CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004754
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial 
Protein Synonyms/Alias
 2-oxoglutarate dehydrogenase complex component E2; OGDC-E2; Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex 
Gene Name
 KGD2 
Gene Synonyms/Alias
 YDR148C; YD8358.05C 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
280MEMRKLYKDEIIKKTacetylation[1]
285LYKDEIIKKTGTKFGacetylation[1]
290IIKKTGTKFGFMGLFacetylation[1]
448REAVTFLKTVKELIEacetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919
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
 DOMAIN 74 147 Lipoyl-binding.
 REPEAT 185 190 1.
 REPEAT 191 196 2.
 REPEAT 197 202 3.
 REPEAT 204 209 4; approximate.
 REGION 185 209 4 X 6 AA approximate tandem repeats of A-
 ACT_SITE 435 435 By similarity.
 ACT_SITE 439 439 By similarity.
 MOD_RES 114 114 N6-lipoyllysine (Potential).
 MOD_RES 340 340 Phosphothreonine.  
Keyword
 Acyltransferase; Complete proteome; Lipoyl; Mitochondrion; Phosphoprotein; Reference proteome; Repeat; Transferase; Transit peptide; Tricarboxylic acid cycle. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 463 AA 
Protein Sequence
MLSRATRTAA AKSLVKSKVA RNVMAASFVK RHASTSLFKQ ANKVESLGSI YLSGKKISVA 60
ANPFSITSNR FKSTSIEVPP MAESLTEGSL KEYTKNVGDF IKEDELLATI ETDKIDIEVN 120
SPVSGTVTKL NFKPEDTVTV GEELAQVEPG EAPAEGSGES KPEPTEQAEP SQGVAARENS 180
SEETASKKEA APKKEAAPKK EVTEPKKADQ PKKTVSKAQE PPVASNSFTP FPRTETRVKM 240
NRMRLRIAER LKESQNTAAS LTTFNEVDMS ALMEMRKLYK DEIIKKTGTK FGFMGLFSKA 300
CTLAAKDIPA VNGAIEGDQI VYRDYTDISV AVATPKGLVT PVVRNAESLS VLDIENEIVR 360
LSHKARDGKL TLEDMTGGTF TISNGGVFGS LYGTPIINSP QTAVLGLHGV KERPVTVNGQ 420
IVSRPMMYLA LTYDHRLLDG REAVTFLKTV KELIEDPRKM LLW 463 
Gene Ontology
 GO:0042645; C:mitochondrial nucleoid; IDA:SGD.
 GO:0009353; C:mitochondrial oxoglutarate dehydrogenase complex; IDA:SGD.
 GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; ISA:SGD.
 GO:0006103; P:2-oxoglutarate metabolic process; IMP:SGD.
 GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
 GO:0000002; P:mitochondrial genome maintenance; IGI:SGD.
 GO:0006099; P:tricarboxylic acid cycle; IC:SGD. 
Interpro
 IPR003016; 2-oxoA_DH_lipoyl-BS.
 IPR001078; 2-oxoacid_DH_actylTfrase.
 IPR000089; Biotin_lipoyl.
 IPR023213; CAT-like_dom.
 IPR011053; Single_hybrid_motif.
 IPR006255; SucB. 
Pfam
 PF00198; 2-oxoacid_dh
 PF00364; Biotin_lipoyl 
SMART
  
PROSITE
 PS50968; BIOTINYL_LIPOYL
 PS00189; LIPOYL 
PRINTS