ID KBL_ECOLI STANDARD; PRT; 398 AA. AC P0AB77; P07912; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 04-APR-2006, entry version 7. DE 2-amino-3-ketobutyrate coenzyme A ligase (EC 2.3.1.29) (AKB ligase) DE (Glycine acetyltransferase). GN Name=kbl; OrderedLocusNames=b3617; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX MEDLINE=88233955; PubMed=3287333; RA Aronson B.D., Ravnikar P.D., Somerville R.L.; RT "Nucleotide sequence of the 2-amino-3-ketobutyrate coenzyme A ligase RT (kbl) gene of E. coli."; RL Nucleic Acids Res. 16:3586-3586(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12 / MG1655; RX MEDLINE=94316500; PubMed=8041620; RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.; RT "Analysis of the Escherichia coli genome. V. DNA sequence of the RT region from 76.0 to 81.5 minutes."; RL Nucleic Acids Res. 22:2576-2586(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21. RX MEDLINE=88032988; PubMed=3117785; RA Mukherjee J.J., Dekker E.E.; RT "Purification, properties, and N-terminal amino acid sequence of RT homogeneous Escherichia coli 2-amino-3-ketobutyrate CoA ligase, a RT pyridoxal phosphate-dependent enzyme."; RL J. Biol. Chem. 262:14441-14447(1987). RN [5] RP PROTEIN SEQUENCE OF 235-257, AND PYRIDOXAL PHOSPHATE-BINDING SITE RP LYS-244. RX MEDLINE=90105507; PubMed=2104756; DOI=10.1016/0167-4838(90)90097-Y; RA Mukherjee J.J., Dekker E.E.; RT "2-amino-3-ketobutyrate CoA ligase of Escherichia coli: stoichiometry RT of pyridoxal phosphate binding and location of the pyridoxyllysine RT peptide in the primary structure of the enzyme."; RL Biochim. Biophys. Acta 1037:24-29(1990). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX MEDLINE=21218591; PubMed=11318637; RA Schmidt A., Sivaraman J., Li Y., Larocque R., Barbosa J.A., Smith C., RA Matte A., Schrag J.D., Cygler M.; RT "Three-dimensional structure of 2-amino-3-ketobutyrate CoA ligase from RT Escherichia coli complexed with a PLP-substrate intermediate: inferred RT reaction mechanism."; RL Biochemistry 40:5151-5160(2001). CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + glycine = CoA + 2-amino-3- CC oxobutanoate. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- SUBUNIT: Homodimer. CC -!- INTERACTION: CC P76104:ydcP; NbExp=1; IntAct=EBI-560602, EBI-556974; CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent CC aminotransferase family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X06690; CAA29883.1; -; Genomic_DNA. DR EMBL; U00039; AAB18594.1; -; Genomic_DNA. DR EMBL; U00096; AAC76641.1; -; Genomic_DNA. DR PIR; C65162; XUECGA. DR PDB; 1FC4; X-ray; A/B=1-398. DR IntAct; P0AB77; -. DR ECO2DBASE; G042.2; 6TH EDITION. DR GenomeReviews; U00096_GR; b3617. DR EchoBASE; EB0507; -. DR EcoGene; EG10512; kbl. DR BioCyc; EcoCyc:AKBLIG-MONOMER; -. DR InterPro; IPR011282; 2am3keto_CoA. DR InterPro; IPR004839; Aminotrans_I/II. DR InterPro; IPR001917; Aminotrans_II. DR PANTHER; PTHR13693:SF8; 2am3keto_CoA; 1. DR Pfam; PF00155; Aminotran_1_2; 1. DR TIGRFAMs; TIGR01822; 2am3keto_CoA; 1. DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1. KW 3D-structure; Acyltransferase; Complete proteome; KW Direct protein sequencing; Pyridoxal phosphate; Transferase. FT CHAIN 1 398 2-amino-3-ketobutyrate coenzyme A ligase. FT /FTId=PRO_0000163843. FT BINDING 244 244 Pyridoxal phosphate (covalent). FT CONFLICT 43 43 H -> Q (in Ref. 1). FT CONFLICT 171 171 A -> R (in Ref. 1). FT CONFLICT 183 183 V -> L (in Ref. 1). FT HELIX 2 18 FT TURN 19 20 FT STRAND 28 28 FT STRAND 35 38 FT TURN 39 40 FT STRAND 43 46 FT TURN 52 53 FT TURN 56 57 FT HELIX 59 72 FT HELIX 80 83 FT STRAND 86 86 FT HELIX 87 100 FT TURN 101 101 FT STRAND 104 108 FT HELIX 111 116 FT TURN 117 118 FT HELIX 119 122 FT TURN 125 126 FT STRAND 128 132 FT TURN 133 134 FT HELIX 137 144 FT TURN 145 145 FT STRAND 149 153 FT TURN 155 156 FT HELIX 158 170 FT TURN 171 172 FT STRAND 176 181 FT STRAND 183 184 FT TURN 185 188 FT STRAND 189 190 FT HELIX 193 202 FT TURN 203 204 FT STRAND 205 210 FT TURN 212 217 FT TURN 220 221 FT HELIX 225 228 FT TURN 229 230 FT TURN 232 233 FT STRAND 237 241 FT TURN 245 246 FT STRAND 252 256 FT HELIX 258 267 FT HELIX 269 273 FT HELIX 279 293 FT TURN 294 294 FT HELIX 296 315 FT TURN 316 317 FT STRAND 320 320 FT STRAND 327 333 FT HELIX 335 347 FT TURN 348 349 FT STRAND 350 351 FT STRAND 354 355 FT TURN 357 358 FT TURN 362 363 FT STRAND 365 370 FT TURN 373 374 FT HELIX 377 393 FT TURN 394 395 SQ SEQUENCE 398 AA; 43117 MW; 7E6E5DC4AA2F84F5 CRC64; MRGEFYQQLT NDLETARAEG LFKEERIITS AQQADITVAD GSHVINFCAN NYLGLANHPD LIAAAKAGMD SHGFGMASVR FICGTQDSHK ELEQKLAAFL GMEDAILYSS CFDANGGLFE TLLGAEDAII SDALNHASII DGVRLCKAKR YRYANNDMQE LEARLKEARE AGARHVLIAT DGVFSMDGVI ANLKGVCDLA DKYDALVMVD DSHAVGFVGE NGRGSHEYCD VMGRVDIITG TLGKALGGAS GGYTAARKEV VEWLRQRSRP YLFSNSLAPA IVAASIKVLE MVEAGSELRD RLWANARQFR EQMSAAGFTL AGADHAIIPV MLGDAVVAQK FARELQKEGI YVTGFFYPVV PKGQARIRTQ MSAAHTPEQI TRAVEAFTRI GKQLGVIA //