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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)DescriptionActionsGraphical viewLength
Binding sitei136SubstrateUniRule annotation1 Publication1
Binding sitei185Pyridoxal phosphateUniRule annotation1 Publication1
Binding sitei368SubstrateUniRule annotation1 Publication1

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.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
ChainiPRO_00001638431 – 3982-amino-3-ketobutyrate coenzyme A ligaseAdd BLAST398

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei244N6-(pyridoxal phosphate)lysine1

Proteomic databases

EPDiP0AB77.
PaxDbiP0AB77.
PRIDEiP0AB77.

Interactioni

Subunit structurei

Homodimer.UniRule annotation2 Publications

Protein-protein interaction databases

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

Structurei

Secondary structure

1398
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1 – 18Combined sources18
Beta strandi32 – 38Combined sources7
Beta strandi43 – 46Combined sources4
Helixi59 – 72Combined sources14
Turni80 – 83Combined sources4
Helixi87 – 100Combined sources14
Beta strandi103 – 109Combined sources7
Helixi111 – 116Combined sources6
Helixi119 – 122Combined sources4
Beta strandi128 – 132Combined sources5
Helixi137 – 144Combined sources8
Beta strandi148 – 153Combined sources6
Helixi158 – 170Combined sources13
Beta strandi174 – 183Combined sources10
Turni185 – 187Combined sources3
Helixi193 – 202Combined sources10
Beta strandi205 – 210Combined sources6
Turni212 – 217Combined sources6
Helixi225 – 228Combined sources4
Beta strandi236 – 244Combined sources9
Beta strandi248 – 250Combined sources3
Beta strandi252 – 256Combined sources5
Helixi258 – 267Combined sources10
Helixi269 – 273Combined sources5
Helixi279 – 293Combined sources15
Helixi296 – 315Combined sources20
Beta strandi323 – 333Combined sources11
Helixi335 – 347Combined sources13
Beta strandi365 – 370Combined sources6
Helixi377 – 393Combined sources17

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP0AB77.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni111 – 112Pyridoxal phosphate binding2
Regioni210 – 213Pyridoxal phosphate binding4
Regioni241 – 244Pyridoxal phosphate binding4
Regioni274 – 275Pyridoxal phosphate binding; shared with dimeric partner2

Sequence similaritiesi

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

Phylogenomic databases

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

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00985. 2am3keto_CoA_ligase. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti43H → Q in CAA29883 (PubMed:3287333).Curated1
Sequence conflicti171A → R in CAA29883 (PubMed:3287333).Curated1
Sequence conflicti183V → L in CAA29883 (PubMed:3287333).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FC4X-ray2.00A/B1-398[»]
ProteinModelPortaliP0AB77.
SMRiP0AB77.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263301. 13 interactors.
DIPiDIP-48030N.
IntActiP0AB77. 6 interactors.
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.
PhylomeDBiP0AB77.

Enzyme and pathway databases

UniPathwayiUPA00046; UER00506.
BioCyciEcoCyc:AKBLIG-MONOMER.
ECOL316407:JW3592-MONOMER.
MetaCyc:AKBLIG-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. 1 hit.
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...

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: November 2, 2016
This is version 97 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.