Reviewed,
UniProtKB/Swiss-Prot Q9HN74 (DLDH_HALSA)
Last modified
February 9, 2010.
Version 62.
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 salinarium (Halobacterium halobium) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 2242 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Halobacterium |
Protein attributes
| Sequence length | 474 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
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 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 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 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 474 | 474 | Dihydrolipoyl dehydrogenase | PRO_0000068057 | |||||||
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 | 450 | 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 | 326 | 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] | "Genome sequence of Halobacterium species NRC-1." Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D., Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D., Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K. DasSarma S.Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000) [PubMed: 11016950] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700922 / JCM 11081 / NRC-1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE004437 Genomic DNA. Translation: AAG20347.1. |
| PIR | G84372. |
| RefSeq | NP_280867.1. |
3D structure databases | |
| SMR | Q9HN74. Positions 7-465. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1448649. |
| GenomeReviews | Gene locus VNG_2220G in contig AE004437_GR. |
| KEGG | hal:VNG2220G. |
| NMPDR | fig|64091.1.peg.1893. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG515043. |
| OMA | ETVVIAT. |
Enzyme and pathway databases | |
| BioCyc | HSP64091:VNG2220G-MONOMER. |
| BRENDA | 1.8.1.4. 141893. |
Family and domain databases | |
| InterPro | IPR016156. FAD/NAD-linked_Rdtase_dimer. 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. |
| TIGRFAMs | TIGR01350. lipoamide_DH. 1 hit. |
| PROSITE | PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DLDH_HALSA | ||||||||
| Accession | Primary (citable) accession number: Q9HN74 | ||||||||
| 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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