Reviewed,
UniProtKB/Swiss-Prot P36413 (ODP2_DICDI)
Last modified
June 16, 2009.
Version 71.
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 acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial EC=2.3.1.12 Alternative name(s): Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex PDC-E2 Short name=E2 | ||||||
| Gene names |
| ||||||
| Organism | Dictyostelium discoideum (Slime mold) [Complete proteome] | ||||||
| Taxonomic identifier | 44689 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium |
Protein attributes
| Sequence length | 635 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)
| Function | The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). |
| Catalytic activity | Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine. |
| Cofactor | Binds 2 lipoyl cofactors covalently By similarity. |
| Subunit structure | 20 to 30 alpha(2)-beta2 tetramers of E1 + 6 homodimers of E3 + 60 copies of E2. |
| Subcellular location | |
| Sequence similarities | Belongs to the 2-oxoacid dehydrogenase family. Contains 2 lipoyl-binding domains. |
| Sequence caution | The sequence AAA16511.1 differs from that shown. Reason: Frameshift at positions 577 and 585. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Mitochondrion |
| Domain | Lipoyl Repeat Transit peptide |
| Molecular function | Acyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | glycolysis Inferred from electronic annotation. Source: UniProtKB-KW pyruvate metabolic processInferred from electronic annotation. Source: InterPro |
| Cellular component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell pyruvate dehydrogenase complexInferred from electronic annotation. Source: InterPro |
| Molecular function | dihydrolipoyllysine-residue acetyltransferase activity Inferred from electronic annotation. Source: EC lipoic acid bindingInferred from electronic annotation. Source: UniProtKB-KW protein 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 – ? | Mitochondrion | |||||||
| Chain | ? – 635 | Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial | PRO_0000020480 | ||||||
Regions | |||||||||
| Domain | 84 – 159 | 76 | Lipoyl-binding 1 | ||||||
| Domain | 207 – 282 | 76 | Lipoyl-binding 2 | ||||||
| Region | 340 – 379 | 40 | E3-binding site By similarity | ||||||
| Region | 403 – 635 | 233 | Catalytic By similarity | ||||||
| Compositional bias | 301 – 314 | 14 | Ser/Thr-rich (hinge) | ||||||
Amino acid modifications | |||||||||
| Modified residue | 124 | 1 | N6-lipoyllysine By similarity | ||||||
| Modified residue | 247 | 1 | N6-lipoyllysine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 97 | 1 | E → V in AAA16511. Ref.2 | ||||||
| Sequence conflict | 118 | 1 | A → R in AAA16511. Ref.2 | ||||||
| Sequence conflict | 129 – 130 | 2 | FQ → S in AAA16511. Ref.2 | ||||||
| Sequence conflict | 472 – 473 | 2 | AA → LP in AAA16511. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. Kuspa A.Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4. |
| [2] | "Dihydrolipoamide transacetylase gene from Dictyostelium discoideum." Mueller-Taubenberger A. Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 43-635. Strain: AX2. |
Cross-references
Sequence databases | |
|---|---|
| AAFI02000023 Genomic DNA. Translation: EAL68096.1. U06634 mRNA. Translation: AAA16511.1. Frameshift. | |
| RefSeq | XP_642438.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1FYC based on UniProtKB P10515. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3393169. |
| KEGG | ddi:DDB_0215387. |
Organism-specific databases | |
| dictyBase | DDB_G0277847. pdhC. |
Phylogenomic databases | |
| OMA | P36413. ISNLGMN. |
Enzyme and pathway databases | |
| BRENDA | 2.3.1.12. 424. |
Family and domain databases | |
| InterPro | IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR006257. AcTrfase_Pyrv_DH_cplx_L. IPR000089. Biotin_lipoyl. IPR004167. E3_bd. [Graphical view] |
| Gene3D | G3DSA:4.10.320.10. E3_bd. 2 hits. |
| Pfam | PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 2 hits. PF02817. E3_binding. 1 hit. [Graphical view] |
| ProDom | PD001115. 2Oxoacid_dh. 2 hits. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR01349. PDHac_trf_mito. 1 hit. |
| PROSITE | PS50968. BIOTINYL_LIPOYL. 2 hits. PS00189. LIPOYL. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ODP2_DICDI | ||||||||
| Accession | Primary (citable) accession number: P36413 Secondary accession number(s): Q54XW4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| Dictyostelium discoideum Dictyostelium discoideum: entries, gene names and cross-references to dictyBase |
| SIMILARITY comments Index of protein domains and families |

Clusters with


