Q89AQ8 (DLDH_BUCBP) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 82.
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: Dihydrolipoyl dehydrogenase EC=1.8.1.4 Alternative name(s): Dihydrolipoamide dehydrogenase E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes | ||||
| Gene names |
| ||||
| Organism | Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 224915 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › ![]() |
Protein attributes
| Sequence length | 475 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes By similarity. |
| Catalytic activity | Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH. |
| Cofactor | Binds 1 FAD per subunit By similarity. |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Miscellaneous | The active site is a redox-active disulfide bond By similarity. |
| Sequence similarities | Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Cytoplasm |
| Domain | Redox-active center |
| Ligand | FAD Flavoprotein NAD |
| Molecular function | Oxidoreductase |
| PTM | Disulfide bond |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro glycolysisInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | dihydrolipoyl dehydrogenase activity Inferred from electronic annotation. Source: EC flavin adenine dinucleotide 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 – 475 | 475 | Dihydrolipoyl dehydrogenase | PRO_0000068021 | |||||||
Regions | |||||||||||
| Nucleotide binding | 37 – 46 | 10 | FAD By similarity | ||||||||
| Nucleotide binding | 183 – 187 | 5 | NAD By similarity | ||||||||
| Nucleotide binding | 272 – 275 | 4 | NAD By similarity | ||||||||
Sites | |||||||||||
| Active site | 447 | 1 | Proton acceptor By similarity | ||||||||
| Binding site | 55 | 1 | FAD By similarity | ||||||||
| Binding site | 118 | 1 | FAD; via amide nitrogen and carbonyl oxygen By similarity | ||||||||
| Binding site | 206 | 1 | NAD By similarity | ||||||||
| Binding site | 239 | 1 | NAD; via amide nitrogen By similarity | ||||||||
| Binding site | 315 | 1 | FAD By similarity | ||||||||
| Binding site | 323 | 1 | FAD; via amide nitrogen By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 46 ↔ 51 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | "Reductive genome evolution in Buchnera aphidicola." van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A. Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bp. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE016826 Genomic DNA. Translation: AAO26923.1. |
| RefSeq | NP_777818.1. NC_004545.1. |
3D structure databases | |
| ProteinModelPortal | Q89AQ8. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 224915.bbp191. |
Proteomic databases | |
| PRIDE | Q89AQ8. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAO26923; AAO26923; bbp_191. |
| GeneID | 1058236. |
| KEGG | bab:bbp191. |
| PATRIC | 21245157. VBIBucAph80364_0185. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1249. |
| KO | K00382. |
| OMA | FAHKAYA. |
Enzyme and pathway databases | |
| BioCyc | BAPH224915:GJ9D-191-MONOMER. |
Family and domain databases | |
| Gene3D | 3.30.390.30. 1 hit. |
| InterPro | IPR016156. FAD/NAD-linked_Rdtase_dimer. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR006258. Lipoamide_DH. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD. IPR012999. Pyr_OxRdtase_I_AS. IPR001327. Pyr_OxRdtase_NAD-bd_dom. [Graphical view] |
| PANTHER | PTHR22912:SF20. PTHR22912:SF20. 1 hit. |
| Pfam | PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view] |
| PRINTS | PR00368. FADPNR. |
| SUPFAM | SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit. |
| TIGRFAMs | TIGR01350. lipoamide_DH. 1 hit. |
| PROSITE | PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DLDH_BUCBP | ||||||||
| Accession | Primary (citable) accession number: Q89AQ8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
