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4-hydroxy-2-oxoglutarate aldolase (EC 4.1.3.16) (KHG-aldolase) catalyzes the interconversion of 4-hydroxy-2-oxoglutarate into pyruvate and glyoxylate. Phospho-2-dehydro-3-deoxygluconate aldolase (EC 4.1.2.14) (KDPG-aldolase) catalyzes the interconversion of 6-phospho-2-dehydro-3-deoxy-D-gluconate into pyruvate and glyceraldehyde 3-phosphate.

These two enzymes are structurally and functionally related [1]. They are both homotrimeric proteins of approximately 220 amino-acid residues. They are class I aldolases whose catalytic mechanism involves the formation of a Schiff-base intermediate between the substrate and the epsilon-amino group of a lysine residue. In both enzymes, an arginine is required for catalytic activity.

We developed two signature patterns for these enzymes. The first one contains the active site arginine and the second, the lysine involved in the Schiff-base formation.

November 1997 / Patterns and text revised.

PROSITE methods (with tools and information) covered by this documentation:

ALDOLASE_KDPG_KHG_1, PS00159; KDPG and KHG aldolases active site  (PATTERN)

Consensus pattern: G-[LIVM]-x(3)-E-[LIV]-T-[LF]-R R is the active site residue Sequences known to belong to this class detected by the pattern: ALL, except for Bacillus subtilis KDPG-aldolase which has Thr instead of Arg in the active site Other sequence(s) detected in Swiss-Prot: NONE.

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00159 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00159 • Scan Swiss-Prot/TrEMBL entries against PS00159 • view ligand binding statistics

Matching PDB structures: 1EUA 1EUN 1FQ0 1FWR ... [ALL]

ALDOLASE_KDPG_KHG_2, PS00160; KDPG and KHG aldolases Schiff-base forming residue  (PATTERN)

Consensus pattern: G-x(3)-[LIVMF]-K-[LF]-F-P-[SA]-x(3)-G K is involved in Schiff-base formation Sequences known to belong to this class detected by the pattern: ALL Other sequence(s) detected in Swiss-Prot: NONE.

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00160 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00160 • Scan Swiss-Prot/TrEMBL entries against PS00160 • view ligand binding statistics

Matching PDB structures: 1EUA 1EUN 1FQ0 1MXS ... [ALL]

1	Authors	Vlahos C.J., Dekker E.E.
	Title	The complete amino acid sequence and identification of the active-site arginine peptide of Escherichia coli 2-keto-4-hydroxyglutarate aldolase.
	Source	J. Biol. Chem. 263:11683-11691(1988).
	PubMed ID	3136164

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