Q6GGZ6 (ODO2_STAAR) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 70.
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 succinyltransferase component of 2-oxoglutarate dehydrogenase complex EC=2.3.1.61 Alternative name(s): 2-oxoglutarate dehydrogenase complex component E2 Short name=OGDC-E2 Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex | ||||||
| Gene names |
| ||||||
| Organism | Staphylococcus aureus (strain MRSA252) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 282458 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus › ![]() |
Protein attributes
| Sequence length | 423 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
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 three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity. |
| Catalytic activity | Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine. |
| Cofactor | Binds 1 lipoyl cofactor covalently By similarity. |
| Pathway | |
| 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 | Tricarboxylic acid cycle |
| Domain | Lipoyl |
| Molecular function | Acyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | L-lysine catabolic process to acetyl-CoA via saccharopine Inferred from electronic annotation. Source: UniProtKB-UniPathway tricarboxylic acid cycleInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | oxoglutarate dehydrogenase complex Inferred from electronic annotation. Source: InterPro |
| Molecular_function | dihydrolipoyllysine-residue succinyltransferase 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 – 423 | 423 | Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex | PRO_0000288100 | |||||
Regions | |||||||||
| Domain | 2 – 75 | 74 | Lipoyl-binding | ||||||
Sites | |||||||||
| Active site | 394 | 1 | By similarity | ||||||
| Active site | 398 | 1 | By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 42 | 1 | N6-lipoyllysine Potential | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance." Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C. Parkhill J.Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MRSA252. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX571856 Genomic DNA. Translation: CAG40421.1. |
| RefSeq | YP_040826.1. NC_002952.2. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1GHJ based on UniProtKB P20708. |
| ProteinModelPortal | Q6GGZ6. |
| SMR | Q6GGZ6. Positions 194-420. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 282458.SAR1424. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAG40421; CAG40421; SAR1424. |
| GeneID | 2859175. |
| KEGG | sar:SAR1424. |
| PATRIC | 19546392. VBIStaAur71814_1425. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0508. |
| HOGENOM | HOG000281563. |
| KO | K00658. |
| OMA | GQDIVYK. |
| ProtClustDB | PRK05704. |
Enzyme and pathway databases | |
| BioCyc | SAUR282458:GJA5-1425-MONOMER. |
| UniPathway | UPA00868; UER00840. |
Family and domain databases | |
| Gene3D | 3.30.559.10. 1 hit. 4.10.320.10. 1 hit. |
| InterPro | IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR000089. Biotin_lipoyl. IPR023213. CAT-like_dom. IPR004167. E3-bd. IPR011053. Single_hybrid_motif. IPR006255. SucB. [Graphical view] |
| Pfam | PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 1 hit. PF02817. E3_binding. 1 hit. [Graphical view] |
| SUPFAM | SSF51230. Hybrid_motif. 1 hit. |
| TIGRFAMs | TIGR01347. sucB. 1 hit. |
| PROSITE | PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ODO2_STAAR | ||||||||
| Accession | Primary (citable) accession number: Q6GGZ6 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
