Q9Z773 (DLDH_CHLPN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 100.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Dihydrolipoyl dehydrogenase EC=1.8.1.4 Alternative name(s): Dihydrolipoamide dehydrogenase E3 component of 2-oxoglutarate dehydrogenase complex | ||||
| Gene names |
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| Organism | Chlamydia pneumoniae (Chlamydophila pneumoniae) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83558 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia |
Protein attributes
| Sequence length | 461 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity. |
| 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 By similarity. |
| 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 |
| 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 |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | dihydrolipoyl dehydrogenase activity Inferred from electronic annotation. Source: EC flavin adenine dinucleotide bindingInferred 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 – 461 | 461 | Dihydrolipoyl dehydrogenase | PRO_0000068025 | |||||||
Regions | |||||||||||
| Nucleotide binding | 34 – 42 | 9 | FAD By similarity | ||||||||
| Nucleotide binding | 177 – 181 | 5 | NAD By similarity | ||||||||
| Nucleotide binding | 261 – 264 | 4 | NAD By similarity | ||||||||
Sites | |||||||||||
| Active site | 436 | 1 | Proton acceptor By similarity | ||||||||
| Binding site | 51 | 1 | FAD By similarity | ||||||||
| Binding site | 114 | 1 | FAD; via amide nitrogen and carbonyl oxygen By similarity | ||||||||
| Binding site | 200 | 1 | NAD By similarity | ||||||||
| Binding site | 304 | 1 | FAD By similarity | ||||||||
| Binding site | 312 | 1 | FAD; via amide nitrogen By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 42 ↔ 47 | Redox-active By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 64 | 1 | K → T in AAP98791. Ref.5 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Comparative genomes of Chlamydia pneumoniae and C. trachomatis." Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., Olinger L., Grimwood J., Davis R.W., Stephens R.S. Nat. Genet. 21:385-389(1999) [PubMed: 10192388] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CWL029. |
| [2] | "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39." Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. Fraser C.M.Nucleic Acids Res. 28:1397-1406(2000) [PubMed: 10684935] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AR39. |
| [3] | "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA." Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T. Nucleic Acids Res. 28:2311-2314(2000) [PubMed: 10871362] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: J138. |
| [4] | "Genomic sequence comparison of two unrelated isolates of Chlamydia pneumoniae from Japan and U.S." Shirai M. Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: J138. |
| [5] | "The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis." Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TW-183. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE001363 Genomic DNA. Translation: AAD18970.1. AE002161 Genomic DNA. Translation: AAF38812.1. BA000008 Genomic DNA. Translation: BAA99041.1. AB035943 Genomic DNA. Translation: BAA88651.1. AE009440 Genomic DNA. Translation: AAP98791.1. |
| PIR | C72031. G86594. |
| RefSeq | NP_225028.1. NC_000922.1. NP_300890.1. NC_002491.1. NP_445574.1. NC_002179.2. NP_877134.1. NC_005043.1. |
3D structure databases | |
| ProteinModelPortal | Q9Z773. |
| ModBase | Search... |
2D gel databases | |
| PHCI-2DPAGE | Q9Z773. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1467541. 895532. 919599. 963515. |
| GenomeReviews | Gene locus CPn_0833 in contig AE001363_GR. Gene locus CP_1037 in contig AE002161_GR. Gene locus CpB0862 in contig AE009440_GR. Gene locus lpdA in contig BA000008_GR. |
| KEGG | cpa:CP1037. cpn:CPn0833. cpt:CpB0862. |
| TIGR | CP_1037. |
Phylogenomic databases | |
| HOGENOM | HBG515043. |
| OMA | LLATNHP. |
| ProtClustDB | PRK06327. |
Enzyme and pathway databases | |
| BioCyc | CPNE115711:CP_1037-MONOMER. CPNE115713:CPN0833-MONOMER. CPNE138677:CPJ0833-MONOMER. CPNE182082:CPB0862-MONOMER. |
Family and domain databases | |
| InterPro | IPR016156. FAD/NAD-linked_Rdtase_dimer. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR006258. Lipoamide_DH. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD. IPR012999. Pyr_OxRdtase_I_AS. IPR001327. Pyr_OxRdtase_NAD-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit. |
| KO | K00382. |
| Pfam | PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view] |
| PRINTS | PR00368. FADPNR. |
| SUPFAM | SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit. |
| TIGRFAMs | TIGR01350. Lipoamide_DH. 1 hit. |
| PROSITE | PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DLDH_CHLPN | ||||||||
| Accession | Primary (citable) accession number: Q9Z773 Secondary accession number(s): Q9JQE6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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