Q9KPF6 (DLDH_VIBCH) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 94.
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 2-oxoglutarate dehydrogenase complex | ||||
| Gene names |
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| Organism | Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 243277 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio › ![]() |
Protein attributes
| Sequence length | 475 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity. |
| Catalytic activity | Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH. |
| Cofactor | Binds 1 FAD per subunit By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Miscellaneous | The active site is a redox-active disulfide bond. |
| 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 Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | acetyl-CoA biosynthetic process from pyruvate Inferred from sequence or structural similarity Ref.1. Source: TIGR cell redox homeostasisInferred from electronic annotation. Source: InterPro glycolysisInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | cytosolic pyruvate dehydrogenase complex Inferred from sequence or structural similarity Ref.1. Source: TIGR |
| Molecular_function | dihydrolipoyl dehydrogenase activity Inferred from sequence or structural similarity Ref.1. Source: TIGR 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_0000068052 | |||||||
Regions | |||||||||||
| Nucleotide binding | 36 – 45 | 10 | FAD By similarity | ||||||||
| Nucleotide binding | 182 – 186 | 5 | NAD By similarity | ||||||||
| Nucleotide binding | 270 – 273 | 4 | NAD By similarity | ||||||||
Sites | |||||||||||
| Active site | 445 | 1 | Proton acceptor By similarity | ||||||||
| Binding site | 54 | 1 | FAD By similarity | ||||||||
| Binding site | 117 | 1 | FAD; via amide nitrogen and carbonyl oxygen By similarity | ||||||||
| Binding site | 205 | 1 | NAD By similarity | ||||||||
| Binding site | 238 | 1 | NAD; via amide nitrogen By similarity | ||||||||
| Binding site | 313 | 1 | FAD By similarity | ||||||||
| Binding site | 321 | 1 | FAD; via amide nitrogen By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 45 ↔ 50 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | "DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae." Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S. Fraser C.M.Nature 406:477-483(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39315 / El Tor Inaba N16961. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE003852 Genomic DNA. Translation: AAF95555.1. |
| PIR | B82079. |
| RefSeq | NP_232042.1. NC_002505.1. |
3D structure databases | |
| ProteinModelPortal | Q9KPF6. |
| SMR | Q9KPF6. Positions 19-470. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 243277.VC2412. |
Proteomic databases | |
| PRIDE | Q9KPF6. |
Protocols and materials databases | |
| DNASU | 2613081. |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAF95555; AAF95555; VC_2412. |
| GeneID | 2613081. |
| KEGG | vch:VC2412. |
| PATRIC | 20083841. VBIVibCho83274_2295. |
Phylogenomic databases | |
| eggNOG | COG1249. |
| KO | K00382. |
| OMA | GMAAEIY. |
| ProtClustDB | PRK06467. |
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_VIBCH | ||||||||
| Accession | Primary (citable) accession number: Q9KPF6 | ||||||||
| 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
