Reviewed,
UniProtKB/Swiss-Prot Q54EW8 (DLDH_DICDI)
Last modified
November 3, 2009.
Version 39.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
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 Glycine cleavage system L protein | ||||||
| Gene names |
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| Organism | Dictyostelium discoideum (Slime mold) [Complete proteome] | ||||||
| Taxonomic identifier | 44689 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium |
Protein attributes
| Sequence length | 488 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| Subcellular location | Cytoplasm Potential. |
| 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 | |
|---|---|
| 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 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 – 488 | 488 | Dihydrolipoyl dehydrogenase | PRO_0000327450 | |||||||
Regions | |||||||||||
| Nucleotide binding | 52 – 61 | 10 | FAD By similarity | ||||||||
| Nucleotide binding | 163 – 165 | 3 | FAD By similarity | ||||||||
| Nucleotide binding | 200 – 207 | 8 | NAD By similarity | ||||||||
| Nucleotide binding | 341 – 344 | 4 | FAD By similarity | ||||||||
Sites | |||||||||||
| Active site | 467 | 1 | Proton acceptor By similarity | ||||||||
| Binding site | 70 | 1 | FAD By similarity | ||||||||
| Binding site | 134 | 1 | FAD; via amide nitrogen and carbonyl oxygen By similarity | ||||||||
| Binding site | 223 | 1 | NAD By similarity | ||||||||
| Binding site | 257 | 1 | NAD; via amide nitrogen and carbonyl oxygen By similarity | ||||||||
| Binding site | 294 | 1 | NAD; via amide nitrogen By similarity | ||||||||
| Binding site | 335 | 1 | FAD By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 61 ↔ 66 | Redox-active By similarity | |||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. Kuspa A.Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4. |
| [2] | "A first glimpse into the pattern and scale of gene transfer in Apicomplexa." Huang J., Mullapudi N., Sicheritz-Ponten T., Kissinger J.C. Int. J. Parasitol. 34:265-274(2004) [PubMed: 15003488] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-357. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AAFI02000177 Genomic DNA. Translation: EAL61808.1. AY466389 Genomic DNA. Translation: AAS47709.1. | |
| RefSeq | XP_635122.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q54EW8. |
Genome annotation databases | |
| GeneID | 3386860. |
| GenomeReviews | Gene locus lpd in contig CM000155_GR. |
| KEGG | ddi:DDB_0216232. |
Organism-specific databases | |
| dictyBase | DDB_G0291648. lpd. |
Phylogenomic databases | |
| OMA | LAHGKDF. |
Enzyme and pathway databases | |
| BRENDA | 1.8.1.4. 424. |
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_DICDI | ||||||||
| Accession | Primary (citable) accession number: Q54EW8 Secondary accession number(s): Q6S4V6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| Dictyostelium discoideum Dictyostelium discoideum: entries, gene names and cross-references to dictyBase |
| SIMILARITY comments Index of protein domains and families |

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