320.10. 1 hit. |
| InterPro | IPR001078. 2-oxoacid_DH_actylTfrase. IPR023213. CAT-like_dom. IPR004167. E3-bd. [Graphical view] |
| Pfam | PF00198. 2-oxoacid_dh. 1 hit. [Graphical view] |
| PROSITE | PS50968. BIOTINYL_LIPOYL. Partial match. PS00189. LIPOYL. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ODP2_MESAU | ||||||||
| Accession | Primary (citable) accession number: P86197 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
