CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010099
UniProt Accession
Genbank Protein ID
 U00089 
Genbank Nucleotide ID
Protein Name
 Pyruvate dehydrogenase E1 component subunit beta 
Protein Synonyms/Alias
  
Gene Name
 pdhB 
Gene Synonyms/Alias
 MPN_392; MP446 
Created Date
 July 27, 2013 
Organism
 Mycoplasma pneumoniae (strain ATCC 29342 / M129) 
NCBI Taxa ID
 272634 
Lysine Modification
Position
Peptide
Type
References
255ETVFNSVKKTGRLLVacetylation[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
 The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). 
Sequence Annotation
 BINDING 63 63 Thiamine pyrophosphate (By similarity).  
Keyword
 Complete proteome; Glycolysis; Oxidoreductase; Pyruvate; Reference proteome; Thiamine pyrophosphate. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 327 AA 
Protein Sequence
MSKTIQANNI EALGNAMDLA LERDPNVVLY GQDAGFEGGV FRATKGLQKK YGEERVWDCP 60
IAEAAMAGIG VGAAIGGLKP IVEIQFSGFS FPAMFQIFTH AARIRNRSRG VYTCPIIVRM 120
PMGGGIKALE HHSETLEAIY GQIAGLKTVM PSNPYDTKGL FLAAVESPDP VVFFEPKKLY 180
RAFRQEIPAD YYTVPIGQAN LISQGNNLTI VSYGPTMFDL INMVYGGELK DKGIELIDLR 240
TISPWDKETV FNSVKKTGRL LVVTEAAKTF TTSGEIIASV TEELFSYLKA APQRVTGWDI 300
VVPLARGEHY QFNLNARILE AVNQLLK 327 
Gene Ontology
 GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:EC.
 GO:0006096; P:glycolysis; IEA:UniProtKB-KW. 
Interpro
 IPR009014; Transketo_C/Pyr-ferredox_oxred.
 IPR015941; Transketolase-like_C.
 IPR005475; Transketolase-like_Pyr-bd.
 IPR005476; Transketolase_C. 
Pfam
 PF02779; Transket_pyr
 PF02780; Transketolase_C 
SMART
 SM00861; Transket_pyr 
PROSITE
  
PRINTS