ID KBL_ECOLI Reviewed; 398 AA. AC P0AB77; P07912; Q2M7T1; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 27-JUL-2011, entry version 59. DE RecName: Full=2-amino-3-ketobutyrate coenzyme A ligase; DE Short=AKB ligase; DE EC=2.3.1.29; DE AltName: Full=Glycine acetyltransferase; GN Name=kbl; OrderedLocusNames=b3617, JW3592; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX MEDLINE=88233955; PubMed=3287333; DOI=10.1093/nar/16.8.3586; 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 [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=94316500; PubMed=8041620; DOI=10.1093/nar/22.13.2576; 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 / ATCC 47076; 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 [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] 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 [6] RP PROTEIN SEQUENCE OF 235-257, FUNCTION, COFACTOR, CATALYTIC ACTIVITY, RP PYRIDOXAL PHOSPHATE AT LYS-244, AND SUBUNIT. 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 [7] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND RP PYRIDOXAL PHOSPHATE, REACTION MECHANISM, AND SUBUNIT. RX MEDLINE=21218591; PubMed=11318637; DOI=10.1021/bi002204y; 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 -!- FUNCTION: Catalyzes the cleavage of 2-amino-3-ketobutyrate to CC glycine and acetyl-CoA. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + glycine = CoA + 2-amino-3- CC oxobutanoate. CC -!- COFACTOR: Binds 1 pyridoxal phosphate per subunit. CC -!- PATHWAY: Amino-acid degradation; L-threonine degradation via CC oxydo-reductase pathway; glycine from L-threonine: step 2/2. CC -!- SUBUNIT: Homodimer. 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 EMBL; AP009048; BAE77675.1; -; Genomic_DNA. DR PIR; C65162; XUECGA. DR RefSeq; AP_004174.1; AC_000091.1. DR RefSeq; NP_418074.1; NC_000913.2. DR PDB; 1FC4; X-ray; 2.00 A; A/B=1-398. DR PDBsum; 1FC4; -. DR ProteinModelPortal; P0AB77; -. DR SMR; P0AB77; 1-398. DR DIP; DIP-48030N; -. DR MINT; MINT-1315923; -. DR ECO2DBASE; G042.2; 6TH EDITION. DR EnsemblBacteria; EBESCT00000001179; EBESCP00000001179; EBESCG00000000974. DR EnsemblBacteria; EBESCT00000016919; EBESCP00000016210; EBESCG00000015978. DR GeneID; 948138; -. DR GenomeReviews; AP009048_GR; JW3592. DR GenomeReviews; U00096_GR; b3617. DR KEGG; ecj:JW3592; -. DR KEGG; eco:b3617; -. DR EchoBASE; EB0507; -. DR EcoGene; EG10512; kbl. DR eggNOG; COG0156; -. DR GeneTree; EBGT00050000008229; -. DR HOGENOM; HBG649839; -. DR OMA; NNDMAAL; -. DR ProtClustDB; PRK06939; -. DR BioCyc; EcoCyc:AKBLIG-MONOMER; -. DR BioCyc; MetaCyc:AKBLIG-MONOMER; -. DR BRENDA; 2.3.1.29; 2026. DR Genevestigator; P0AB77; -. DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki. DR GO; GO:0008890; F:glycine C-acetyltransferase activity; IEA:EC. DR GO; GO:0016874; F:ligase activity; IDA:EcoliWiki. DR GO; GO:0046872; F:metal ion binding; IDA:EcoliWiki. DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoliWiki. DR GO; GO:0016769; F:transferase activity, transferring nitrogenous groups; IEA:InterPro. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR InterPro; IPR011282; 2am3keto_CoA_ligase. DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR015424; PyrdxlP-dep_Trfase_major_dom. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1. DR Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 1. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1. DR TIGRFAMs; TIGR01822; 2am3keto_CoA; 1. DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1. PE 1: Evidence at protein level; 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 REGION 111 112 Pyridoxal phosphate binding. FT REGION 210 213 Pyridoxal phosphate binding. FT REGION 241 244 Pyridoxal phosphate binding. FT REGION 274 275 Pyridoxal phosphate binding. FT BINDING 136 136 Pyridoxal phosphate. FT BINDING 136 136 Substrate. FT BINDING 185 185 Pyridoxal phosphate. FT BINDING 185 185 Substrate. FT BINDING 213 213 Substrate. FT BINDING 244 244 Substrate. FT BINDING 368 368 Substrate. FT MOD_RES 244 244 N6-(pyridoxal phosphate)lysine. FT CONFLICT 43 43 H -> Q (in Ref. 1; CAA29883). FT CONFLICT 171 171 A -> R (in Ref. 1; CAA29883). FT CONFLICT 183 183 V -> L (in Ref. 1; CAA29883). FT HELIX 1 18 FT STRAND 32 38 FT STRAND 43 46 FT HELIX 59 72 FT TURN 80 83 FT HELIX 87 100 FT STRAND 103 109 FT HELIX 111 116 FT HELIX 119 122 FT STRAND 128 132 FT HELIX 137 144 FT STRAND 148 153 FT HELIX 158 170 FT STRAND 174 183 FT TURN 185 187 FT HELIX 193 202 FT STRAND 205 210 FT TURN 212 217 FT HELIX 225 228 FT STRAND 236 244 FT STRAND 248 250 FT STRAND 252 256 FT HELIX 258 267 FT HELIX 269 273 FT HELIX 279 293 FT HELIX 296 315 FT STRAND 323 333 FT HELIX 335 347 FT STRAND 365 370 FT HELIX 377 393 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 //