UniProt Accession

 DLDH_ECOLI; P0A9P0; P00391 

Genbank Protein ID

 V01498; U00096; AP009048 

Genbank Nucleotide ID

 CAA24742.1; AAC73227.1; BAB96686.2 

Protein Name

 Dihydrolipoyl dehydrogenase 

Protein Synonyms/Alias

 Dihydrolipoamide dehydrogenase; E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes; Glycine cleavage system L protein 

Gene Name

 lpdA 

Gene Synonyms/Alias

 lpd; b0116; JW0112 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
54	NVGCIPSKALLHVAK	acetylation	[1, 2]
61	KALLHVAKVIEEAKA	acetylation	[1, 2]
67	AKVIEEAKALAEHGI	acetylation	[1, 2]
80	GIVFGEPKTDIDKIR	acetylation	[1, 2]
85	EPKTDIDKIRTWKEK	acetylation	[1, 2]
92	KIRTWKEKVINQLTG	acetylation	[1, 2]
106	GGLAGMAKGRKVKVV	acetylation	[1, 2]
109	AGMAKGRKVKVVNGL	acetylation	[2]
111	MAKGRKVKVVNGLGK	acetylation	[1, 2, 3]
118	KVVNGLGKFTGANTL	acetylation	[2]
172	STDALELKEVPERLL	acetylation	[2]
220	AADKDIVKVFTKRIS	acetylation	[2, 3, 4]
224	DIVKVFTKRISKKFN	acetylation	[2]
229	FTKRISKKFNLMLET	acetylation	[1, 2]
244	KVTAVEAKEDGIYVT	acetylation	[2]
255	IYVTMEGKKAPAEPQ	acetylation	[2]
256	YVTMEGKKAPAEPQR	acetylation	[1, 2]
278	IGRVPNGKNLDAGKA	acetylation	[2]
284	GKNLDAGKAGVEVDD	acetylation	[2]
299	RGFIRVDKQLRTNVP	acetylation	[1, 3]
338	AAEVIAGKKHYFDPK	acetylation	[1, 2]
339	AEVIAGKKHYFDPKV	acetylation	[2]
345	KKHYFDPKVIPSIAY	acetylation	[2]
365	AWVGLTEKEAKEKGI	acetylation	[2]
368	GLTEKEAKEKGISYE	acetylation	[2]
370	TEKEAKEKGISYETA	acetylation	[1, 2]
398	DCADGMTKLIFDKES	acetylation	[1, 2]
403	MTKLIFDKESHRVIG	acetylation	[2]

Reference

 [1] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111]
 [2] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [3] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508]
 [4] 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 CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842] 

Functional Description

 Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. 

Sequence Annotation

 NP_BIND 36 45 FAD (By similarity).
 NP_BIND 182 186 NAD (By similarity).
 NP_BIND 270 273 NAD (By similarity).
 ACT_SITE 445 445 Proton acceptor (By similarity).
 BINDING 54 54 FAD (By similarity).
 BINDING 117 117 FAD; via amide nitrogen and carbonyl
 BINDING 205 205 NAD (By similarity).
 BINDING 238 238 NAD; via amide nitrogen (By similarity).
 BINDING 313 313 FAD (By similarity).
 BINDING 321 321 FAD; via amide nitrogen (By similarity).
 MOD_RES 220 220 N6-acetyllysine.
 DISULFID 45 50 Redox-active (By similarity).  

Keyword

 3D-structure; Acetylation; Cell inner membrane; Cell membrane; Complete proteome; Cytoplasm; Direct protein sequencing; Disulfide bond; FAD; Flavoprotein; Glycolysis; Membrane; NAD; Oxidoreductase; Redox-active center; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 474 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0004148; F:dihydrolipoyl dehydrogenase activity; IDA:EcoliWiki.
 GO:0015036; F:disulfide oxidoreductase activity; IDA:EcoliWiki.
 GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoliWiki.
 GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
 GO:0006103; P:2-oxoglutarate metabolic process; IMP:EcoliWiki.
 GO:0045454; P:cell redox homeostasis; IEA:InterPro.
 GO:0019464; P:glycine decarboxylation via glycine cleavage system; IMP:EcoCyc.
 GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
 GO:0006090; P:pyruvate metabolic process; IDA:EcoliWiki. 

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. 

Pfam

 PF00070; Pyr_redox
 PF07992; Pyr_redox_2
 PF02852; Pyr_redox_dim 

SMART

  

PROSITE

 PS00076; PYRIDINE_REDOX_1 

PRINTS

 PR00368; FADPNR.