UniProt Accession

 ODO2_ECOLI; P0AFG6; P07016 

Genbank Protein ID

 J01619; X00664; U00096; AP009048; X00661 

Genbank Nucleotide ID

 AAA23898.1; CAA25284.1; AAC73821.1; BAA35393.1; CAA25281.1 

Protein Name

 Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 

Protein Synonyms/Alias

 2-oxoglutarate dehydrogenase complex component E2; OGDC-E2; Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex 

Gene Name

 sucB 

Gene Synonyms/Alias

 b0727; JW0716 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
94	TSAKSEEKASTPAQR	acetylation	[1]
133	NLDASAIKGTGVGGR	acetylation	[1]
148	LTREDVEKHLAKAPA	acetylation	[1, 2, 3]
152	DVEKHLAKAPAKESA	acetylation	[1, 3]
156	HLAKAPAKESAPAAA	acetylation	[1]
211	TFNEVNMKPIMDLRK	acetylation	[1]
218	KPIMDLRKQYGEAFE	acetylation	[1, 3]
226	QYGEAFEKRHGIRLG	acetylation	[1, 4]
297	LGMADIEKKIKELAV	acetylation	[1]
300	ADIEKKIKELAVKGR	acetylation	[1, 3]
305	KIKELAVKGRDGKLT	acetylation	[1]
392	VGFLVTIKELLEDPT	acetylation	[3]

Reference

 [1] 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]
 [2] Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
 Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842]
 [3] 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]
 [4] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508] 

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 2 77 Lipoyl-binding.
 ACT_SITE 376 376
 ACT_SITE 380 380
 MOD_RES 44 44 N6-lipoyllysine.
 MOD_RES 148 148 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Acyltransferase; Complete proteome; Direct protein sequencing; Lipoyl; Reference proteome; Transferase; Tricarboxylic acid cycle. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 405 AA 

Protein Sequence

Gene Ontology

 GO:0045252; C:oxoglutarate dehydrogenase complex; IDA:EcoliWiki.
 GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IDA:EcoliWiki.
 GO:0031405; F:lipoic acid binding; IDA:EcoliWiki.
 GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
 GO:0006099; P:tricarboxylic acid cycle; IMP:EcoliWiki. 

Interpro

 IPR003016; 2-oxoA_DH_lipoyl-BS.
 IPR001078; 2-oxoacid_DH_actylTfrase.
 IPR000089; Biotin_lipoyl.
 IPR023213; CAT-like_dom.
 IPR004167; E3-bd.
 IPR011053; Single_hybrid_motif.
 IPR006255; SucB. 

Pfam

 PF00198; 2-oxoacid_dh
 PF00364; Biotin_lipoyl
 PF02817; E3_binding 

SMART

  

PROSITE

 PS50968; BIOTINYL_LIPOYL
 PS00189; LIPOYL 

PRINTS