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Protein

2-amino-3-ketobutyrate coenzyme A ligase

Gene

kbl

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA.UniRule annotation1 Publication

Catalytic activityi

Acetyl-CoA + glycine = CoA + 2-amino-3-oxobutanoate.UniRule annotation1 Publication

Cofactori

pyridoxal 5'-phosphateUniRule annotation1 PublicationNote: Binds 1 pyridoxal phosphate per subunit.UniRule annotation1 Publication

Pathwayi: L-threonine degradation via oxydo-reductase pathway

This protein is involved in step 2 of the subpathway that synthesizes glycine from L-threonine.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. L-threonine 3-dehydrogenase (tdh)
  2. 2-amino-3-ketobutyrate coenzyme A ligase (kbl)
This subpathway is part of the pathway L-threonine degradation via oxydo-reductase pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes glycine from L-threonine, the pathway L-threonine degradation via oxydo-reductase pathway and in Amino-acid degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei136 – 1361SubstrateUniRule annotation1 Publication
Binding sitei185 – 1851Pyridoxal phosphateUniRule annotation1 Publication
Binding sitei368 – 3681SubstrateUniRule annotation1 Publication

GO - Molecular functioni

  • glycine C-acetyltransferase activity Source: UniProtKB-HAMAP
  • ligase activity Source: EcoliWiki
  • metal ion binding Source: EcoliWiki
  • pyridoxal phosphate binding Source: EcoliWiki

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:AKBLIG-MONOMER.
ECOL316407:JW3592-MONOMER.
MetaCyc:AKBLIG-MONOMER.
RETL1328306-WGS:GSTH-2990-MONOMER.
BRENDAi2.3.1.29. 2026.
SABIO-RKP0AB77.
UniPathwayiUPA00046; UER00506.

Names & Taxonomyi

Protein namesi
Recommended name:
2-amino-3-ketobutyrate coenzyme A ligaseUniRule annotation (EC:2.3.1.29UniRule annotation)
Short name:
AKB ligaseUniRule annotation
Alternative name(s):
Glycine acetyltransferaseUniRule annotation
Gene namesi
Name:kblUniRule annotation
Ordered Locus Names:b3617, JW3592
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10512. kbl.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3983982-amino-3-ketobutyrate coenzyme A ligasePRO_0000163843Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei244 – 2441N6-(pyridoxal phosphate)lysine

Proteomic databases

EPDiP0AB77.
PaxDbiP0AB77.
PRIDEiP0AB77.

Interactioni

Subunit structurei

Homodimer.UniRule annotation2 Publications

Protein-protein interaction databases

BioGridi4263301. 13 interactions.
DIPiDIP-48030N.
IntActiP0AB77. 6 interactions.
MINTiMINT-1315923.
STRINGi511145.b3617.

Structurei

Secondary structure

398
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 1818Combined sources
Beta strandi32 – 387Combined sources
Beta strandi43 – 464Combined sources
Helixi59 – 7214Combined sources
Turni80 – 834Combined sources
Helixi87 – 10014Combined sources
Beta strandi103 – 1097Combined sources
Helixi111 – 1166Combined sources
Helixi119 – 1224Combined sources
Beta strandi128 – 1325Combined sources
Helixi137 – 1448Combined sources
Beta strandi148 – 1536Combined sources
Helixi158 – 17013Combined sources
Beta strandi174 – 18310Combined sources
Turni185 – 1873Combined sources
Helixi193 – 20210Combined sources
Beta strandi205 – 2106Combined sources
Turni212 – 2176Combined sources
Helixi225 – 2284Combined sources
Beta strandi236 – 2449Combined sources
Beta strandi248 – 2503Combined sources
Beta strandi252 – 2565Combined sources
Helixi258 – 26710Combined sources
Helixi269 – 2735Combined sources
Helixi279 – 29315Combined sources
Helixi296 – 31520Combined sources
Beta strandi323 – 33311Combined sources
Helixi335 – 34713Combined sources
Beta strandi365 – 3706Combined sources
Helixi377 – 39317Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FC4X-ray2.00A/B1-398[»]
ProteinModelPortaliP0AB77.
SMRiP0AB77. Positions 1-398.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AB77.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni111 – 1122Pyridoxal phosphate binding
Regioni210 – 2134Pyridoxal phosphate binding
Regioni241 – 2444Pyridoxal phosphate binding
Regioni274 – 2752Pyridoxal phosphate binding; shared with dimeric partner

Sequence similaritiesi

Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107EEK. Bacteria.
COG0156. LUCA.
HOGENOMiHOG000221022.
InParanoidiP0AB77.
KOiK00639.
OMAiQYVIDAF.
OrthoDBiEOG6Q8HZD.
PhylomeDBiP0AB77.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00985. 2am3keto_CoA_ligase.
InterProiIPR011282. 2am3keto_CoA_ligase.
IPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01822. 2am3keto_CoA. 1 hit.
PROSITEiPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AB77-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRGEFYQQLT NDLETARAEG LFKEERIITS AQQADITVAD GSHVINFCAN
60 70 80 90 100
NYLGLANHPD LIAAAKAGMD SHGFGMASVR FICGTQDSHK ELEQKLAAFL
110 120 130 140 150
GMEDAILYSS CFDANGGLFE TLLGAEDAII SDALNHASII DGVRLCKAKR
160 170 180 190 200
YRYANNDMQE LEARLKEARE AGARHVLIAT DGVFSMDGVI ANLKGVCDLA
210 220 230 240 250
DKYDALVMVD DSHAVGFVGE NGRGSHEYCD VMGRVDIITG TLGKALGGAS
260 270 280 290 300
GGYTAARKEV VEWLRQRSRP YLFSNSLAPA IVAASIKVLE MVEAGSELRD
310 320 330 340 350
RLWANARQFR EQMSAAGFTL AGADHAIIPV MLGDAVVAQK FARELQKEGI
360 370 380 390
YVTGFFYPVV PKGQARIRTQ MSAAHTPEQI TRAVEAFTRI GKQLGVIA
Length:398
Mass (Da):43,117
Last modified:November 8, 2005 - v1
Checksum:i7E6E5DC4AA2F84F5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431H → Q in CAA29883 (PubMed:3287333).Curated
Sequence conflicti171 – 1711A → R in CAA29883 (PubMed:3287333).Curated
Sequence conflicti183 – 1831V → L in CAA29883 (PubMed:3287333).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06690 Genomic DNA. Translation: CAA29883.1.
U00039 Genomic DNA. Translation: AAB18594.1.
U00096 Genomic DNA. Translation: AAC76641.1.
AP009048 Genomic DNA. Translation: BAE77675.1.
PIRiC65162. XUECGA.
RefSeqiNP_418074.1. NC_000913.3.
WP_001213834.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76641; AAC76641; b3617.
BAE77675; BAE77675; BAE77675.
GeneIDi948138.
KEGGiecj:JW3592.
eco:b3617.
PATRICi32122721. VBIEscCol129921_3737.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06690 Genomic DNA. Translation: CAA29883.1.
U00039 Genomic DNA. Translation: AAB18594.1.
U00096 Genomic DNA. Translation: AAC76641.1.
AP009048 Genomic DNA. Translation: BAE77675.1.
PIRiC65162. XUECGA.
RefSeqiNP_418074.1. NC_000913.3.
WP_001213834.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FC4X-ray2.00A/B1-398[»]
ProteinModelPortaliP0AB77.
SMRiP0AB77. Positions 1-398.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263301. 13 interactions.
DIPiDIP-48030N.
IntActiP0AB77. 6 interactions.
MINTiMINT-1315923.
STRINGi511145.b3617.

Proteomic databases

EPDiP0AB77.
PaxDbiP0AB77.
PRIDEiP0AB77.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76641; AAC76641; b3617.
BAE77675; BAE77675; BAE77675.
GeneIDi948138.
KEGGiecj:JW3592.
eco:b3617.
PATRICi32122721. VBIEscCol129921_3737.

Organism-specific databases

EchoBASEiEB0507.
EcoGeneiEG10512. kbl.

Phylogenomic databases

eggNOGiENOG4107EEK. Bacteria.
COG0156. LUCA.
HOGENOMiHOG000221022.
InParanoidiP0AB77.
KOiK00639.
OMAiQYVIDAF.
OrthoDBiEOG6Q8HZD.
PhylomeDBiP0AB77.

Enzyme and pathway databases

UniPathwayiUPA00046; UER00506.
BioCyciEcoCyc:AKBLIG-MONOMER.
ECOL316407:JW3592-MONOMER.
MetaCyc:AKBLIG-MONOMER.
RETL1328306-WGS:GSTH-2990-MONOMER.
BRENDAi2.3.1.29. 2026.
SABIO-RKP0AB77.

Miscellaneous databases

EvolutionaryTraceiP0AB77.
PROiP0AB77.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00985. 2am3keto_CoA_ligase.
InterProiIPR011282. 2am3keto_CoA_ligase.
IPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01822. 2am3keto_CoA. 1 hit.
PROSITEiPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the 2-amino-3-ketobutyrate coenzyme A ligase (kbl) gene of E. coli."
    Aronson B.D., Ravnikar P.D., Somerville R.L.
    Nucleic Acids Res. 16:3586-3586(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
    Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
    Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Purification, properties, and N-terminal amino acid sequence of homogeneous Escherichia coli 2-amino-3-ketobutyrate CoA ligase, a pyridoxal phosphate-dependent enzyme."
    Mukherjee J.J., Dekker E.E.
    J. Biol. Chem. 262:14441-14447(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
  6. "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."
    Mukherjee J.J., Dekker E.E.
    Biochim. Biophys. Acta 1037:24-29(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 235-257, FUNCTION, COFACTOR, CATALYTIC ACTIVITY, PYRIDOXAL PHOSPHATE AT LYS-244, SUBUNIT.
  7. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  8. "Three-dimensional structure of 2-amino-3-ketobutyrate CoA ligase from Escherichia coli complexed with a PLP-substrate intermediate: inferred reaction mechanism."
    Schmidt A., Sivaraman J., Li Y., Larocque R., Barbosa J.A., Smith C., Matte A., Schrag J.D., Cygler M.
    Biochemistry 40:5151-5160(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND PYRIDOXAL PHOSPHATE, REACTION MECHANISM, SUBUNIT.

Entry informationi

Entry nameiKBL_ECOLI
AccessioniPrimary (citable) accession number: P0AB77
Secondary accession number(s): P07912, Q2M7T1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: November 8, 2005
Last modified: March 16, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.