2-amino-3-ketobutyrate coenzyme A ligase (P0AB77)

Identification
Name:2-amino-3-ketobutyrate coenzyme A ligase
Synonyms:
  • AKB ligase
  • Glycine acetyltransferase
Gene Name:kbl
Enzyme Class:
Biological Properties
General Function:Involved in glycine C-acetyltransferase activity
Specific Function:Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
  • Glycine, serine and threonine metabolism ec00260
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Acetyl-CoA + 1.0Glycine ↔ 1.0L-2-Amino-3-oxobutanoic acid + 1.0Coenzyme A
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0L-2-Amino-3-oxobutanoic acid + 1.0Coenzyme A → 1.0Acetyl-CoA + 1.0Glycine
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Acetyl-CoA + 1.0Glycine ↔ 1.0L-2-Amino-3-oxobutanoic acid + 1.0Coenzyme A
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01206Acetyl-CoAMetaboCard
ECMDB01423Coenzyme AMetaboCard
ECMDB00123GlycineMetaboCard
ECMDB06454L-2-Amino-3-oxobutanoic acidMetaboCard
GO Classification:
Function
acetyltransferase activity
acyltransferase activity
binding
C-acetyltransferase activity
catalytic activity
cofactor binding
glycine C-acetyltransferase activity
pyridoxal phosphate binding
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring acyl groups other than amino-acyl groups
transferase activity, transferring nitrogenous groups
Process
biosynthetic process
metabolic process
Gene Properties
Blattner:b3617
Gene OrientationCounterclockwise
Centisome Percentage:81.67
Left Sequence End3789378
Right Sequence End3790574
Gene Sequence:
>1197 bp
ATGAAGCAACTCACCATTCTGGGCTCGACCGGCTCGATTGGTTGCAGCACGCTGGACGTG
GTGCGCCATAATCCCGAACACTTCCGCGTAGTTGCGCTGGTGGCAGGCAAAAATGTCACT
CGCATGGTAGAACAGTGCCTGGAATTCTCTCCCCGCTATGCCGTAATGGACGATGAAGCG
AGTGCGAAACTTCTTAAAACGATGCTACAGCAACAGGGTAGCCGCACCGAAGTCTTAAGT
GGGCAACAAGCCGCTTGCGATATGGCAGCGCTTGAGGATGTTGATCAGGTGATGGCAGCC
ATTGTTGGCGCTGCTGGGCTGTTACCTACGCTTGCTGCGATCCGCGCGGGTAAAACCATT
TTGCTGGCCAATAAAGAATCACTGGTTACCTGCGGACGTCTGTTTATGGACGCCGTAAAG
CAGAGCAAAGCGCAATTGTTACCGGTCGATAGCGAACATAACGCCATTTTTCAGAGTTTA
CCGCAACCTATCCAGCATAATCTGGGATACGCTGACCTTGAGCAAAATGGCGTGGTGTCC
ATTTTACTTACCGGGTCTGGTGGCCCTTTCCGTGAGACGCCATTGCGCGATTTGGCAACA
ATGACGCCGGATCAAGCCTGCCGTCATCCGAACTGGTCGATGGGGCGTAAAATTTCTGTC
GATTCGGCTACCATGATGAACAAAGGTCTGGAATACATTGAAGCGCGTTGGCTGTTTAAC
GCCAGCGCCAGCCAGATGGAAGTGCTGATTCACCCGCAGTCAGTGATTCACTCAATGGTG
CGCTATCAGGACGGCAGTGTTCTGGCGCAGCTGGGGGAACCGGATATGCGTACGCCAATT
GCCCACACCATGGCATGGCCGAATCGCGTGAACTCTGGCGTGAAGCCGCTCGATTTTTGC
AAACTAAGTGCGTTGACATTTGCCGCACCGGATTATGATCGTTATCCATGCCTGAAACTG
GCGATGGAGGCGTTCGAACAAGGCCAGGCAGCGACGACAGCATTGAATGCCGCAAACGAA
ATCACCGTTGCTGCTTTTCTTGCGCAACAAATCCGCTTTACGGATATCGCTGCGTTGAAT
TTATCCGTACTGGAAAAAATGGATATGCGCGAACCACAATGTGTGGACGATGTGTTATCT
GTTGATGCGAACGCGCGTGAAGTCGCCAGAAAAGAGGTGATGCGTCTCGCAAGCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:398
Protein Molecular Weight:43117
Protein Theoretical pI:6
PDB File:1FC4
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>2-amino-3-ketobutyrate coenzyme A ligase
MRGEFYQQLTNDLETARAEGLFKEERIITSAQQADITVADGSHVINFCANNYLGLANHPD
LIAAAKAGMDSHGFGMASVRFICGTQDSHKELEQKLAAFLGMEDAILYSSCFDANGGLFE
TLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMQELEARLKEAREAGARHVLIAT
DGVFSMDGVIANLKGVCDLADKYDALVMVDDSHAVGFVGENGRGSHEYCDVMGRVDIITG
TLGKALGGASGGYTAARKEVVEWLRQRSRPYLFSNSLAPAIVAASIKVLEMVEAGSELRD
RLWANARQFREQMSAAGFTLAGADHAIIPVMLGDAVVAQKFARELQKEGIYVTGFFYPVV
PKGQARIRTQMSAAHTPEQITRAVEAFTRIGKQLGVIA
References
External Links:
ResourceLink
Uniprot ID:P0AB77
Uniprot Name:KBL_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674366
PDB ID:1FC4
Ecogene ID:EG10512
Ecocyc:EG10512
ColiBase:b3617
Kegg Gene:b3617
EchoBASE ID:EB0507
CCDB:KBL_ECOLI
BacMap:16131488
General Reference:
  • Aronson, B. D., Ravnikar, P. D., Somerville, R. L. (1988). "Nucleotide sequence of the 2-amino-3-ketobutyrate coenzyme A ligase (kbl) gene of E. coli." Nucleic Acids Res 16:3586. Pubmed: 3287333
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Mukherjee, J. J., Dekker, E. E. (1987). "Purification, properties, and N-terminal amino acid sequence of homogeneous Escherichia coli 2-amino-3-ketobutyrate CoA ligase, a pyridoxal phosphate-dependent enzyme." J Biol Chem 262:14441-14447. Pubmed: 3117785
  • Mukherjee, J. J., Dekker, E. E. (1990). "2-Amino-3-ketobutyrate CoA ligase of Escherichia coli: stoichiometry of pyridoxal phosphate binding and location of the pyridoxyllysine peptide in the primary structure of the enzyme." Biochim Biophys Acta 1037:24-29. Pubmed: 2104756
  • Schmidt, A., Sivaraman, J., Li, Y., Larocque, R., Barbosa, J. A., Smith, C., Matte, A., Schrag, J. D., Cygler, M. (2001). "Three-dimensional structure of 2-amino-3-ketobutyrate CoA ligase from Escherichia coli complexed with a PLP-substrate intermediate: inferred reaction mechanism." Biochemistry 40:5151-5160. Pubmed: 11318637
  • Sofia, H. J., Burland, V., Daniels, D. L., Plunkett, G. 3rd, Blattner, F. R. (1994). "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes." Nucleic Acids Res 22:2576-2586. Pubmed: 8041620