Reviewed,
UniProtKB/Swiss-Prot O50286 (DLDH_VIBPA)
Last modified
November 3, 2009.
Version 76.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names 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 parahaemolyticus [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 670 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio |
Protein attributes
| Sequence length | 475 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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 |
| Gene Ontology (GO) | |
| Biological process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro glycolysisInferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | FAD binding Inferred from electronic annotation. Source: InterPro dihydrolipoyl dehydrogenase activityInferred from electronic annotation. Source: EC electron carrier activityInferred 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_0000068053 | |||||||
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 | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 160 | 1 | P → S in AAC46405. Ref.1 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "OpaR, a homolog of Vibrio harveyi LuxR, controls opacity of Vibrio parahaemolyticus." McCarter L.L. J. Bacteriol. 180:3166-3173(1998) [PubMed: 9620967] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BB22. |
| [2] | "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae." Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T. Lancet 361:743-749(2003) [PubMed: 12620739] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RIMD 2210633 / Serotype O3:K6. |
Cross-references
Sequence databases | |
|---|---|
| AF035967 Genomic DNA. Translation: AAC46405.1. BA000031 Genomic DNA. Translation: BAC60780.1. | |
| RefSeq | NP_798896.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1OJT based on UniProtKB Q51225. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1190032. |
| GenomeReviews | Gene locus VP2517 in contig BA000031_GR. |
| KEGG | vpa:VP2517. |
| NMPDR | fig|223926.1.peg.2517. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | O50286. |
| OMA | PFIPEDP. |
Enzyme and pathway databases | |
| BioCyc | VPAR223926:VP2517-MON. |
| BRENDA | 1.8.1.4. 3063. |
Family and domain databases | |
| InterPro | IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR000815. Hg_reductase. IPR006258. Lipoamide_DH. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR012999. Pyr_OxRdtase_I_AS. IPR001327. Pyr_OxRdtase_NAD_bd. [Graphical view] |
| Gene3D | G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit. |
| PANTHER | PTHR22912:SF20. Lipoamide_DH. 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. PR00945. HGRDTASE. |
| ProDom | PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR01350. lipoamide_DH. 1 hit. |
| PROSITE | PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DLDH_VIBPA | ||||||||
| Accession | Primary (citable) accession number: O50286 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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