CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003540
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 2-oxoglutarate dehydrogenase E1 component 
Protein Synonyms/Alias
 Alpha-ketoglutarate dehydrogenase 
Gene Name
 sucA 
Gene Synonyms/Alias
 b0726; JW0715 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
54QLPGTGVKPDQFHSQacetylation[1, 2]
88SDPDTNVKQVKVLQLacetylation[2]
91DTNVKQVKVLQLINAacetylation[2]
152ASGKETMKLGELLEAacetylation[2]
181HITSTEEKRWIQQRIacetylation[2]
220LERYLGAKFPGAKRFacetylation[2]
225GAKFPGAKRFSLEGGacetylation[2]
273VLVNVLGKKPQDLFDacetylation[1, 2]
274LVNVLGKKPQDLFDEacetylation[2]
285LFDEFAGKHKEHLGTacetylation[2]
287DEFAGKHKEHLGTGDacetylation[2]
476TQPLMYQKIKKHPTPacetylation[2]
478PLMYQKIKKHPTPRKacetylation[2]
485KKHPTPRKIYADKLEacetylation[1, 2]
490PRKIYADKLEQEKVAacetylation[2]
495ADKLEQEKVATLEDAacetylation[2]
559KRLQELAKRISTVPEacetylation[2]
576EMQSRVAKIYGDRQAacetylation[2]
812EIDELDPKGVKRVVMacetylation[2]
854QLYPFPHKAMQEVLQacetylation[2]
920GYMSVHQKQQQDLVNacetylation[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] 
Functional Description
 The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2- oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3). 
Sequence Annotation
  
Keyword
 3D-structure; Complete proteome; Glycolysis; Oxidoreductase; Reference proteome; Thiamine pyrophosphate. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 933 AA 
Protein Sequence
MQNSALKAWL DSSYLSGANQ SWIEQLYEDF LTDPDSVDAN WRSTFQQLPG TGVKPDQFHS 60
QTREYFRRLA KDASRYSSTI SDPDTNVKQV KVLQLINAYR FRGHQHANLD PLGLWQQDKV 120
ADLDPSFHDL TEADFQETFN VGSFASGKET MKLGELLEAL KQTYCGPIGA EYMHITSTEE 180
KRWIQQRIES GRATFNSEEK KRFLSELTAA EGLERYLGAK FPGAKRFSLE GGDALIPMLK 240
EMIRHAGNSG TREVVLGMAH RGRLNVLVNV LGKKPQDLFD EFAGKHKEHL GTGDVKYHMG 300
FSSDFQTDGG LVHLALAFNP SHLEIVSPVV IGSVRARLDR LDEPSSNKVL PITIHGDAAV 360
TGQGVVQETL NMSKARGYEV GGTVRIVINN QVGFTTSNPL DARSTPYCTD IGKMVQAPIF 420
HVNADDPEAV AFVTRLALDF RNTFKRDVFI DLVCYRRHGH NEADEPSATQ PLMYQKIKKH 480
PTPRKIYADK LEQEKVATLE DATEMVNLYR DALDAGDCVV AEWRPMNMHS FTWSPYLNHE 540
WDEEYPNKVE MKRLQELAKR ISTVPEAVEM QSRVAKIYGD RQAMAAGEKL FDWGGAENLA 600
YATLVDEGIP VRLSGEDSGR GTFFHRHAVI HNQSNGSTYT PLQHIHNGQG AFRVWDSVLS 660
EEAVLAFEYG YATAEPRTLT IWEAQFGDFA NGAQVVIDQF ISSGEQKWGR MCGLVMLLPH 720
GYEGQGPEHS SARLERYLQL CAEQNMQVCV PSTPAQVYHM LRRQALRGMR RPLVVMSPKS 780
LLRHPLAVSS LEELANGTFL PAIGEIDELD PKGVKRVVMC SGKVYYDLLE QRRKNNQHDV 840
AIVRIEQLYP FPHKAMQEVL QQFAHVKDFV WCQEEPLNQG AWYCSQHHFR EVIPFGASLR 900
YAGRPASASP AVGYMSVHQK QQQDLVNDAL NVE 933 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IDA:EcoCyc.
 GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
 GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
 GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. 
Interpro
 IPR011603; 2oxoglutarate_DH_E1.
 IPR001017; DH_E1.
 IPR005475; Transketolase-like_Pyr-bd. 
Pfam
 PF00676; E1_dh
 PF02779; Transket_pyr 
SMART
 SM00861; Transket_pyr 
PROSITE
  
PRINTS