UniProt Accession

 KBL_ECOLI; P0AB77; P07912; Q2M7T1 

Genbank Protein ID

 X06690; U00039; U00096; AP009048 

Genbank Nucleotide ID

 CAA29883.1; AAB18594.1; AAC76641.1; BAE77675.1 

Protein Name

 2-amino-3-ketobutyrate coenzyme A ligase 

Protein Synonyms/Alias

 AKB ligase; Glycine acetyltransferase 

Gene Name

 kbl 

Gene Synonyms/Alias

 b3617; JW3592 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
23	ARAEGLFKEERIITS	acetylation	[1, 2]
90	CGTQDSHKELEQKLA	acetylation	[1]
244	IITGTLGKALGGASG	acetylation	[1, 2]
340	GDAVVAQKFARELQK	acetylation	[2]
347	KFARELQKEGIYVTG	acetylation	[2]
362	FFYPVVPKGQARIRT	acetylation	[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

 Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. 

Sequence Annotation

 REGION 111 112 Pyridoxal phosphate binding.
 REGION 210 213 Pyridoxal phosphate binding.
 REGION 241 244 Pyridoxal phosphate binding.
 REGION 274 275 Pyridoxal phosphate binding.
 BINDING 136 136 Pyridoxal phosphate.
 BINDING 136 136 Substrate.
 BINDING 185 185 Pyridoxal phosphate.
 BINDING 185 185 Substrate.
 BINDING 213 213 Substrate.
 BINDING 244 244 Substrate.
 BINDING 368 368 Substrate.
 MOD_RES 244 244 N6-(pyridoxal phosphate)lysine.  

Keyword

 3D-structure; Acyltransferase; Complete proteome; Direct protein sequencing; Pyridoxal phosphate; Reference proteome; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 398 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IDA:EcoliWiki.
 GO:0008890; F:glycine C-acetyltransferase activity; IEA:EC.
 GO:0016874; F:ligase activity; IDA:EcoliWiki.
 GO:0046872; F:metal ion binding; IDA:EcoliWiki.
 GO:0030170; F:pyridoxal phosphate binding; IDA:EcoliWiki.
 GO:0009058; P:biosynthetic process; IEA:InterPro.
 GO:0019518; P:L-threonine catabolic process to glycine; IEA:UniProtKB-UniPathway. 

Interpro

 IPR011282; 2am3keto_CoA_ligase.
 IPR001917; Aminotrans_II_pyridoxalP_BS.
 IPR004839; Aminotransferase_I/II.
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1.
 IPR015422; PyrdxlP-dep_Trfase_major_sub2. 

Pfam

 PF00155; Aminotran_1_2 

SMART

  

PROSITE

 PS00599; AA_TRANSFER_CLASS_2 

PRINTS