Reviewed,
UniProtKB/Swiss-Prot Q04829 (DLDH_HALVO)
Last modified
June 16, 2009.
Version 70.
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 | ||||
| Gene names |
| ||||
| Organism | Halobacterium volcanii (Haloferax volcanii) | ||||
| Taxonomic identifier | 2246 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Haloferax |
Protein attributes
| Sequence length | 475 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| 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. |
| Subcellular location | |
| 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 | Direct protein sequencing |
| 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 |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.2 | ||||||||
| Chain | 2 – 475 | 474 | Dihydrolipoyl dehydrogenase | PRO_0000068058 | |||||||
Regions | |||||||||||
| Nucleotide binding | 39 – 47 | 9 | FAD By similarity | ||||||||
| Nucleotide binding | 186 – 190 | 5 | NAD By similarity | ||||||||
| Nucleotide binding | 275 – 278 | 4 | NAD By similarity | ||||||||
Sites | |||||||||||
| Active site | 451 | 1 | Proton acceptor By similarity | ||||||||
| Binding site | 56 | 1 | FAD By similarity | ||||||||
| Binding site | 118 | 1 | FAD; via amide nitrogen and carbonyl oxygen By similarity | ||||||||
| Binding site | 209 | 1 | NAD By similarity | ||||||||
| Binding site | 318 | 1 | FAD By similarity | ||||||||
| Binding site | 327 | 1 | FAD; via amide nitrogen By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 47 ↔ 52 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | "Dihydrolipoamide dehydrogenase from Haloferax volcanii: gene cloning, complete primary structure, and comparison to other dihydrolipoamide dehydrogenases." Vettakkorumakankav N.N., Stevenson K.J. Biochem. Cell Biol. 70:656-663(1992) [PubMed: 1339281] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 326-348. Strain: ATCC 29605 / DS2 / DSM 3757 / IFO 14742 / NCIMB 2012. |
| [2] | "Dihydrolipoamide dehydrogenase from the halophilic archaebacterium Haloferax volcanii: characterization and N-terminal sequence." Vettakkorumakankav N.N., Danson M.J., Hough D.W. Biochem. Cell Biol. 70:70-75(1992) [PubMed: 1581034] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-49. |
Cross-references
Sequence databases | |
|---|---|
| L09733 Genomic DNA. Translation: AAA72340.1. | |
| PIR | A56824. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1EBD based on UniProtKB P11959. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 1.8.1.4. 430. |
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_HALVO | ||||||||
| Accession | Primary (citable) accession number: Q04829 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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