Reviewed,
UniProtKB/Swiss-Prot P20285 (ODP2_NEUCR)
Last modified
September 1, 2009.
Version 87.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
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 MRP3 | ||||
| Gene names |
| ||||
| Organism | Neurospora crassa [Complete proteome] | ||||
| Taxonomic identifier | 5141 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora |
Protein attributes
| Sequence length | 458 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 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). Ref.3 |
| Catalytic activity | Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine. |
| Cofactor | Binds 1 lipoyl cofactor covalently By similarity. |
| Subcellular location | |
| Miscellaneous | The E2 component contains covalently-bound lipoyl cofactors and it participates in the generation of acetyl groups from hydroxyethyl-thiamine pyrophosphate-E1 and their transfer to coenzyme A. |
| Sequence similarities | Belongs to the 2-oxoacid dehydrogenase family. Contains 1 lipoyl-binding domain. |
| Caution | Was originally (Ref.1) thought to be a ribosomal protein. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Mitochondrion |
| Domain | Lipoyl Transit peptide |
| Molecular function | Acyltransferase Transferase |
| Technical term | Complete proteome Direct protein sequencing |
| 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 – 28 | 28 | Mitochondrion Ref.1 | ||||||
| Chain | 29 – 458 | 430 | Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial | PRO_0000020481 | |||||
Regions | |||||||||
| Domain | 35 – 109 | 75 | Lipoyl-binding | ||||||
Sites | |||||||||
| Active site | 431 | 1 | Potential | ||||||
| Active site | 435 | 1 | Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 75 | 1 | N6-lipoyllysine By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "A mitochondrial protein from Neurospora crassa detected both on ribosomes and in membrane fractions. Analysis of the gene, the message, and the protein." Kreader C.A., Langer C.S., Heckman J.E. J. Biol. Chem. 264:317-327(1989) [PubMed: 2521217] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 29-50. |
| [2] | "The genome sequence of the filamentous fungus Neurospora crassa." Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. Birren B.W.Nature 422:859-868(2003) [PubMed: 12712197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987. |
| [3] | "Sequence similarities within the family of dihydrolipoamide acyltransferases and discovery of a previously unidentified fungal enzyme." Russel G.C., Guest J.R. Biochim. Biophys. Acta 1076:225-232(1991) [PubMed: 1825611] [Abstract] Cited for: PROBABLE FUNCTION. |
Cross-references
Sequence databases | |
|---|---|
| J04432 Genomic DNA. Translation: AAA60452.1. AABX02000043 Genomic DNA. Translation: EAA33550.1. | |
| PIR | A30775. |
| RefSeq | XP_962786.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1FYC based on UniProtKB P10515. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P20285. |
Genome annotation databases | |
| GeneID | 3878934. |
| KEGG | ncr:NCU07659. |
| NMPDR | fig|5141.1.peg.6298. |
| UCSC | E03G2.2. c. elegans. |
Enzyme and pathway databases | |
| BioCyc | NCRA-XX3-01:NCRA-XX3-01-002518-MON. |
| BRENDA | 2.3.1.12. 266. |
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] |
| Pfam | PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 1 hit. PF02817. E3_binding. 1 hit. [Graphical view] |
| ProDom | PD001115. 2Oxoacid_dh. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR01349. PDHac_trf_mito. 1 hit. |
| PROSITE | PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ODP2_NEUCR | ||||||||
| Accession | Primary (citable) accession number: P20285 Secondary accession number(s): Q7RVH2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||

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