CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010101
UniProt Accession
Genbank Protein ID
 U00089 
Genbank Nucleotide ID
Protein Name
 Dihydrolipoyl dehydrogenase 
Protein Synonyms/Alias
 Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex 
Gene Name
 pdhD 
Gene Synonyms/Alias
 MPN_390; MP448 
Created Date
 July 27, 2013 
Organism
 Mycoplasma pneumoniae (strain ATCC 29342 / M129) 
NCBI Taxa ID
 272634 
Lysine Modification
Position
Peptide
Type
References
92QKGKVVSKLVGGVKAacetylation[1]
105KAIIASAKAETVMGEacetylation[1]
126NTVEVAGKTYTTKSIacetylation[1]
328AVNHILNKKQVKPAQacetylation[1]
360GYTEMELKKQGIPYVacetylation[1]
Reference
 [1] Cross-talk between phosphorylation and lysine acetylation in a genome-reduced bacterium.
 van Noort V, Seebacher J, Bader S, Mohammed S, Vonkova I, Betts MJ, Kühner S, Kumar R, Maier T, O'Flaherty M, Rybin V, Schmeisky A, Yus E, Stülke J, Serrano L, Russell RB, Heck AJ, Bork P, Gavin AC.
 Mol Syst Biol. 2012 Feb 28;8:571. [PMID: 22373819
Functional Description
 Lipoamide dehydrogenase is a component of the alpha- ketoacid dehydrogenase complexes (By similarity). 
Sequence Annotation
 NP_BIND 32 40 FAD (By similarity).
 NP_BIND 178 182 NAD (By similarity).
 NP_BIND 262 265 NAD (By similarity).
 ACT_SITE 437 437 Proton acceptor (By similarity).
 BINDING 49 49 FAD (By similarity).
 BINDING 113 113 FAD; via amide nitrogen and carbonyl
 BINDING 235 235 NAD; via amide nitrogen (By similarity).
 BINDING 303 303 FAD (By similarity).
 BINDING 311 311 FAD; via amide nitrogen (By similarity).
 DISULFID 40 45 Redox-active (By similarity).  
Keyword
 Complete proteome; Cytoplasm; Disulfide bond; FAD; Flavoprotein; Glycolysis; NAD; Oxidoreductase; Redox-active center; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 457 AA 
Protein Sequence
MNYDLIIIGA GPAGYVAAEY AGKHKLKTLV VEKEYFGGVC LNVGCIPTKT LLKRAKIVDY 60
LRHAQDYGIS INGQVALNWN QLLEQKGKVV SKLVGGVKAI IASAKAETVM GEAKVLDPNT 120
VEVAGKTYTT KSIVVATGSR PRYLTLPGFA EARQNGFVID STQALSLEGV PRKLVVVGGG 180
VIGIEFAFLY ASLGSEVTIL QGVDRILEIF DTEVSDLVAK LLQTKNVKII TNAQVTRANN 240
NEVFYSQNGQ EGSVVGDRIL VSIGRIPNTE CLDGLNLQRD ERNRIVLNQD LQTSIPNIYI 300
VGDANAQLML AHFAYQQGRY AVNHILNKKQ VKPAQKLTCP SCIYTNPEVA SVGYTEMELK 360
KQGIPYVKTN LVLAHCGKAI ADNETNGFVK MMFDPQTGKI LGCCIIAATA SDMIAELALA 420
MGAGLTVFDI ANSISPHPTI NEMIADVCKK ALFDHFK 457 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:EC.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0045454; P:cell redox homeostasis; IEA:InterPro.
 GO:0006096; P:glycolysis; IEA:UniProtKB-KW. 
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.