P45302 (ODO2_HAEIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 104.
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 | Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 71421 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › ![]() |
Protein attributes
| Sequence length | 409 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 Reference 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 – 409 | 409 | Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex | PRO_0000162264 | |||||
Regions | |||||||||
| Domain | 1 – 76 | 76 | Lipoyl-binding | ||||||
Sites | |||||||||
| Active site | 380 | 1 | Potential | ||||||
| Active site | 384 | 1 | Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 43 | 1 | N6-lipoyllysine Potential | ||||||
Sequences
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References
| [1] | "Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. Venter J.C.Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L42023 Genomic DNA. Translation: AAC23307.1. |
| PIR | D64135. |
| RefSeq | NP_439803.1. NC_000907.1. |
3D structure databases | |
| ProteinModelPortal | P45302. |
| SMR | P45302. Positions 2-76, 111-153, 177-409. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 71421.HI1661. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAC23307; AAC23307; HI_1661. |
| GeneID | 950492. |
| KEGG | hin:HI1661. |
| PATRIC | 20192071. VBIHaeInf48452_1739. |
Phylogenomic databases | |
| eggNOG | COG0508. |
| KO | K00658. |
| OMA | AAMLTTY. |
| ProtClustDB | CLSK892422. |
Enzyme and pathway databases | |
| 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 | SSF47005. E3_bd. 1 hit. 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_HAEIN | ||||||||
| Accession | Primary (citable) accession number: P45302 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Haemophilus influenzae Haemophilus influenzae (strain Rd): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
