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   02-SEP-2026, entry version 146.
DE   RecName: Full=2-amino-3-ketobutyrate coenzyme A ligase {ECO:0000255|HAMAP-Rule:MF_00985};
DE            Short=AKB ligase {ECO:0000255|HAMAP-Rule:MF_00985};
DE            EC=2.3.1.29 {ECO:0000255|HAMAP-Rule:MF_00985};
DE   AltName: Full=Glycine acetyltransferase {ECO:0000255|HAMAP-Rule:MF_00985};
GN   Name=kbl {ECO:0000255|HAMAP-Rule:MF_00985};
GN   OrderedLocusNames=b3617, JW3592;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   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 (kbl)
RT   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   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 region
RT   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   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., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(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 MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX   PubMed=3117785; DOI=10.1016/s0021-9258(18)47814-3;
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 pyridoxal
RT   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   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 of
RT   pyridoxal phosphate binding and location of the pyridoxyllysine peptide in
RT   the primary structure of the enzyme.";
RL   Biochim. Biophys. Acta 1037:24-29(1990).
RN   [7]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND
RP   PYRIDOXAL PHOSPHATE, REACTION MECHANISM, AND SUBUNIT.
RX   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 glycine
CC       and acetyl-CoA. {ECO:0000255|HAMAP-Rule:MF_00985,
CC       ECO:0000269|PubMed:2104756}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine + acetyl-CoA = (2S)-2-amino-3-oxobutanoate + CoA;
CC         Xref=Rhea:RHEA:20736, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:78948; EC=2.3.1.29;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00985,
CC         ECO:0000269|PubMed:2104756};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00985,
CC         ECO:0000269|PubMed:2104756};
CC       Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00985, ECO:0000269|PubMed:2104756};
CC   -!- PATHWAY: Amino-acid degradation; L-threonine degradation via oxydo-
CC       reductase pathway; glycine from L-threonine: step 2/2.
CC       {ECO:0000255|HAMAP-Rule:MF_00985}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00985,
CC       ECO:0000269|PubMed:11318637, ECO:0000269|PubMed:2104756}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000255|HAMAP-Rule:MF_00985}.
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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; NP_418074.1; NC_000913.3.
DR   RefSeq; WP_001213834.1; NZ_CP009789.1.
DR   PDB; 1FC4; X-ray; 2.00 A; A/B=1-398.
DR   AlphaFoldDB; P0AB77; -.
DR   SMR; P0AB77; -.
DR   BioGRID; 4263301; 22.
DR   BioGRID; 852445; 1.
DR   DIP; DIP-48030N; -.
DR   FunCoup; P0AB77; 606.
DR   IntAct; P0AB77; 7.
DR   STRING; 511145.b3617; -.
DR   DrugBank; DB03915; 2-Amino-3-Ketobutyric Acid.
DR   jPOST; P0AB77; -.
DR   PaxDb; 511145-b3617; -.
DR   EnsemblBacteria; AAC76641; AAC76641; b3617.
DR   GeneID; 75173814; -.
DR   GeneID; 75202189; -.
DR   GeneID; 948138; -.
DR   KEGG; ecj:JW3592; -.
DR   KEGG; eco:b3617; -.
DR   KEGG; ecoc:C3026_19610; -.
DR   PATRIC; fig|1411691.4.peg.3089; -.
DR   EchoBASE; EB0507; -.
DR   eggNOG; COG0156; Bacteria.
DR   HOGENOM; CLU_015846_11_0_6; -.
DR   InParanoid; P0AB77; -.
DR   OMA; GTHEYCD; -.
DR   OrthoDB; 9807157at2; -.
DR   PhylomeDB; P0AB77; -.
DR   BioCyc; EcoCyc:AKBLIG-MONOMER; -.
DR   BioCyc; MetaCyc:AKBLIG-MONOMER; -.
DR   BRENDA; 2.3.1.29; 2026.
DR   SABIO-RK; P0AB77; -.
DR   UniPathway; UPA00046; UER00506.
DR   EvolutionaryTrace; P0AB77; -.
DR   PRO; PR:P0AB77; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P0AB77; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0008890; F:glycine C-acetyltransferase activity; IDA:EcoCyc.
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:0006567; P:L-threonine catabolic process; IEA:InterPro.
DR   CDD; cd06454; KBL_like; 1.
DR   FunFam; 3.90.1150.10:FF:000004; 2-amino-3-ketobutyrate coenzyme A ligase; 1.
DR   FunFam; 3.40.640.10:FF:000006; 5-aminolevulinate synthase, mitochondrial; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_00985; 2am3keto_CoA_ligase; 1.
DR   InterPro; IPR011282; 2am3keto_CoA_ligase.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II_large.
DR   InterPro; IPR050087; AON_synthase_class-II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01822; 2am3keto_CoA; 1.
DR   NCBIfam; NF005394; PRK06939.1; 1.
DR   PANTHER; PTHR13693:SF102; 2-AMINO-3-KETOBUTYRATE COENZYME A LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
DR   PDBsum; 1FC4; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Direct protein sequencing;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..398
FT                   /note="2-amino-3-ketobutyrate coenzyme A ligase"
FT                   /id="PRO_0000163843"
FT   BINDING         111..112
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00985,
FT                   ECO:0000269|PubMed:11318637"
FT   BINDING         185
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00985,
FT                   ECO:0000269|PubMed:11318637"
FT   BINDING         210..213
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT   BINDING         241..244
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT   BINDING         274..275
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT   BINDING         368
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00985,
FT                   ECO:0000269|PubMed:11318637"
FT   MOD_RES         244
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT   CONFLICT        43
FT                   /note="H -> Q (in Ref. 1; CAA29883)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        171
FT                   /note="A -> R (in Ref. 1; CAA29883)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        183
FT                   /note="V -> L (in Ref. 1; CAA29883)"
FT                   /evidence="ECO:0000305"
FT   HELIX           1..18
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   HELIX           23..27
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   STRAND          32..38
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   STRAND          43..46
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   HELIX           59..72
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   HELIX           80..83
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   HELIX           87..100
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   STRAND          103..109
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   HELIX           111..116
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   HELIX           119..122
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   STRAND          128..132
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   HELIX           137..144
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   STRAND          148..153
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   HELIX           158..170
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   STRAND          174..184
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   TURN            185..188
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   HELIX           193..202
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   STRAND          205..210
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   TURN            212..217
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   HELIX           225..228
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   STRAND          236..244
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   STRAND          248..250
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   STRAND          252..256
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   HELIX           258..267
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   HELIX           269..273
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   HELIX           276..278
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   HELIX           279..293
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   HELIX           296..315
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   STRAND          323..333
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   HELIX           335..347
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   STRAND          365..370
FT                   /evidence="ECO:0007829|PDB:1FC4"
FT   HELIX           377..393
FT                   /evidence="ECO:0007829|PDB:1FC4"
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
//