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UniProtKB - P0A9P0 (DLDH_ECOLI)
Protein
Dihydrolipoyl dehydrogenase
Gene
lpdA
Organism
Escherichia coli (strain K12)
Status
Functioni
Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes.
Miscellaneous
The active site is a redox-active disulfide bond.
Catalytic activityi
- EC:1.8.1.4
Cofactori
FADBy similarityNote: Binds 1 FAD per subunit.By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 54 | FADBy similarity | 1 | |
Binding sitei | 117 | FAD; via amide nitrogen and carbonyl oxygenBy similarity | 1 | |
Binding sitei | 205 | NADBy similarity | 1 | |
Binding sitei | 238 | NAD; via amide nitrogenBy similarity | 1 | |
Binding sitei | 313 | FADBy similarity | 1 | |
Binding sitei | 321 | FAD; via amide nitrogenBy similarity | 1 | |
Active sitei | 445 | Proton acceptorBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 36 – 45 | FADBy similarity | 10 | |
Nucleotide bindingi | 182 – 186 | NADBy similarity | 5 | |
Nucleotide bindingi | 270 – 273 | NADBy similarity | 4 |
GO - Molecular functioni
- dihydrolipoyl dehydrogenase activity Source: EcoCyc
- disulfide oxidoreductase activity Source: EcoliWiki
- flavin adenine dinucleotide binding Source: EcoliWiki
- identical protein binding Source: IntAct
- zinc ion binding Source: EcoliWiki
GO - Biological processi
- 2-oxoglutarate metabolic process Source: EcoliWiki
- cell redox homeostasis Source: InterPro
- glycine decarboxylation via glycine cleavage system Source: EcoCyc
- glycolytic process Source: UniProtKB-KW
- one-carbon metabolic process Source: ComplexPortal
- pyruvate catabolic process Source: ComplexPortal
- pyruvate metabolic process Source: EcoliWiki
- response to oxidative stress Source: EcoCyc
- tricarboxylic acid cycle Source: ComplexPortal
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Glycolysis |
Ligand | FAD, Flavoprotein, NAD |
Enzyme and pathway databases
BioCyci | EcoCyc:E3-MONOMER |
BRENDAi | 1.8.1.4, 2026 |
SABIO-RKi | P0A9P0 |
Names & Taxonomyi
Protein namesi | 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 namesi | Name:lpdA Synonyms:lpd Ordered Locus Names:b0116, JW0112 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm 1 Publication
Plasma membrane
- Cell inner membrane 1 Publication; Peripheral membrane protein 1 Publication
Cytosol
- cytosol Source: EcoCyc
- cytosolic pyruvate dehydrogenase complex Source: EcoCyc
Plasma Membrane
- plasma membrane Source: UniProtKB-SubCell
Other locations
- cytoplasm Source: ComplexPortal
- glycine cleavage complex Source: ComplexPortal
- membrane Source: UniProtKB
- oxoglutarate dehydrogenase complex Source: ComplexPortal
- pyruvate dehydrogenase complex Source: ComplexPortal
Keywords - Cellular componenti
Cell inner membrane, Cell membrane, Cytoplasm, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000068027 | 2 – 474 | Dihydrolipoyl dehydrogenaseAdd BLAST | 473 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 45 ↔ 50 | Redox-activeBy similarity | ||
Modified residuei | 220 | N6-acetyllysine1 Publication | 1 |
Keywords - PTMi
Acetylation, Disulfide bondProteomic databases
jPOSTi | P0A9P0 |
PaxDbi | P0A9P0 |
PRIDEi | P0A9P0 |
2D gel databases
SWISS-2DPAGEi | P0A9P0 |
PTM databases
iPTMneti | P0A9P0 |
Interactioni
Subunit structurei
Homodimer.
Binary interactionsi
P0A9P0
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 4261370, 34 interactors 849254, 2 interactors |
ComplexPortali | CPX-3921, 2-oxoglutarate dehydrogenase complex CPX-3943, Pyruvate dehydrogenase complex CPX-3949, Glycine cleavage system complex |
DIPi | DIP-6854N |
IntActi | P0A9P0, 92 interactors |
STRINGi | 511145.b0116 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
AlphaFoldDBi | P0A9P0 |
SMRi | P0A9P0 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Sequence similaritiesi
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.Curated
Keywords - Domaini
Redox-active centerPhylogenomic databases
eggNOGi | COG1249, Bacteria |
HOGENOMi | CLU_016755_0_3_6 |
InParanoidi | P0A9P0 |
OMAi | HMVGDRM |
PhylomeDBi | P0A9P0 |
Family and domain databases
Gene3Di | 3.30.390.30, 1 hit 3.50.50.60, 2 hits |
InterProi | View protein in InterPro IPR036188, FAD/NAD-bd_sf IPR023753, FAD/NAD-binding_dom IPR016156, FAD/NAD-linked_Rdtase_dimer_sf IPR006258, Lipoamide_DH IPR001100, Pyr_nuc-diS_OxRdtase IPR004099, Pyr_nucl-diS_OxRdtase_dimer IPR012999, Pyr_OxRdtase_I_AS |
Pfami | View protein in Pfam PF07992, Pyr_redox_2, 1 hit PF02852, Pyr_redox_dim, 1 hit |
PIRSFi | PIRSF000350, Mercury_reductase_MerA, 1 hit |
SUPFAMi | SSF51905, SSF51905, 1 hit SSF55424, SSF55424, 1 hit |
TIGRFAMsi | TIGR01350, lipoamide_DH, 1 hit |
PROSITEi | View protein in PROSITE PS00076, PYRIDINE_REDOX_1, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P0A9P0-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSTEIKTQVV VLGAGPAGYS AAFRCADLGL ETVIVERYNT LGGVCLNVGC
60 70 80 90 100
IPSKALLHVA KVIEEAKALA EHGIVFGEPK TDIDKIRTWK EKVINQLTGG
110 120 130 140 150
LAGMAKGRKV KVVNGLGKFT GANTLEVEGE NGKTVINFDN AIIAAGSRPI
160 170 180 190 200
QLPFIPHEDP RIWDSTDALE LKEVPERLLV MGGGIIGLEM GTVYHALGSQ
210 220 230 240 250
IDVVEMFDQV IPAADKDIVK VFTKRISKKF NLMLETKVTA VEAKEDGIYV
260 270 280 290 300
TMEGKKAPAE PQRYDAVLVA IGRVPNGKNL DAGKAGVEVD DRGFIRVDKQ
310 320 330 340 350
LRTNVPHIFA IGDIVGQPML AHKGVHEGHV AAEVIAGKKH YFDPKVIPSI
360 370 380 390 400
AYTEPEVAWV GLTEKEAKEK GISYETATFP WAASGRAIAS DCADGMTKLI
410 420 430 440 450
FDKESHRVIG GAIVGTNGGE LLGEIGLAIE MGCDAEDIAL TIHAHPTLHE
460 470
SVGLAAEVFE GSITDLPNPK AKKK
Sequence cautioni
The sequence CAA24742 differs from that shown. Reason: Erroneous initiation.Curated
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | V01498 Genomic DNA Translation: CAA24742.1 Different initiation. U00096 Genomic DNA Translation: AAC73227.1 AP009048 Genomic DNA Translation: BAB96686.2 |
PIRi | S45195, DEECLP |
RefSeqi | NP_414658.1, NC_000913.3 WP_000102485.1, NZ_STEB01000010.1 |
Genome annotation databases
EnsemblBacteriai | AAC73227; AAC73227; b0116 BAB96686; BAB96686; BAB96686 |
GeneIDi | 66671596 944854 |
KEGGi | ecj:JW0112 eco:b0116 |
PATRICi | fig|1411691.4.peg.2166 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | V01498 Genomic DNA Translation: CAA24742.1 Different initiation. U00096 Genomic DNA Translation: AAC73227.1 AP009048 Genomic DNA Translation: BAB96686.2 |
PIRi | S45195, DEECLP |
RefSeqi | NP_414658.1, NC_000913.3 WP_000102485.1, NZ_STEB01000010.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4JDR | X-ray | 2.50 | A/B | 1-474 | [»] | |
AlphaFoldDBi | P0A9P0 | |||||
SMRi | P0A9P0 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4261370, 34 interactors 849254, 2 interactors |
ComplexPortali | CPX-3921, 2-oxoglutarate dehydrogenase complex CPX-3943, Pyruvate dehydrogenase complex CPX-3949, Glycine cleavage system complex |
DIPi | DIP-6854N |
IntActi | P0A9P0, 92 interactors |
STRINGi | 511145.b0116 |
PTM databases
iPTMneti | P0A9P0 |
2D gel databases
SWISS-2DPAGEi | P0A9P0 |
Proteomic databases
jPOSTi | P0A9P0 |
PaxDbi | P0A9P0 |
PRIDEi | P0A9P0 |
Genome annotation databases
EnsemblBacteriai | AAC73227; AAC73227; b0116 BAB96686; BAB96686; BAB96686 |
GeneIDi | 66671596 944854 |
KEGGi | ecj:JW0112 eco:b0116 |
PATRICi | fig|1411691.4.peg.2166 |
Organism-specific databases
EchoBASEi | EB0538 |
Phylogenomic databases
eggNOGi | COG1249, Bacteria |
HOGENOMi | CLU_016755_0_3_6 |
InParanoidi | P0A9P0 |
OMAi | HMVGDRM |
PhylomeDBi | P0A9P0 |
Enzyme and pathway databases
BioCyci | EcoCyc:E3-MONOMER |
BRENDAi | 1.8.1.4, 2026 |
SABIO-RKi | P0A9P0 |
Miscellaneous databases
PROi | PR:P0A9P0 |
Family and domain databases
Gene3Di | 3.30.390.30, 1 hit 3.50.50.60, 2 hits |
InterProi | View protein in InterPro IPR036188, FAD/NAD-bd_sf IPR023753, FAD/NAD-binding_dom IPR016156, FAD/NAD-linked_Rdtase_dimer_sf IPR006258, Lipoamide_DH IPR001100, Pyr_nuc-diS_OxRdtase IPR004099, Pyr_nucl-diS_OxRdtase_dimer IPR012999, Pyr_OxRdtase_I_AS |
Pfami | View protein in Pfam PF07992, Pyr_redox_2, 1 hit PF02852, Pyr_redox_dim, 1 hit |
PIRSFi | PIRSF000350, Mercury_reductase_MerA, 1 hit |
SUPFAMi | SSF51905, SSF51905, 1 hit SSF55424, SSF55424, 1 hit |
TIGRFAMsi | TIGR01350, lipoamide_DH, 1 hit |
PROSITEi | View protein in PROSITE PS00076, PYRIDINE_REDOX_1, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | DLDH_ECOLI | |
Accessioni | P0A9P0Primary (citable) accession number: P0A9P0 Secondary accession number(s): P00391 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | January 23, 2007 | |
Last modified: | May 25, 2022 | |
This is version 143 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families