KBL_ECOLI
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 03-AUG-2022, entry version 130.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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=acetyl-CoA + glycine = (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_STEB01000024.1.
DR PDB; 1FC4; X-ray; 2.00 A; A/B=1-398.
DR PDBsum; 1FC4; -.
DR AlphaFoldDB; P0AB77; -.
DR SMR; P0AB77; -.
DR BioGRID; 4263301; 17.
DR BioGRID; 852445; 1.
DR DIP; DIP-48030N; -.
DR IntAct; P0AB77; 7.
DR STRING; 511145.b3617; -.
DR DrugBank; DB03915; 2-Amino-3-Ketobutyric Acid.
DR jPOST; P0AB77; -.
DR PaxDb; P0AB77; -.
DR PRIDE; P0AB77; -.
DR EnsemblBacteria; AAC76641; AAC76641; b3617.
DR EnsemblBacteria; BAE77675; BAE77675; BAE77675.
DR GeneID; 66672485; -.
DR GeneID; 948138; -.
DR KEGG; ecj:JW3592; -.
DR KEGG; eco:b3617; -.
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; MDTHGFG; -.
DR PhylomeDB; P0AB77; -.
DR BioCyc; EcoCyc:AKBLIG-MON; -.
DR BioCyc; MetaCyc:AKBLIG-MON; -.
DR BRENDA; 2.3.1.29; 2026.
DR SABIO-RK; P0AB77; -.
DR UniPathway; UPA00046; UER00506.
DR EvolutionaryTrace; P0AB77; -.
DR PRO; PR:P0AB77; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0019518; P:L-threonine catabolic process to glycine; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 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; 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 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 TURN 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..183
FT /evidence="ECO:0007829|PDB:1FC4"
FT TURN 185..187
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 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
