Reviewed,
UniProtKB/Swiss-Prot O00087 (DLDH_SCHPO)
Last modified
February 9, 2010.
Version 94.
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, mitochondrial EC=1.8.1.4 Alternative name(s): Dihydrolipoamide dehydrogenase Short name=DLDH | ||||
| Gene names |
| ||||
| Organism | Schizosaccharomyces pombe (Fission yeast) [Complete proteome] | ||||
| Taxonomic identifier | 4896 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces |
Protein attributes
| Sequence length | 511 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes By similarity. Malfunction of this protein blocks the progression of cell cycle from G1 to S phase. |
| 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 | Mitochondrion matrix Potential. |
| Miscellaneous | The active site is a redox-active disulfide bond. |
| Sequence similarities | Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Redox-active center Transit peptide |
| Ligand | FAD Flavoprotein NAD |
| Molecular function | Oxidoreductase |
| PTM | Disulfide bond |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | 2-oxoglutarate metabolic process Inferred by curator. Source: GeneDB_SPombe cell redox homeostasisInferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrial oxoglutarate dehydrogenase complex Inferred by curator. Source: GeneDB_SPombe |
| 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 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – ? | Mitochondrion | |||||||||
| Chain | ? – 511 | Dihydrolipoyl dehydrogenase, mitochondrial | PRO_0000030300 | ||||||||
Regions | |||||||||||
| Nucleotide binding | 75 – 84 | 10 | FAD By similarity | ||||||||
| Nucleotide binding | 187 – 189 | 3 | FAD By similarity | ||||||||
| Nucleotide binding | 224 – 231 | 8 | NAD By similarity | ||||||||
| Nucleotide binding | 363 – 366 | 4 | FAD By similarity | ||||||||
Sites | |||||||||||
| Active site | 489 | 1 | Proton acceptor By similarity | ||||||||
| Binding site | 93 | 1 | FAD By similarity | ||||||||
| Binding site | 157 | 1 | FAD; via amide nitrogen and carbonyl oxygen By similarity | ||||||||
| Binding site | 247 | 1 | NAD By similarity | ||||||||
| Binding site | 281 | 1 | NAD; via amide nitrogen and carbonyl oxygen By similarity | ||||||||
| Binding site | 316 | 1 | NAD; via amide nitrogen By similarity | ||||||||
| Binding site | 357 | 1 | FAD By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 84 ↔ 89 | Redox-active By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 210 – 216 | 7 | ALSLSEV → GPYLYQRY in AAB97089. Ref.1 | ||||||||
| Sequence conflict | 277 | 1 | T → R in AAB97089. Ref.1 | ||||||||
| Sequence conflict | 282 | 1 | L → V in AAB97089. Ref.1 | ||||||||
| Sequence conflict | 424 | 1 | P → G in AAB97089. Ref.1 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Fission yeast dihydrolipoamide dehydrogenase gene is involved in G1/S cell cycle progression." Jang Y.-J., Chung K.-S., Park C., Yoo H.-S. Biochim. Biophys. Acta 1358:229-239(1997) [PubMed: 9366254] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ATCC 38366 / 972. |
| [2] | "The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. Nurse P.Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L40360 mRNA. Translation: AAB97089.1. CU329670 Genomic DNA. Translation: CAB65609.1. |
| PIR | T43405. |
| RefSeq | NP_593496.1. |
3D structure databases | |
| SMR | O00087. Positions 43-510. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | O00087. |
Genome annotation databases | |
| GeneID | 2543269. |
| GenomeReviews | Gene locus dld1 in contig CU329670_GR. |
| KEGG | spo:SPAC1002.09c. |
| NMPDR | fig|4896.1.peg.3466. |
Organism-specific databases | |
| GeneDB_Spombe | SPAC1002.09c. |
Phylogenomic databases | |
| eggNOG | fuNOG07682. |
| HOGENOM | HBG515043. |
| OMA | FNRISHG. |
| OrthoDB | EOG900329. |
| PhylomeDB | O00087. |
Enzyme and pathway databases | |
| BRENDA | 1.8.1.4. 653. |
Gene expression databases | |
| ArrayExpress | O00087. |
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_SCHPO | ||||||||
| Accession | Primary (citable) accession number: O00087 Secondary accession number(s): Q9US50 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| Schizosaccharomyces pombe Schizosaccharomyces pombe: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with


