Reviewed,
UniProtKB/Swiss-Prot P65635 (ODP2_STAAM)
Last modified
June 16, 2009.
Version 33.
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 EC=2.3.1.12 Alternative name(s): E2 Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex | ||||
| Gene names |
| ||||
| Organism | Staphylococcus aureus (strain Mu50 / ATCC 700699) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 158878 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 430 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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). |
| Catalytic activity | Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine. |
| Cofactor | Binds 1 lipoyl cofactor covalently By similarity. |
| Subunit structure | Forms a 24-polypeptide structural core with octahedral symmetry By similarity. |
| Sequence similarities | Belongs to the 2-oxoacid dehydrogenase family. Contains 1 lipoyl-binding domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Domain | Lipoyl |
| Molecular function | Acyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | glycolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 430 | 430 | Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex | PRO_0000162288 | |||||
Regions | |||||||||
| Domain | 1 – 76 | 76 | Lipoyl-binding | ||||||
Sites | |||||||||
| Active site | 401 | 1 | Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 43 | 1 | N6-lipoyllysine By similarity | ||||||
Sequences
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References
| [1] | "Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. Hiramatsu K.Lancet 357:1225-1240(2001) [PubMed: 11418146] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| BA000017 Genomic DNA. Translation: BAB57257.1. | |
| RefSeq | NP_371619.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 2PDE based on UniProtKB P11961. |
| SMR | P65635. Positions 2-79, 121-165. |
| ModBase | Search... |
2-D gel databases | |
| World-2DPAGE | 0002:P65635. |
Genome annotation databases | |
| GeneID | 1121072. |
| GenomeReviews | Gene locus SAV1095 in contig BA000017_GR. |
| KEGG | sav:SAV1095. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P65635. |
| OMA | P65635. YKHYFNI. |
Enzyme and pathway databases | |
| BioCyc | SAUR158878:SAV1095-MON. |
Family and domain databases | |
| InterPro | IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR000089. Biotin_lipoyl. IPR004167. E3_bd. [Graphical view] |
| Gene3D | G3DSA:4.10.320.10. E3_bd. 1 hit. |
| 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] |
| PROSITE | PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ODP2_STAAM | ||||||||
| Accession | Primary (citable) accession number: P65635 Secondary accession number(s): Q99V06 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


