KHG/KDPG aldolase - Escherichia coli (strain K12)

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P0A955 (ALKH_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 73. 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:
KHG/KDPG aldolase

Including the following 2 domains:

4-hydroxy-2-oxoglutarate aldolase
EC=4.1.3.16
Alternative name(s):
2-keto-4-hydroxyglutarate aldolase
Short name=KHG-aldolase
2-dehydro-3-deoxy-phosphogluconate aldolase
EC=4.1.2.14
Alternative name(s):
2-keto-3-deoxy-6-phosphogluconate aldolase
Short name=KDPG-aldolase
Phospho-2-dehydro-3-deoxygluconate aldolase
Phospho-2-keto-3-deoxygluconate aldolase

Gene names

Name:	eda
Synonyms:	hga, kdgA
Ordered Locus Names:	b1850, JW1839

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	213 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate. 2-dehydro-3-deoxy-D-gluconate 6-phosphate = pyruvate + D-glyceraldehyde 3-phosphate.
Pathway	Carbohydrate acid metabolism; 2-dehydro-3-deoxy-D-gluconate degradation; D-glyceraldehyde 3-phosphate and pyruvate from 2-dehydro-3-deoxy-D-gluconate: step 2/2. Carbohydrate metabolism; glyoxylate and dicarboxylate metabolism.
Subunit structure	Homotrimer.
Subcellular location	Cytoplasm.
Induction	Constitutive, three-fold induction occurs for growth on gluconate and two-fold for growth on hexuronic acids.
Miscellaneous	It also catalyzes the beta-decarboxylation of oxaloacetate.
Sequence similarities	Belongs to the KHG/KDPG aldolase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Schiff base
Molecular function	Lyase
Technical term	3D-structure Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Cellular_component	cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB membrane Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	2-dehydro-3-deoxy-phosphogluconate aldolase activity Inferred from mutant phenotype PubMed 4945194. Source: EcoliWiki 4-hydroxy-2-oxoglutarate aldolase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 213

213

KHG/KDPG aldolase

PRO_0000201037

Sites

Active site

Ref.9

Active site

Ref.9

Active site

133

Schiff-base intermediate with KHG or pyruvate Ref.9

Secondary structure

213

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A955 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: CC8D51B50480D0B7
Show »

FASTA

213

22,284

        10         20         30         40         50         60 
MKNWKTSAES ILTTGPVVPV IVVKKLEHAV PMAKALVAGG VRVLEVTLRT ECAVDAIRAI 

        70         80         90        100        110        120 
AKEVPEAIVG AGTVLNPQQL AEVTEAGAQF AISPGLTEPL LKAATEGTIP LIPGISTVSE 

       130        140        150        160        170        180 
LMLGMDYGLK EFKFFPAEAN GGVKALQAIA GPFSQVRFCP TGGISPANYR DYLALKSVLC 

       190        200        210 
IGGSWLVPAD ALEAGDYDRI TKLAREAVEG AKL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete amino acid sequence and identification of the active-site arginine peptide of Escherichia coli 2-keto-4-hydroxyglutarate aldolase." Vlahos C.J., Dekker E.E. J. Biol. Chem. 263:11683-11691(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: K12.
[2]	"Cloning, nucleotide sequence, overexpression, and inactivation of the Escherichia coli 2-keto-4-hydroxyglutarate aldolase gene." Patil R.V., Dekker E.E. J. Bacteriol. 174:102-107(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Molecular characterization of the Entner-Doudoroff pathway in Escherichia coli: sequence analysis and localization of promoters for the edd-eda operon." Egan S.E., Fliege R., Tong S., Shibata A., Wolf R.E. Jr., Conway T. J. Bacteriol. 174:4638-4646(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Purine and one-carbon metabolism in Escherichia coli K12: DNA sequence of a second GAR transformylase." Smith J.M., Nygaard P. Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[5]	"Sequence of the Escherichia coli K-12 edd and eda genes of the Entner-Doudoroff pathway." Carter A.T., Pearson B.M., Dickinson J.R., Lancashire W.E. Gene 130:155-156(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[6]	"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. Horiuchi T. DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"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.
[8]	"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.
[9]	"Active-site residues of 2-keto-4-hydroxyglutarate aldolase from Escherichia coli. Bromopyruvate inactivation and labeling of glutamate 45." Vlahos C.J., Dekker E.E. J. Biol. Chem. 265:20384-20389(1990) [PubMed] [Europe PMC] [Abstract] Cited for: ACTIVE SITE.
[10]	"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.
[11]	"Directed evolution of a new catalytic site in 2-keto-3-deoxy-6-phosphogluconate aldolase from Escherichia coli." Wymer N., Buchanan L.V., Henderson D., Mehta N., Botting C.H., Pocivavsek L., Fierke C.A., Toone E.J., Naismith J.H. Structure 9:1-9(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[12]	"Covalent intermediate trapped in 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase structure at 1.95-A resolution." Allard J., Grochulski P., Sygusch J. Proc. Natl. Acad. Sci. U.S.A. 98:3679-3684(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X68871 Genomic DNA. Translation: CAA48732.1.
M87458 Genomic DNA. Translation: AAA23723.1.
L20897 Genomic DNA. Translation: AAA23862.1.
X63694 Genomic DNA. Translation: CAA45222.1.
U00096 Genomic DNA. Translation: AAC74920.1.
AP009048 Genomic DNA. Translation: BAA15658.1.

PIR

ADECOG. B42986.

RefSeq

NP_416364.1. NC_000913.2.
YP_490112.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EUA	X-ray	1.95	A/B/C	1-213	[»]
1EUN	X-ray	2.00	A/B/C	1-213	[»]
1FQ0	X-ray	2.10	A/B/C	1-213	[»]
1FWR	X-ray	2.70	A/B/C	1-213	[»]
1WAU	X-ray	2.80	A	1-213	[»]
1WBH	X-ray	1.55	A/B/C	1-213	[»]
2C0A	X-ray	1.55	A/B/C	1-213	[»]

ProteinModelPortal

P0A955.

SMR

P0A955. Positions 1-213.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36196N.

IntAct

P0A955. 8 interactions.

STRING

511145.b1850.

2D gel databases

SWISS-2DPAGE

P0A955.

Proteomic databases

PaxDb

P0A955.

PRIDE

P0A955.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74920; AAC74920; b1850.
BAA15658; BAA15658; BAA15658.

GeneID

12930159.
946367.

KEGG

ecj:Y75_p1826.
eco:b1850.

PATRIC

32119021. VBIEscCol129921_1928.

Organism-specific databases

EchoBASE

EB0252.

EcoGene

EG10256. eda.

Phylogenomic databases

eggNOG

COG0800.

HOGENOM

HOG000233114.

K01625.

OMA

AQFAVSP.

ProtClustDB

PRK05718.

Enzyme and pathway databases

BioCyc

EcoCyc:KDPGALDOL-4OH2OXOGLUTARALDOL-MONOMER.
ECOL316407:JW1839-MONOMER.
MetaCyc:KDPGALDOL-4OH2OXOGLUTARALDOL-MONOMER.

UniPathway

UPA00227.
UPA00856; UER00829.

Gene expression databases

Genevestigator

P0A955.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

InterPro

IPR000887. Aldlse_KDPG_KHG.
IPR013785. Aldolase_TIM.
[Graphical view]

Pfam

PF01081. Aldolase. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01182. eda. 1 hit.

PROSITE

PS00159. ALDOLASE_KDPG_KHG_1. 1 hit.
PS00160. ALDOLASE_KDPG_KHG_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A955.

Entry information

Entry name

ALKH_ECOLI

Accession

Primary (citable) accession number: P0A955
Secondary accession number(s): P10177

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	May 1, 2013
This is version 73 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

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel 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