Reviewed,
UniProtKB/Swiss-Prot P0A9P0 (DLDH_ECOLI)
Last modified
June 16, 2009.
Version 44.
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 E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes Glycine cleavage system L protein | ||||||
| Gene names |
| ||||||
| Organism | Escherichia coli (strain K12) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 83333 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 474 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)
| Function | Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. |
| 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 | Cytoplasm. Cell inner membrane; Peripheral membrane protein. Ref.7 |
| 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 | Cell inner membrane Cell membrane Cytoplasm Membrane |
| Domain | Redox-active center |
| Ligand | FAD Flavoprotein NAD |
| Molecular function | Oxidoreductase |
| PTM | Acetylation Disulfide bond |
| Technical term | Complete proteome 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 | cytosol Inferred from direct assay. Source: UniProtKB plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | FAD binding Inferred from electronic annotation. Source: InterPro dihydrolipoyl dehydrogenase activityInferred from electronic annotation. Source: EC protein bindingInferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| idnD | P39346 | 1 | EBI-542856,EBI-552913 | |
| uvrD | P03018 | 1 | EBI-542856,EBI-559573 | |
| ybaK | P0AAR3 | 1 | EBI-542856,EBI-559987 | |
| ycgE | P75989 | 1 | EBI-542856,EBI-560582 | |
| ydjF | P77721 | 1 | EBI-542856,EBI-545197 | |
| ygfF | P52037 | 1 | EBI-542856,EBI-561028 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.5 | ||||||||
| Chain | 2 – 474 | 473 | Dihydrolipoyl dehydrogenase | PRO_0000068027 | |||||||
Regions | |||||||||||
| Nucleotide binding | 36 – 45 | 10 | FAD By similarity | ||||||||
| Nucleotide binding | 182 – 186 | 5 | NAD By similarity | ||||||||
| Nucleotide binding | 270 – 273 | 4 | NAD By similarity | ||||||||
Sites | |||||||||||
| Active site | 445 | 1 | Proton acceptor By similarity | ||||||||
| Binding site | 54 | 1 | FAD By similarity | ||||||||
| Binding site | 117 | 1 | FAD; via amide nitrogen and carbonyl oxygen By similarity | ||||||||
| Binding site | 205 | 1 | NAD By similarity | ||||||||
| Binding site | 238 | 1 | NAD; via amide nitrogen By similarity | ||||||||
| Binding site | 313 | 1 | FAD By similarity | ||||||||
| Binding site | 321 | 1 | FAD; via amide nitrogen By similarity | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 220 | 1 | N6-acetyllysine Ref.8 | ||||||||
| Disulfide bond | 45 ↔ 50 | Redox-active By similarity | |||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Nucleotide sequence of the lipoamide dehydrogenase gene of Escherichia coli K12." Stephens P.E., Lewis H.M., Darlison M.G., Guest J.R. Eur. J. Biochem. 135:519-527(1983) [PubMed: 6352260] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Fujita N., Mori H., Yura T., Ishihama A. Nucleic Acids Res. 22:1637-1639(1994) [PubMed: 8202364] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [3] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [4] | "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [5] | "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Strain: K12 / EMG2. |
| [6] | "The lpd gene product functions as the L protein in the Escherichia coli glycine cleavage enzyme system." Steiert P.S., Stauffer L.T., Stauffer G.V. J. Bacteriol. 172:6142-6144(1990) [PubMed: 2211531] [Abstract] Cited for: INVOLVEMENT IN GLYCINE CLEAVAGE SYSTEM. |
| [7] | "Protein complexes of the Escherichia coli cell envelope." Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O. J. Biol. Chem. 280:34409-34419(2005) [PubMed: 16079137] [Abstract] Cited for: SUBCELLULAR LOCATION. Strain: BL21-DE3. |
| [8] | "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-220, MASS SPECTROMETRY. |
Cross-references
Sequence databases | |
|---|---|
| V01498 Genomic DNA. Translation: CAA24742.1. Different initiation. U00096 Genomic DNA. Translation: AAC73227.1. AP009048 Genomic DNA. Translation: BAB96686.2. | |
| PIR | DEECLP. S45195. |
| RefSeq | AP_000777.1. NP_414658.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1OJT based on UniProtKB Q51225. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P0A9P0. 90 interactions. |
2-D gel databases | |
| SWISS-2DPAGE | P0A9P0. |
| 2DBase-Ecoli | P0A9P0. |
| ECO2DBASE | G050.5. 6TH EDITION. |
Genome annotation databases | |
| GeneID | 944854. |
| GenomeReviews | Gene locus JW0112 in contig AP009048_GR. Gene locus b0116 in contig U00096_GR. |
| KEGG | ecj:JW0112. eco:b0116. |
Organism-specific databases | |
| EchoBASE | EB0538. |
| EcoGene | EG10543. lpd. |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P0A9P0. |
| OMA | P0A9P0. MMDGLMA. |
Enzyme and pathway databases | |
| BioCyc | EcoCyc:E3-MON. MetaCyc:E3-MON. |
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_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P0A9P0 Secondary accession number(s): P00391 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| SIMILARITY comments Index of protein domains and families |

Clusters with


