KHG/KDPG aldolase

NameKHG/KDPG aldolase
Synonyms
  • hga
  • kdgA
Gene Nameeda
OrganismEscherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0011505|KHG/KDPG aldolase
MKNWKTSAESILTTGPVVPVIVVKKLEHAVPMAKALVAGGVRVLEVTLRTECAVDAIRAI
AKEVPEAIVGAGTVLNPQQLAEVTEAGAQFAISPGLTEPLLKAATEGTIPLIPGISTVSE
LMLGMDYGLKEFKFFPAEANGGVKALQAIAGPFSQVRFCPTGGISPANYRDYLALKSVLC
IGGSWLVPADALEAGDYDRITKLAREAVEGAKL
Number of residuesNone
Molecular Weight22283.8
Theoretical pI5.35
GO Classification
Functions
  • identical protein binding
  • 2-dehydro-3-deoxy-phosphogluconate aldolase activity
  • 4-hydroxy-2-oxoglutarate aldolase activity
Processes
Components
  • membrane
  • cytosol
General FunctionIdentical protein binding
Specific FunctionInvolved in the degradation of glucose via the Entner-Doudoroff pathway. Catalyzes the reversible, stereospecific retro-aldol cleavage of 2-Keto-3-deoxy-6-phosphogluconate (KDPG) to pyruvate and D-glyceraldehyde-3-phosphate. In the synthetic direction, it catalyzes the addition of pyruvate to electrophilic aldehydes with si-facial selectivity. It accepts some nucleophiles other than pyruvate, including 2-oxobutanoate, phenylpyruvate, and fluorobutanoate. It has a preference for the S-configuration at C2 of the electrophile.
Transmembrane Regions
GenBank Protein ID
UniProtKB IDP0A955
UniProtKB Entry Name
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0011506|KHG/KDPG aldolase (eda)
ATGAAAAACTGGAAAACAAGTGCAGAATCAATCCTGACCACCGGCCCGGTTGTACCGGTT
ATCGTGGTAAAAAAACTGGAACACGCGGTGCCGATGGCAAAAGCGTTGGTTGCTGGTGGG
GTGCGCGTTCTGGAAGTGACTCTGCGTACCGAGTGTGCAGTTGACGCTATCCGTGCTATC
GCCAAAGAAGTGCCTGAAGCGATTGTGGGTGCCGGTACGGTGCTGAATCCACAGCAGCTG
GCAGAAGTCACTGAAGCGGGTGCACAGTTCGCAATTAGCCCGGGTCTGACCGAGCCGCTG
CTGAAAGCTGCTACCGAAGGGACTATTCCTCTGATTCCGGGGATCAGCACTGTTTCCGAA
CTGATGCTGGGTATGGACTACGGTTTGAAAGAGTTCAAATTCTTCCCGGCTGAAGCTAAC
GGCGGCGTGAAAGCCCTGCAGGCGATCGCGGGTCCGTTCTCCCAGGTCCGTTTCTGCCCG
ACGGGTGGTATTTCTCCGGCTAACTACCGTGACTACCTGGCGCTGAAAAGCGTGCTGTGC
ATCGGTGGTTCCTGGCTGGTTCCGGCAGATGCGCTGGAAGCGGGCGATTACGACCGCATT
ACTAAGCTGGCGCGTGAAGCTGTAGAAGGCGCTAAGCTGTAA
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC ID
Chromosome LocationNone
LocusNone
References
  1. Vlahos CJ, Dekker EE: The complete amino acid sequence and identification of the active-site arginine peptide of Escherichia coli 2-keto-4-hydroxyglutarate aldolase. J Biol Chem. 1988 Aug 25;263(24):11683-91. [3136164 ]
  2. Patil RV, Dekker EE: Cloning, nucleotide sequence, overexpression, and inactivation of the Escherichia coli 2-keto-4-hydroxyglutarate aldolase gene. J Bacteriol. 1992 Jan;174(1):102-7. [1339418 ]
  3. Egan SE, Fliege R, Tong S, Shibata A, Wolf RE 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. 1992 Jul;174(14):4638-46. [1624451 ]
  4. Carter AT, Pearson BM, Dickinson JR, Lancashire WE: Sequence of the Escherichia coli K-12 edd and eda genes of the Entner-Doudoroff pathway. Gene. 1993 Aug 16;130(1):155-6. [8344525 ]
  5. Itoh T, Aiba H, Baba T, 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, Horiuchi T, et al.: 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. 1996 Dec 31;3(6):379-92. [9097040 ]
  6. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [9278503 ]
  7. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [16738553 ]
  8. Vlahos CJ, Dekker EE: Active-site residues of 2-keto-4-hydroxyglutarate aldolase from Escherichia coli. Bromopyruvate inactivation and labeling of glutamate 45. J Biol Chem. 1990 Nov 25;265(33):20384-9. [1978721 ]
  9. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [9298644 ]
  10. Walters MJ, Srikannathasan V, McEwan AR, Naismith JH, Fierke CA, Toone EJ: Characterization and crystal structure of Escherichia coli KDPGal aldolase. Bioorg Med Chem. 2008 Jan 15;16(2):710-20. Epub 2007 Oct 18. [17981470 ]
  11. 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. 2001 Mar 27;98(7):3679-84. [11274385 ]
  12. Wymer N, Buchanan LV, Henderson D, Mehta N, Botting CH, Pocivavsek L, Fierke CA, Toone EJ, Naismith JH: Directed evolution of a new catalytic site in 2-keto-3-deoxy-6-phosphogluconate aldolase from Escherichia coli. Structure. 2001 Jan 10;9(1):1-9. [11342129 ]
  13. Fullerton SW, Griffiths JS, Merkel AB, Cheriyan M, Wymer NJ, Hutchins MJ, Fierke CA, Toone EJ, Naismith JH: Mechanism of the Class I KDPG aldolase. Bioorg Med Chem. 2006 May 1;14(9):3002-10. Epub 2006 Jan 5. [16403639 ]

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