2-amino-3-ketobutyrate coenzyme A ligase - Escherichia coli (strain K12)

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P0AB77 (KBL_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 75. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
2-amino-3-ketobutyrate coenzyme A ligase
Short name=AKB ligase
EC=2.3.1.29

Alternative name(s):
Glycine acetyltransferase

Gene names

Name:	kbl
Ordered Locus Names:	b3617, JW3592

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	398 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. Ref.6
Catalytic activity	Acetyl-CoA + glycine = CoA + 2-amino-3-oxobutanoate. Ref.6
Cofactor	Binds 1 pyridoxal phosphate per subunit. Ref.6
Pathway	Amino-acid degradation; L-threonine degradation via oxydo-reductase pathway; glycine from L-threonine: step 2/2.
Subunit structure	Homodimer. Ref.6 Ref.8
Sequence similarities	Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
Ligand	Pyridoxal phosphate
Molecular function	Acyltransferase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	L-threonine catabolic process to glycine Inferred from electronic annotation. Source: UniProtKB-UniPathway biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from direct assay Ref.8. Source: EcoliWiki
Molecular_function	glycine C-acetyltransferase activity Inferred from electronic annotation. Source: EC ligase activity Inferred from direct assay Ref.5. Source: EcoliWiki metal ion binding Inferred from direct assay Ref.5. Source: EcoliWiki pyridoxal phosphate binding Inferred from direct assay Ref.8 Ref.5. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 398

398

2-amino-3-ketobutyrate coenzyme A ligase

PRO_0000163843

Regions

Region

111 – 112

Pyridoxal phosphate binding

Region

210 – 213

Pyridoxal phosphate binding

Region

241 – 244

Pyridoxal phosphate binding

Region

274 – 275

Pyridoxal phosphate binding

Sites

Binding site

136

Pyridoxal phosphate

Binding site

136

Substrate

Binding site

185

Pyridoxal phosphate

Binding site

185

Substrate

Binding site

213

Substrate

Binding site

244

Substrate

Binding site

368

Substrate

Amino acid modifications

Modified residue

244

N6-(pyridoxal phosphate)lysine

Experimental info

Sequence conflict

H → Q in CAA29883. Ref.1

Sequence conflict

171

A → R in CAA29883. Ref.1

Sequence conflict

183

V → L in CAA29883. Ref.1

Secondary structure

398

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AB77 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 7E6E5DC4AA2F84F5
Show »

FASTA

398

43,117

        10         20         30         40         50         60 
MRGEFYQQLT NDLETARAEG LFKEERIITS AQQADITVAD GSHVINFCAN NYLGLANHPD 

        70         80         90        100        110        120 
LIAAAKAGMD SHGFGMASVR FICGTQDSHK ELEQKLAAFL GMEDAILYSS CFDANGGLFE 

       130        140        150        160        170        180 
TLLGAEDAII SDALNHASII DGVRLCKAKR YRYANNDMQE LEARLKEARE AGARHVLIAT 

       190        200        210        220        230        240 
DGVFSMDGVI ANLKGVCDLA DKYDALVMVD DSHAVGFVGE NGRGSHEYCD VMGRVDIITG 

       250        260        270        280        290        300 
TLGKALGGAS GGYTAARKEV VEWLRQRSRP YLFSNSLAPA IVAASIKVLE MVEAGSELRD 

       310        320        330        340        350        360 
RLWANARQFR EQMSAAGFTL AGADHAIIPV MLGDAVVAQK FARELQKEGI YVTGFFYPVV 

       370        380        390 
PKGQARIRTQ MSAAHTPEQI TRAVEAFTRI GKQLGVIA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X06690 Genomic DNA. Translation: CAA29883.1.
U00039 Genomic DNA. Translation: AAB18594.1.
U00096 Genomic DNA. Translation: AAC76641.1.
AP009048 Genomic DNA. Translation: BAE77675.1.

PIR

XUECGA. C65162.

RefSeq

NP_418074.1. NC_000913.2.
YP_491816.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FC4	X-ray	2.00	A/B	1-398	[»]

ProteinModelPortal

P0AB77.

SMR

P0AB77. Positions 1-398.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48030N.

IntAct

P0AB77. 6 interactions.

MINT

MINT-1315923.

STRING

511145.b3617.

Proteomic databases

PaxDb

P0AB77.

PRIDE

P0AB77.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76641; AAC76641; b3617.
BAE77675; BAE77675; BAE77675.

GeneID

12934307.
948138.

KEGG

ecj:Y75_p3557.
eco:b3617.

PATRIC

32122721. VBIEscCol129921_3737.

Organism-specific databases

EchoBASE

EB0507.

EcoGene

EG10512. kbl.

Phylogenomic databases

eggNOG

COG0156.

HOGENOM

HOG000221022.

K00639.

OMA

GTHEYCD.

ProtClustDB

PRK06939.

Enzyme and pathway databases

BioCyc

EcoCyc:AKBLIG-MONOMER.
ECOL316407:JW3592-MONOMER.
MetaCyc:AKBLIG-MONOMER.

BRENDA

2.3.1.29. 2026.

SABIO-RK

P0AB77.

UniPathway

UPA00046; UER00506.

Gene expression databases

Genevestigator

P0AB77.

Family and domain databases

Gene3D

3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.

InterPro

IPR011282. 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]

Pfam

PF00155. Aminotran_1_2. 1 hit.
[Graphical view]

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

TIGRFAMs

TIGR01822. 2am3keto_CoA. 1 hit.

PROSITE

PS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0AB77.

Entry information

Entry name

KBL_ECOLI

Accession

Primary (citable) accession number: P0AB77
Secondary accession number(s): P07912, Q2M7T1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	November 8, 2005
Last modified:	May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents