Sequence of KBL_ECOLI
EC Number:2.3.1.29
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
acetyl-CoA + glycine = CoA + L-2-amino-3-oxobutanoate
Other sequences found for EC No. 2.3.1.29
General information:
Sequence
0 MRGEFYQQLT NDLETARAEG LFKEERIITS AQQADITVAD GSHVINFCAN NYLGLANHPD
60 LIAAAKAGMD SHGFGMASVR FICGTQDSHK ELEQKLAAFL GMEDAILYSS CFDANGGLFE
120 TLLGAEDAII SDALNHASII DGVRLCKAKR YRYANNDMQE LEARLKEARE AGARHVLIAT
180 DGVFSMDGVI ANLKGVCDLA DKYDALVMVD DSHAVGFVGE NGRGSHEYCD VMGRVDIITG
240 TLGKALGGAS GGYTAARKEV VEWLRQRSRP YLFSNSLAPA IVAASIKVLE MVEAGSELRD
300 RLWANARQFR EQMSAAGFTL AGADHAIIPV MLGDAVVAQK FARELQKEGI YVTGFFYPVV
360 PKGQARIRTQ MSAAHTPEQI TRAVEAFTRI GKQLGVIA
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
815637
Aronson B.D.,Ravnikar P.D.,Somerville R.L.
Nucleotide sequence of the 2-amino-3-ketobutyrate coenzyme A ligase (kbl) gene of E. coli.
Nucleic Acids Res.
16
3586-3586
1988
815638
Sofia H.J.,Burland V.,Daniels D.L.,Plunkett G. III,Blattner F.R.
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
1994
815639
Blattner F.R.,Plunkett G. III,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.
The complete genome sequence of Escherichia coli K-12.
Science
277
1453-1462
1997
815640
Hayashi K.,Morooka N.,Yamamoto Y.,Fujita K.,Isono K.,Choi S.,Ohtsubo E.,Baba T.,Wanner B.L.,Mori H.,Horiuchi T.
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.
Mol. Syst. Biol.
2
0-0
2006
815641
Mukherjee J.J.,Dekker E.E.
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
1987
815642
Mukherjee J.J.,Dekker E.E.
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
1990
815643
VanBogelen R.A.,Abshire K.Z.,Moldover B.,Olson E.R.,Neidhardt F.C.
Escherichia coli proteome analysis using the gene-protein database.
Electrophoresis
18
1243-1251
1997
815644
Schmidt A.,Sivaraman J.,Li Y.,Larocque R.,Barbosa J.A.,Smith C.,Matte A.,Schrag J.D.,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
40
5151-5160
2001
