2-amino-3-ketobutyrate coenzyme A ligase

Details

Name
2-amino-3-ketobutyrate coenzyme A ligase
Synonyms
  • 2.3.1.29
  • AKB ligase
  • Glycine acetyltransferase
Gene Name
kbl
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0011483|2-amino-3-ketobutyrate coenzyme A ligase
MRGEFYQQLTNDLETARAEGLFKEERIITSAQQADITVADGSHVINFCANNYLGLANHPD
LIAAAKAGMDSHGFGMASVRFICGTQDSHKELEQKLAAFLGMEDAILYSSCFDANGGLFE
TLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMQELEARLKEAREAGARHVLIAT
DGVFSMDGVIANLKGVCDLADKYDALVMVDDSHAVGFVGENGRGSHEYCDVMGRVDIITG
TLGKALGGASGGYTAARKEVVEWLRQRSRPYLFSNSLAPAIVAASIKVLEMVEAGSELRD
RLWANARQFREQMSAAGFTLAGADHAIIPVMLGDAVVAQKFARELQKEGIYVTGFFYPVV
PKGQARIRTQMSAAHTPEQITRAVEAFTRIGKQLGVIA
Number of residues
398
Molecular Weight
43116.625
Theoretical pI
5.83
GO Classification
Functions
glycine C-acetyltransferase activity / ligase activity / metal ion binding / pyridoxal phosphate binding
Processes
biosynthetic process / L-threonine catabolic process to glycine
Components
cytoplasm / cytosol
General Function
Pyridoxal phosphate binding
Specific Function
Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0011484|2-amino-3-ketobutyrate coenzyme A ligase (kbl)
ATGCGTGGAGAATTTTATCAGCAGTTAACCAACGATCTGGAAACCGCACGGGCGGAAGGG
TTGTTTAAAGAAGAGCGCATTATTACGTCTGCGCAGCAAGCAGATATCACTGTGGCTGAT
GGAAGCCACGTCATTAACTTTTGTGCCAACAACTATCTCGGGCTGGCGAATCATCCTGAT
CTGATTGCGGCGGCAAAGGCGGGAATGGATTCTCACGGTTTCGGCATGGCTTCGGTGCGT
TTTATTTGCGGCACTCAGGACAGCCATAAAGAGCTTGAACAAAAACTGGCGGCCTTCCTG
GGGATGGAAGATGCGATTCTCTACTCTTCCTGCTTTGATGCTAACGGTGGCCTGTTTGAA
ACGCTTCTGGGTGCGGAAGACGCCATTATCTCCGACGCACTGAACCACGCGTCTATTATT
GATGGTGTGCGTCTGTGCAAAGCTAAACGCTATCGCTATGCCAACAACGATATGCAGGAG
CTGGAAGCACGTCTGAAAGAAGCGCGTGAAGCCGGTGCGCGTCATGTGCTGATCGCCACC
GATGGTGTGTTCTCAATGGACGGCGTGATTGCCAACCTGAAGGGCGTTTGCGATCTGGCA
GATAAATATGATGCCCTGGTGATGGTAGACGACTCCCACGCGGTCGGTTTTGTCGGTGAA
AATGGTCGTGGTTCCCATGAATACTGCGATGTGATGGGCCGGGTCGATATTATCACCGGT
ACGCTTGGTAAAGCGCTGGGCGGGGCTTCTGGTGGTTATACCGCGGCGCGCAAAGAAGTG
GTTGAGTGGCTGCGCCAGCGTTCTCGTCCGTACCTGTTCTCCAACTCGCTGGCACCGGCC
ATTGTTGCCGCGTCCATCAAAGTACTGGAGATGGTCGAAGCGGGCAGCGAACTGCGTGAC
CGTCTGTGGGCGAACGCGCGTCAGTTCCGTGAGCAAATGTCGGCGGCGGGCTTTACCCTG
GCGGGAGCCGATCACGCCATTATTCCGGTCATGCTTGGTGATGCGGTAGTGGCGCAGAAA
TTTGCCCGTGAGCTGCAAAAAGAGGGCATTTACGTTACCGGTTTCTTCTATCCGGTCGTT
CCGAAAGGTCAGGCGCGTATTCGTACCCAGATGTCTGCGGCGCATACCCCTGAGCAAATT
ACGCGTGCAGTAGAAGCATTTACGCGTATTGGTAAACAACTGGGCGTTATCGCCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0AB77
UniProtKB Entry NameKBL_ECOLI
GenBank Gene IDX06690
General References
  1. Aronson BD, Ravnikar PD, Somerville RL: Nucleotide sequence of the 2-amino-3-ketobutyrate coenzyme A ligase (kbl) gene of E. coli. Nucleic Acids Res. 1988 Apr 25;16(8):3586. [Article]
  2. Sofia HJ, Burland V, Daniels DL, Plunkett G 3rd, Blattner FR: Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes. Nucleic Acids Res. 1994 Jul 11;22(13):2576-86. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. Mukherjee JJ, Dekker EE: 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. 1987 Oct 25;262(30):14441-7. [Article]
  6. Mukherjee JJ, Dekker EE: 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. 1990 Jan 19;1037(1):24-9. [Article]
  7. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
  8. Schmidt A, Sivaraman J, Li Y, Larocque R, Barbosa JA, Smith C, Matte A, Schrag JD, Cygler M: Three-dimensional structure of 2-amino-3-ketobutyrate CoA ligase from Escherichia coli complexed with a PLP-substrate intermediate: inferred reaction mechanism. Biochemistry. 2001 May 1;40(17):5151-60. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB039152-Amino-3-Ketobutyric AcidexperimentalunknownDetails