CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-035900
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dihydrolipoyllysine-residue acetyltransferase component of pyruvat dehydrogenase complex 
Protein Synonyms/Alias
  
Gene Name
 aceF 
Gene Synonyms/Alias
 EAM_0748 
Created Date
 July 27, 2013 
Organism
 Erwinia amylovora (strain ATCC 49946 / CCPPB 0273 / Ea273 / 27-3) 
NCBI Taxa ID
 716540 
Lysine Modification
Position
Peptide
Type
References
432RELTTISKKARDGKLacetylation[1]
433ELTTISKKARDGKLTacetylation[1]
Reference
 [1] Differential lysine acetylation profiles of Erwinia amylovora strains revealed by proteomics.
 Wu X, Vellaichamy A, Wang D, Zamdborg L, Kelleher NL, Huber SC, Zhao Y.
 J Proteomics. 2013 Feb 21;79:60-71. [PMID: 23234799
Functional Description
  
Sequence Annotation
  
Keyword
 Acyltransferase; Complete proteome; Lipoyl; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 531 AA 
Protein Sequence
MAIEINVPDI GADEVEVTEI LVKVGDTVEV EQSILVVEGD KASMEVPSPQ AGVVKEIKIA 60
TGDRVETGKL IMIFEAAGDA AAPAAAQEKQ EAAPAAPAAA PAAASAAKEV NVPDIGGDEV 120
EVTEIMVKVG DKVEAEQSIL TVEGDKASME VPAPFAGTVK EIKISAGDKV STGSLVMVFD 180
VEGAAPAAAP AAKAEAPAPA APVQEEKAAP AAAPAKAEAK SEFAENDAYV HATPVIRRLA 240
REFGVNLAKV KGTGRKSRIL KEDVQSYVKD AVKRAEAPAA GGGMPGMLPW PKVDYSKFGE 300
VEEVELGRIQ KISGANLSRN WVMIPHVTHF DKTDITDLEA FRKQQNAEAE KRKLDVKFTP 360
VVFIMKAVAA ALEQMPRFNS SLSEDAQKLT LKKYINIGVA VDTPNGLVVP VFKDVNKKGI 420
VELSRELTTI SKKARDGKLT AGEMQGGCFT ISSIGGLGTT HFAPIVNAPE VAILGVSKSA 480
MEPVWNGKEF MPRLMMPISL SFDHRVIDGA DGARFITIIN NTLADIRRLV M 531 
Gene Ontology
 GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
 GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:EC.
 GO:0006096; P:glycolysis; IEA:InterPro. 
Interpro
 IPR003016; 2-oxoA_DH_lipoyl-BS.
 IPR001078; 2-oxoacid_DH_actylTfrase.
 IPR006256; AcTrfase_Pyrv_DH_cplx.
 IPR000089; Biotin_lipoyl.
 IPR023213; CAT-like_dom.
 IPR004167; E3-bd.
 IPR011053; Single_hybrid_motif. 
Pfam
 PF00198; 2-oxoacid_dh
 PF00364; Biotin_lipoyl
 PF02817; E3_binding 
SMART
  
PROSITE
 PS50968; BIOTINYL_LIPOYL
 PS00189; LIPOYL 
PRINTS