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Sequence of ALKH_ECOLI

EC Number:4.1.2.14

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
2-dehydro-3-deoxy-phosphogluconate aldolase
P0A955
Escherichia coli (strain K12)
213
22284
Reaction
2-dehydro-3-deoxy-6-phospho-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate
Other sequences found for EC No. 4.1.2.14

EC Number:4.1.3.16

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
4-Hydroxy-2-oxoglutarate aldolase
P0A955
Escherichia coli (strain K12)
213
22284
Reaction
4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate
Other sequences found for EC No. 4.1.3.16

EC Number:4.1.3.42

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
(4S)-4-hydroxy-2-oxoglutarate aldolase
P0A955
Escherichia coli (strain K12)
213
22284
Reaction
(4S)-4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate
Other sequences found for EC No. 4.1.3.42

General information:

Sequence
show sequence in fasta format
  0 MKNWKTSAES ILTTGPVVPV IVVKKLEHAV PMAKALVAGG VRVLEVTLRT ECAVDAIRAI
 60 AKEVPEAIVG AGTVLNPQQL AEVTEAGAQF AISPGLTEPL LKAATEGTIP LIPGISTVSE
120 LMLGMDYGLK EFKFFPAEAN GGVKALQAIA GPFSQVRFCP TGGISPANYR DYLALKSVLC
180 IGGSWLVPAD ALEAGDYDRI TKLAREAVEG AKL
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
513267
Vlahos C.J.,Dekker E.E.
The complete amino acid sequence and identification of the active-site arginine peptide of Escherichia coli 2-keto-4-hydroxyglutarate aldolase.
J. Biol. Chem.
263
11683-11691
1988
513268
Patil R.V.,Dekker E.E.
Cloning, nucleotide sequence, overexpression, and inactivation of the Escherichia coli 2-keto-4-hydroxyglutarate aldolase gene.
J. Bacteriol.
174
102-107
1992
513269
Egan S.E.,Fliege R.,Tong S.,Shibata A.,Wolf R.E. Jr.,Conway T.
Molecular characterization of the Entner-Doudoroff pathway in Escherichia coli: sequence analysis and localization of promoters for the edd-eda operon.
J. Bacteriol.
174
4638-4646
1992
513271
Carter A.T.,Pearson B.M.,Dickinson J.R.,Lancashire W.E.
Sequence of the Escherichia coli K-12 edd and eda genes of the Entner-Doudoroff pathway.
Gene
130
155-156
1993
513272
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.,Nakamura Y.,Nashimoto H.,Nishio Y.,Oshima T.,Saito N.,Sampei G.,Seki Y.,Sivasundaram S.,Tagami H.,Takeda J.,Takemoto K.,Wada C.,Yamamoto Y.,Horiuchi T.
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.
DNA Res.
3
379-392
1996
513273
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.
The complete genome sequence of Escherichia coli K-12.
Science
277
1453-1462
1997
513274
Hayashi K.,Morooka N.,Yamamoto Y.,Fujita K.,Isono K.,Choi S.,Ohtsubo E.,Baba T.,Wanner B.L.,Mori H.,Horiuchi T.
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.
Mol. Syst. Biol.
2
0-0
2006
513275
Vlahos C.J.,Dekker E.E.
Active-site residues of 2-keto-4-hydroxyglutarate aldolase from Escherichia coli. Bromopyruvate inactivation and labeling of glutamate 45.
J. Biol. Chem.
265
20384-20389
1990
513276
VanBogelen R.A.,Abshire K.Z.,Moldover B.,Olson E.R.,Neidhardt F.C.
Escherichia coli proteome analysis using the gene-protein database.
Electrophoresis
18
1243-1251
1997
513277
Walters M.J.,Srikannathasan V.,McEwan A.R.,Naismith J.H.,Fierke C.A.,Toone E.J.
Characterization and crystal structure of Escherichia coli KDPGal aldolase.
Bioorg. Med. Chem.
16
710-720
2008
513278
Allard J.,Grochulski P.,Sygusch J.
Covalent intermediate trapped in 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase structure at 1.95-A resolution.
Proc. Natl. Acad. Sci. U.S.A.
98
3679-3684
2001
513279
Wymer N.,Buchanan L.V.,Henderson D.,Mehta N.,Botting C.H.,Pocivavsek L.,Fierke C.A.,Toone E.J.,Naismith J.H.
Directed evolution of a new catalytic site in 2-keto-3-deoxy-6-phosphogluconate aldolase from Escherichia coli.
Structure
9
1-9
2001
513280
Fullerton S.W.,Griffiths J.S.,Merkel A.B.,Cheriyan M.,Wymer N.J.,Hutchins M.J.,Fierke C.A.,Toone E.J.,Naismith J.H.
Mechanism of the Class I KDPG aldolase.
Bioorg. Med. Chem.
14
3002-3010
2006