2-amino-3-ketobutyrate coenzyme A ligase
Details
- Name
- 2-amino-3-ketobutyrate coenzyme A ligase
- Kind
- protein
- Synonyms
- 2.3.1.29
- AKB ligase
- Glycine acetyltransferase
- Gene Name
- kbl
- UniProtKB Entry
- P0AB77Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- 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
- Functionsglycine C-acetyltransferase activity / ligase activity / metal ion binding / pyridoxal phosphate bindingProcessesbiosynthetic process / L-threonine catabolic process to glycineComponentscytoplasm / cytosol
- General Function
- Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA.
- Specific Function
- glycine C-acetyltransferase activity
- Pfam Domain Function
- Aminotran_1_2 (PF00155)
- Signal Regions
- Not Available
- 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
Resource Link UniProtKB ID P0AB77 UniProtKB Entry Name KBL_ECOLI GenBank Gene ID X06690 PDB ID(s) 1FC4 KEGG ID ecj:JW3592 NCBI Gene ID 948138 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details 2-Amino-3-Ketobutyric Acid experimental unknown target Details