Reviewed,
UniProtKB/Swiss-Prot Q6GAB8 (DLDH_STAAS)
Last modified
December 16, 2008.
Version 35.
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 pyruvate complex Membrane-bound ribosome protein complex 50 kDa subunit | ||||
| Gene names |
| ||||
| Organism | Staphylococcus aureus (strain MSSA476) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 282459 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 468 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Lipoamide dehydrogenase is a component 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 | CytoplasmPotential. Membrane; Peripheral membrane protein. |
| 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 Membrane |
| Domain | Redox-active center |
| Ligand | FAD Flavoprotein NAD |
| Molecular function | Oxidoreductase |
| 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: InterPro membraneInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | FAD binding Inferred from electronic annotation. Source: InterPro dihydrolipoyl dehydrogenase 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 – 468 | 468 | Dihydrolipoyl dehydrogenase | PRO_0000068048 | |||||||
Regions | |||||||||||
| Nucleotide binding | 39 – 47 | 9 | FAD By similarity | ||||||||
| Nucleotide binding | 183 – 187 | 5 | NAD By similarity | ||||||||
| Nucleotide binding | 271 – 274 | 4 | NAD By similarity | ||||||||
Sites | |||||||||||
| Active site | 446 | 1 | Proton acceptor By similarity | ||||||||
| Binding site | 56 | 1 | FAD By similarity | ||||||||
| Binding site | 119 | 1 | FAD; via amide nitrogen and carbonyl oxygen By similarity | ||||||||
| Binding site | 206 | 1 | NAD By similarity | ||||||||
| Binding site | 314 | 1 | FAD By similarity | ||||||||
| Binding site | 322 | 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] | "Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance." Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C. Parkhill J.Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004) [PubMed: 15213324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| BX571857 Genomic DNA. Translation: CAG42805.1. | |
| RefSeq | YP_043155.1. |
3D structure databases | |
| SMR | Q6GAB8. Positions 8-461. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2864342. |
| GenomeReviews | Gene locus SAS1031 in contig BX571857_GR. |
| KEGG | sas:SAS1031. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q6GAB8. |
Enzyme and pathway databases | |
| BioCyc | SAUR282459:SAS1031-MON. |
Family and domain databases | |
| InterPro | IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR000815. Hg_reductase. IPR006258. Lipoamide_DHase. IPR001100. Pyr_nuc-diS_OxRdtase. 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. PR00411. PNDRDTASEI. |
| 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_STAAS | ||||||||
| Accession | Primary (citable) accession number: Q6GAB8 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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