P0A9P3 (DLDH_SHIFL) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 66.
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 Glycine cleavage system L protein | ||||
| Gene names |
| ||||
| Organism | Shigella flexneri [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 623 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella![]() |
Protein attributes
| Sequence length | 474 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Lipoamide dehydrogenase is a component of the glycine cleavage system as well as 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 | Acetylation 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 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||||
| Chain | 2 – 474 | 473 | Dihydrolipoyl dehydrogenase | PRO_0000068043 | |||||||
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 | |||||||||||
| Modified residue | 220 | 1 | N6-acetyllysine By similarity | ||||||||
| Disulfide bond | 45 ↔ 50 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157." Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. Yu J.Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 301 / Serotype 2a. |
| [2] | "Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T." Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R. Infect. Immun. 71:2775-2786(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700930 / 2457T / Serotype 2a. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE005674 Genomic DNA. Translation: AAN41777.2. AE014073 Genomic DNA. Translation: AAP15658.1. |
| RefSeq | NP_706070.2. NC_004337.2. NP_835853.1. NC_004741.1. |
3D structure databases | |
| ProteinModelPortal | P0A9P3. |
| SMR | P0A9P3. Positions 19-470. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 198214.SF0113. |
Proteomic databases | |
| PaxDb | P0A9P3. |
| PRIDE | P0A9P3. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAN41777; AAN41777; SF0113. AAP15658; AAP15658; S0115. |
| GeneID | 1024526. 1076547. |
| KEGG | sfl:SF0113. sfx:S0115. |
| PATRIC | 18701168. VBIShiFle31049_0126. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1249. |
| HOGENOM | HOG000276708. |
| KO | K00382. |
| 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_SHIFL | ||||||||
| Accession | Primary (citable) accession number: P0A9P3 Secondary accession number(s): P00391 | ||||||||
| 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
