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Protein

2-amino-3-ketobutyrate coenzyme A ligase

Gene

kbl

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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-EC
  • ligase activity Source: EcoliWiki
  • metal ion binding Source: EcoliWiki
  • pyridoxal phosphate binding Source: EcoliWiki

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase
LigandPyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:AKBLIG-MONOMER
MetaCyc:AKBLIG-MONOMER
BRENDAi2.3.1.29 2026
SABIO-RKiP0AB77
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

Pathology & Biotechi

Chemistry databases

DrugBankiDB03915 2-Amino-3-Ketobutyric Acid

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, 17 interactors
DIPiDIP-48030N
IntActiP0AB77, 7 interactors
STRINGi316385.ECDH10B_3799

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
OMAiMDTHGFG
PhylomeDBiP0AB77

Family and domain databases

Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 2 hits
HAMAPiMF_00985 2am3keto_CoA_ligase, 1 hit
InterProiView protein in InterPro
IPR011282 2am3keto_CoA_ligase
IPR001917 Aminotrans_II_pyridoxalP_BS
IPR004839 Aminotransferase_I/II
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
PANTHERiPTHR13693:SF60 PTHR13693:SF60, 1 hit
PfamiView protein in Pfam
PF00155 Aminotran_1_2, 1 hit
SUPFAMiSSF53383 SSF53383, 1 hit
TIGRFAMsiTIGR01822 2am3keto_CoA, 1 hit
PROSITEiView protein in PROSITE
PS00599 AA_TRANSFER_CLASS_2, 1 hit

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
PATRICifig|1411691.4.peg.3089

Similar proteinsi

Entry informationi

Entry nameiKBL_ECOLI
AccessioniPrimary (citable) accession number: P0AB77
Secondary accession number(s): P07912, Q2M7T1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: November 8, 2005
Last modified: March 28, 2018
This is version 107 of the entry and version 1 of the sequence. See 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

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