{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P0A955","secondaryAccessions":["P10177"],"uniProtkbId":"ALKH_ECOLI","entryAudit":{"firstPublicDate":"2005-07-19","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2005-07-19","entryVersion":147,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Escherichia coli (strain K12)","taxonId":83333,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"KHG/KDPG aldolase"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"(4S)-4-hydroxy-2-oxoglutarate aldolase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1098660"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"4560498"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"1339418"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"7016177"}],"value":"4.1.3.42"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"2-dehydro-3-deoxy-phosphogluconate aldolase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11342129"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17962400"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17981470"}],"value":"4.1.2.14"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"1624451"}],"value":"2-keto-3-deoxy-6-phosphogluconate aldolase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"1624451"}],"value":"KDPG aldolase"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"1098660"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"4560498"}],"value":"2-keto-4-hydroxyglutarate aldolase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"4560498"}],"value":"KHG aldolase"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"1098660"}],"value":"Ketohydroxyglutarate aldolase"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Entner-Douderoff aldolase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Oxaloacetate decarboxylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1339418"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"4560498"}],"value":"4.1.1.112"}]},{"fullName":{"value":"Phospho-2-dehydro-3-deoxygluconate aldolase"}},{"fullName":{"value":"Phospho-2-keto-3-deoxygluconate aldolase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"1624451"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8344525"}],"value":"eda"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"1339418"}],"value":"hga"},{"value":"kdgA"}],"orderedLocusNames":[{"value":"b1850"},{"value":"JW1839"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1098660"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11342129"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1339418"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15659677"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1624451"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17962400"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17981470"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"4560498"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7016177"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"15659677"}],"value":"Involved in the degradation of glucose via the Entner-Doudoroff pathway (PubMed:15659677, PubMed:1624451). Catalyzes the reversible, stereospecific retro-aldol cleavage of 2-keto-3-deoxy-6-phosphogluconate (KDPG) to pyruvate and D-glyceraldehyde-3-phosphate (PubMed:11342129, PubMed:17962400, PubMed:17981470). In vitro, can also catalyze the cleavage of 2-keto-4-hydroxy-4-(2'-pyridyl)butyrate (KHPB), 2-keto-3-deoxy-6-phosphogalactonate (KDPGal), and of the substrate analogs 2-keto-3-deoxy-gluconate (KDG) and 2-keto-4-hydroxyoctonate (KHO) (PubMed:17962400). Can accept some nucleophiles other than pyruvate, including 2-oxobutanoate, phenylpyruvate and fluorobutanoate (PubMed:17981470). In addition to its KDPG aldolase activity, catalyzes the reversible cleavage of 2-keto-4-hydroxyglutarate (KHG) to glyoxylate and pyruvate (PubMed:1098660, PubMed:1339418, PubMed:4560498, PubMed:7016177). The enzyme is stereoselective for the S-enantiomer of KHG (PubMed:1098660, PubMed:4560498). Cleavage of KHG could serve in tricarboxylic acid (TCA) cycle regulation or, when operating in the reverse direction, in the detoxification of glyoxylate (Probable). Finally, also shows a high level of oxaloacetate beta-decarboxylase activity (PubMed:1339418, PubMed:4560498). The enzyme could have several physiological roles and function as a stress response protein in addition to its role in the catabolism of sugar acids (PubMed:15659677)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-dehydro-3-deoxy-6-phospho-D-gluconate = D-glyceraldehyde 3-phosphate + pyruvate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17089"},{"database":"ChEBI","id":"CHEBI:15361"},{"database":"ChEBI","id":"CHEBI:57569"},{"database":"ChEBI","id":"CHEBI:59776"}],"ecNumber":"4.1.2.14","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11342129"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17962400"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17981470"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(4S)-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:35639"},{"database":"ChEBI","id":"CHEBI:15361"},{"database":"ChEBI","id":"CHEBI:36655"},{"database":"ChEBI","id":"CHEBI:71685"}],"ecNumber":"4.1.3.42","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1098660"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"4560498"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"1339418"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"7016177"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"oxaloacetate + H(+) = pyruvate + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15641"},{"database":"ChEBI","id":"CHEBI:15361"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16452"},{"database":"ChEBI","id":"CHEBI:16526"}],"ecNumber":"4.1.1.112","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1339418"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"4560498"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1978721"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"4560498"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7016177"}],"value":"The formation of KHG is inhibited by halides and substrate analogs such as hydroxypyruvate, tartrate, oxalate or acetaldehyde (PubMed:7016177). KHG aldolase activity is also inhibited by bromopyruvate, which specifically esterifies Glu-45 (PubMed:1978721). Activity is partially inhibited by p-mercuriphenylsulfonate, iodoacetate and N-ethylmaleimide (PubMed:4560498)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"maximumVelocities":[{"velocity":7.9,"unit":"umol/min/mg","enzyme":"enzyme for KHG aldolase activity","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"4560498"}]},{"velocity":3.4,"unit":"umol/min/mg","enzyme":"enzyme for KHG aldolase activity","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1339418"}]},{"velocity":2.1,"unit":"umol/min/mg","enzyme":"enzyme for oxaloacetate decarboxylase activity","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1339418"}]}],"michaelisConstants":[{"constant":0.1,"unit":"mM","substrate":"KDPG","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17962400"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17981470"}]},{"constant":32.0,"unit":"mM","substrate":"KHPB","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17962400"}]},{"constant":0.1,"unit":"mM","substrate":"KDPGal","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17962400"}]},{"constant":0.6,"unit":"mM","substrate":"KDPGal","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17981470"}]},{"constant":1.9,"unit":"mM","substrate":"KDG","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17962400"}]},{"constant":150.0,"unit":"mM","substrate":"KHO","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17962400"}]},{"constant":2.3,"unit":"mM","substrate":"(4S)-4-hydroxy-2-oxoglutarate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"4560498"}]},{"constant":2.4,"unit":"mM","substrate":"4-hydroxy-2-oxoglutarate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1339418"}]},{"constant":0.8,"unit":"mM","substrate":"oxaloacetate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1339418"}]},{"constant":9.0,"unit":"mM","substrate":"2-oxobutyrate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11342129"}]},{"constant":10.0,"unit":"mM","substrate":"pyruvate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11342129"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11342129"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17962400"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17981470"}],"value":"kcat is 83 sec(-1) with KDPG as substrate (PubMed:17962400). kcat is 80 sec(-1) with KDPG as substrate (PubMed:17981470). kcat is 11 sec(-1) with KHPB as substrate (PubMed:17962400). kcat is 0.0063 sec(-1) with KDPGal as substrate (PubMed:17962400). kcat is 0.01 sec(-1) with KDPGal as substrate (PubMed:17981470). kcat is 0.019 sec(-1) with KDG as substrate (PubMed:17962400). kcat is 2 sec(-1) with KHO as substrate (PubMed:17962400). kcat is 0.0121 sec(-1) with pyruvate as substrate (PubMed:11342129). kcat is 0.0004 sec(-1) with 2-oxobutyrate as substrate (PubMed:11342129)."}]}},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1339418"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"4560498"}],"value":"Optimum pH is 8.6 for KHG aldolase activity (PubMed:4560498). Optimum pH is 8.4 for KHG aldolase activity (PubMed:1339418)."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"15659677"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"1624451"}],"value":"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"}],"commentType":"PATHWAY"},{"texts":[{"value":"Carbohydrate metabolism; glyoxylate and dicarboxylate metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11274385"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11342129"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1339418"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16403639"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3136164"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"4560498"}],"value":"Homotrimer"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P0A955","intActId":"EBI-558114"},"interactantTwo":{"uniProtKBAccession":"P0A955","geneName":"eda","intActId":"EBI-558114"},"numberOfExperiments":3,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15659677"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1624451"}],"value":"Part of the edd-eda operon, whose expression is controlled by three functional promoters (P1, P2 and P4), each of which is responsible for induction under different growth conditions (PubMed:15659677, PubMed:1624451). Both P2 and P4 are responsible for the high basal level of expression (PubMed:15659677, PubMed:1624451). P1 controls induction on gluconate and is regulated by GntR (PubMed:15659677). P2 is induced by growth on glucuronate, galacturonate and methyl-beta-D-glucuronide, and is mediated directly by KdgR (PubMed:15659677). P4 is active under conditions of phosphate starvation and is directly controlled by PhoB (PubMed:15659677). In addition, starvation for carbon, but not the transition to stationary phase, slightly increases Eda synthesis (PubMed:15659677). CsrA exerts indirect negative control of Eda levels (PubMed:15659677)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1339418"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31390539"}],"value":"Cells lacking this gene show no detectable KHG aldolase activity (PubMed:1339418). Does not affect growth on glucose and native reaction flux (PubMed:31390539)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11342129"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17962400"}],"value":"Is an attractive enzyme for development as a biocatalyst, however, as with most enzymatic catalysts, substrate selectivity ultimately limits the broad use of KDPG aldolase as a synthetic reagent (PubMed:17962400). The enzyme has been the subject of directed evolution studies and structure-based approach to identify mutants with enhanced substrate specificity (PubMed:11342129, PubMed:17962400). Site-directed mutagenesis of the active site or the phosphate-binding pocket can expand substrate selectivity for unnatural substrates for use in biocatalysis applications (PubMed:11342129, PubMed:17962400)"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the KHG/KDPG aldolase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":213,"modifier":"EXACT"}},"description":"KHG/KDPG aldolase","featureId":"PRO_0000201037"},{"type":"Active site","location":{"start":{"value":45,"modifier":"EXACT"},"end":{"value":45,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"11274385"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"11342129"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"16403639"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"1978721"}]},{"type":"Active site","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"Schiff-base intermediate with substrate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11274385"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"11342129"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"16403639"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"3136164"}]},{"type":"Binding site","location":{"start":{"value":49,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:15361"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11274385"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1EUA"}],"ligand":{"name":"pyruvate","id":"ChEBI:CHEBI:15361"}},{"type":"Binding site","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:15361"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11274385"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1EUA"}],"ligand":{"name":"pyruvate","id":"ChEBI:CHEBI:15361"}},{"type":"Binding site","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"covalent","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:15361"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11274385"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1EUA"}],"ligand":{"name":"pyruvate","id":"ChEBI:CHEBI:15361"}},{"type":"Site","location":{"start":{"value":161,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"Plays a major role in determining the stereoselectivity","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"17981470"}]},{"type":"Mutagenesis","location":{"start":{"value":45,"modifier":"EXACT"},"end":{"value":45,"modifier":"EXACT"}},"description":"Aldolase activity is significantly impaired.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16403639"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["N"]}},{"type":"Mutagenesis","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"Absence of aldolase activity. Has reduced catalytic efficiency relative to wild-type protein but demonstrates a considerably altered substrate profile with an enhanced activity against pyridine carboxaldehyde, benzaldehyde and alpha-ketobutyrate; when associated with K-161.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11342129"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["Q"]}},{"type":"Mutagenesis","location":{"start":{"value":161,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"13-fold decrease in catalytic efficiency with KDPG as substrate and 250-fold increase in catalytic efficiency with KDPGal as substrate.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17981470"}],"alternativeSequence":{"originalSequence":"T","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":161,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"Has reduced catalytic efficiency relative to wild-type protein but demonstrates a considerably altered substrate profile with an enhanced activity against pyridine carboxaldehyde, benzaldehyde and alpha-ketobutyrate; when associated with Q-133.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11342129"}],"alternativeSequence":{"originalSequence":"T","alternativeSequences":["K"]}},{"type":"Mutagenesis","location":{"start":{"value":161,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"Shows little stereoselectivity, accepting KDPG and KDPGal as substrate with roughly equal efficacy. The change in specificity is accompanied by a very significant loss of activity against KDPG and a 5-fold increase in catalytic efficiency with KDPGal as substrate.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17981470"}],"alternativeSequence":{"originalSequence":"T","alternativeSequences":["V"]}},{"type":"Mutagenesis","location":{"start":{"value":168,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"Shows activity significantly greater than wild-type.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11342129"}],"alternativeSequence":{"originalSequence":"N","alternativeSequences":["S"]}},{"type":"Mutagenesis","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"1.35-fold decrease in catalytic efficiency with KDPG as substrate. Has only a modest effect on the catalytic efficiency with KDG or KHO as substrate.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17962400"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"300-fold decrease in catalytic efficiency with KDPG as substrate. Increases the efficiency for retro-aldol cleavage of both KDG and KHO. Enhances the selectivity for reaction with KHO compared to KDPG by 780-fold.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17962400"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["D"]}},{"type":"Mutagenesis","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"4-fold decrease in catalytic efficiency with KDPG as substrate. Increases the efficiency for retro-aldol cleavage of both KDG and KHO. 40-fold increase in catalytic efficiency for the synthesis of KHPB, a precursor of nikkomycin, making this mutant a useful biocatalyst for the preparation of fine chemicals.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17962400"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["L"]}},{"type":"Helix","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1WBH"}]},{"type":"Beta strand","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1WBH"}]},{"type":"Helix","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1WBH"}]},{"type":"Helix","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":38,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1WBH"}]},{"type":"Beta strand","location":{"start":{"value":43,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1WBH"}]},{"type":"Helix","location":{"start":{"value":53,"modifier":"EXACT"},"end":{"value":63,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1WBH"}]},{"type":"Beta strand","location":{"start":{"value":67,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1WBH"}]},{"type":"Helix","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1WBH"}]},{"type":"Beta strand","location":{"start":{"value":91,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1WBH"}]},{"type":"Helix","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1WBH"}]},{"type":"Beta strand","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":109,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1WBH"}]},{"type":"Beta strand","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1WBH"}]},{"type":"Helix","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1WBH"}]},{"type":"Beta strand","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":134,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1WBH"}]},{"type":"Turn","location":{"start":{"value":135,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1WBH"}]},{"type":"Helix","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1WBH"}]},{"type":"Beta strand","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":163,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1WBH"}]},{"type":"Turn","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1WBH"}]},{"type":"Helix","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1WBH"}]},{"type":"Beta strand","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1WBH"}]},{"type":"Helix","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1WBH"}]},{"type":"Helix","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1WBH"}]},{"type":"Helix","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1WBH"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0704","category":"Ligand","name":"Schiff base"}],"references":[{"referenceNumber":1,"citation":{"id":"3136164","citationType":"journal article","authors":["Vlahos C.J.","Dekker E.E."],"citationCrossReferences":[{"database":"PubMed","id":"3136164"},{"database":"DOI","id":"10.1016/s0021-9258(18)37838-4"}],"title":"The complete amino acid sequence and identification of the active-site arginine peptide of Escherichia coli 2-keto-4-hydroxyglutarate aldolase.","publicationDate":"1988","journal":"J. Biol. Chem.","firstPage":"11683","lastPage":"11691","volume":"263"},"referencePositions":["PROTEIN SEQUENCE","SUBUNIT","ACTIVE SITE"],"referenceComments":[{"value":"K12","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"1339418","citationType":"journal article","authors":["Patil R.V.","Dekker E.E."],"citationCrossReferences":[{"database":"PubMed","id":"1339418"},{"database":"DOI","id":"10.1128/jb.174.1.102-107.1992"}],"title":"Cloning, nucleotide sequence, overexpression, and inactivation of the Escherichia coli 2-keto-4-hydroxyglutarate aldolase gene.","publicationDate":"1992","journal":"J. Bacteriol.","firstPage":"102","lastPage":"107","volume":"174"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION AS A KHG ALDOLASE AND A DECARBOXYLASE","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES","SUBUNIT","DISRUPTION PHENOTYPE"]},{"referenceNumber":3,"citation":{"id":"1624451","citationType":"journal article","authors":["Egan S.E.","Fliege R.","Tong S.","Shibata A.","Wolf R.E. Jr.","Conway T."],"citationCrossReferences":[{"database":"PubMed","id":"1624451"},{"database":"DOI","id":"10.1128/jb.174.14.4638-4646.1992"}],"title":"Molecular characterization of the Entner-Doudoroff pathway in Escherichia coli: sequence analysis and localization of promoters for the edd-eda operon.","publicationDate":"1992","journal":"J. Bacteriol.","firstPage":"4638","lastPage":"4646","volume":"174"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION","INDUCTION"]},{"referenceNumber":4,"citation":{"id":"CI-24EN28AG5UE8H","citationType":"submission","authors":["Smith J.M.","Nygaard P."],"title":"Purine and one-carbon metabolism in Escherichia coli K12: DNA sequence of a second GAR transformylase.","publicationDate":"JUL-1993","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"K12","type":"STRAIN"}]},{"referenceNumber":5,"citation":{"id":"8344525","citationType":"journal article","authors":["Carter A.T.","Pearson B.M.","Dickinson J.R.","Lancashire W.E."],"citationCrossReferences":[{"database":"PubMed","id":"8344525"},{"database":"DOI","id":"10.1016/0378-1119(93)90362-7"}],"title":"Sequence of the Escherichia coli K-12 edd and eda genes of the Entner-Doudoroff pathway.","publicationDate":"1993","journal":"Gene","firstPage":"155","lastPage":"156","volume":"130"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"K12","type":"STRAIN"}]},{"referenceNumber":6,"citation":{"id":"9097040","citationType":"journal article","authors":["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."],"citationCrossReferences":[{"database":"PubMed","id":"9097040"},{"database":"DOI","id":"10.1093/dnares/3.6.379"}],"title":"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.","publicationDate":"1996","journal":"DNA Res.","firstPage":"379","lastPage":"392","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"K12 / W3110 / ATCC 27325 / DSM 5911","type":"STRAIN"}]},{"referenceNumber":7,"citation":{"id":"9278503","citationType":"journal article","authors":["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."],"citationCrossReferences":[{"database":"PubMed","id":"9278503"},{"database":"DOI","id":"10.1126/science.277.5331.1453"}],"title":"The complete genome sequence of Escherichia coli K-12.","publicationDate":"1997","journal":"Science","firstPage":"1453","lastPage":"1462","volume":"277"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"K12 / MG1655 / ATCC 47076","type":"STRAIN"}]},{"referenceNumber":8,"citation":{"id":"16738553","citationType":"journal article","authors":["Hayashi K.","Morooka N.","Yamamoto Y.","Fujita K.","Isono K.","Choi S.","Ohtsubo E.","Baba T.","Wanner B.L.","Mori H.","Horiuchi T."],"citationCrossReferences":[{"database":"PubMed","id":"16738553"},{"database":"DOI","id":"10.1038/msb4100049"}],"title":"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.","publicationDate":"2006","journal":"Mol. Syst. Biol.","firstPage":"E1","lastPage":"E5","volume":"2"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"K12 / W3110 / ATCC 27325 / DSM 5911","type":"STRAIN"}]},{"referenceNumber":9,"citation":{"id":"4560498","citationType":"journal article","authors":["Nishihara H.","Dekker E.E."],"citationCrossReferences":[{"database":"PubMed","id":"4560498"},{"database":"DOI","id":"10.1016/s0021-9258(19)44941-7"}],"title":"Purification, substrate specificity and binding, beta-decarboxylase activity, and other properties of Escherichia coli 2-keto-4-hydroxyglutarate aldolase.","publicationDate":"1972","journal":"J. Biol. Chem.","firstPage":"5079","lastPage":"5087","volume":"247"},"referencePositions":["FUNCTION AS A KHG ALDOLASE AND A DECARBOXYLASE","CATALYTIC ACTIVITY","ACTIVITY REGULATION","BIOPHYSICOCHEMICAL PROPERTIES","SUBUNIT"],"referenceComments":[{"value":"K12","type":"STRAIN"}]},{"referenceNumber":10,"citation":{"id":"1098660","citationType":"journal article","authors":["Meloche H.P.","Monti C.T.","Dekker E.E."],"citationCrossReferences":[{"database":"PubMed","id":"1098660"},{"database":"DOI","id":"10.1016/s0006-291x(75)80489-x"}],"title":"Enzyme stereoselectivity: the reversible reaction catalyzed by 2-keto-4-hydroxyglutarate aldolase of Escherichia coli.","publicationDate":"1975","journal":"Biochem. Biophys. Res. Commun.","firstPage":"1033","lastPage":"1039","volume":"65"},"referencePositions":["FUNCTION AS A KHG ALDOLASE","CATALYTIC ACTIVITY"]},{"referenceNumber":11,"citation":{"id":"7016177","citationType":"journal article","authors":["Grady S.R.","Wang J.K.","Dekker E.E."],"citationCrossReferences":[{"database":"PubMed","id":"7016177"},{"database":"DOI","id":"10.1021/bi00512a021"}],"title":"Steady-state kinetics and inhibition studies of the aldol condensation reaction catalyzed by bovine liver and Escherichia coli 2-keto-4-hydroxyglutarate aldolase.","publicationDate":"1981","journal":"Biochemistry","firstPage":"2497","lastPage":"2502","volume":"20"},"referencePositions":["FUNCTION AS A KHG ALDOLASE","CATALYTIC ACTIVITY","ACTIVITY REGULATION"]},{"referenceNumber":12,"citation":{"id":"1978721","citationType":"journal article","authors":["Vlahos C.J.","Dekker E.E."],"citationCrossReferences":[{"database":"PubMed","id":"1978721"},{"database":"DOI","id":"10.1016/s0021-9258(17)30515-x"}],"title":"Active-site residues of 2-keto-4-hydroxyglutarate aldolase from Escherichia coli. Bromopyruvate inactivation and labeling of glutamate 45.","publicationDate":"1990","journal":"J. Biol. Chem.","firstPage":"20384","lastPage":"20389","volume":"265"},"referencePositions":["ACTIVITY REGULATION","ACTIVE SITE"]},{"referenceNumber":13,"citation":{"id":"9298644","citationType":"journal article","authors":["VanBogelen R.A.","Abshire K.Z.","Moldover B.","Olson E.R.","Neidhardt F.C."],"citationCrossReferences":[{"database":"PubMed","id":"9298644"},{"database":"DOI","id":"10.1002/elps.1150180805"}],"title":"Escherichia coli proteome analysis using the gene-protein database.","publicationDate":"1997","journal":"Electrophoresis","firstPage":"1243","lastPage":"1251","volume":"18"},"referencePositions":["IDENTIFICATION BY 2D-GEL"]},{"referenceNumber":14,"citation":{"id":"15659677","citationType":"journal article","authors":["Murray E.L.","Conway T."],"citationCrossReferences":[{"database":"PubMed","id":"15659677"},{"database":"DOI","id":"10.1128/jb.187.3.991-1000.2005"}],"title":"Multiple regulators control expression of the Entner-Doudoroff aldolase (Eda) of Escherichia coli.","publicationDate":"2005","journal":"J. Bacteriol.","firstPage":"991","lastPage":"1000","volume":"187"},"referencePositions":["FUNCTION","TRANSCRIPTIONAL REGULATION"]},{"referenceNumber":15,"citation":{"id":"17962400","citationType":"journal article","authors":["Cheriyan M.","Toone E.J.","Fierke C.A."],"citationCrossReferences":[{"database":"PubMed","id":"17962400"},{"database":"DOI","id":"10.1110/ps.073042907"}],"title":"Mutagenesis of the phosphate-binding pocket of KDPG aldolase enhances selectivity for hydrophobic substrates.","publicationDate":"2007","journal":"Protein Sci.","firstPage":"2368","lastPage":"2377","volume":"16"},"referencePositions":["FUNCTION AS A KDPG ALDOLASE","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES","BIOTECHNOLOGY","MUTAGENESIS OF SER-184"]},{"referenceNumber":16,"citation":{"id":"17981470","citationType":"journal article","authors":["Walters M.J.","Srikannathasan V.","McEwan A.R.","Naismith J.H.","Fierke C.A.","Toone E.J."],"citationCrossReferences":[{"database":"PubMed","id":"17981470"},{"database":"DOI","id":"10.1016/j.bmc.2007.10.043"}],"title":"Characterization and crystal structure of Escherichia coli KDPGal aldolase.","publicationDate":"2008","journal":"Bioorg. Med. Chem.","firstPage":"710","lastPage":"720","volume":"16"},"referencePositions":["FUNCTION AS A KDPG ALDOLASE","CATALYTIC ACTIVITY","SUBSTRATE SPECIFICITY","BIOPHYSICOCHEMICAL PROPERTIES","MUTAGENESIS OF THR-161"]},{"referenceNumber":17,"citation":{"id":"31390539","citationType":"journal article","authors":["Long C.P.","Antoniewicz M.R."],"citationCrossReferences":[{"database":"PubMed","id":"31390539"},{"database":"DOI","id":"10.1016/j.ymben.2019.08.003"}],"title":"Metabolic flux responses to deletion of 20 core enzymes reveal flexibility and limits of E. coli metabolism.","publicationDate":"2019","journal":"Metab. Eng.","firstPage":"249","lastPage":"257","volume":"55"},"referencePositions":["DISRUPTION PHENOTYPE"]},{"referenceNumber":18,"citation":{"id":"11274385","citationType":"journal article","authors":["Allard J.","Grochulski P.","Sygusch J."],"citationCrossReferences":[{"database":"PubMed","id":"11274385"},{"database":"DOI","id":"10.1073/pnas.071380898"}],"title":"Covalent intermediate trapped in 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase structure at 1.95-A resolution.","publicationDate":"2001","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"3679","lastPage":"3684","volume":"98"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH PYRUVATE","REACTION MECHANISM","SUBUNIT","ACTIVE SITE"],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"1EUA"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1EUN"}]},{"referenceNumber":19,"citation":{"id":"11342129","citationType":"journal article","authors":["Wymer N.","Buchanan L.V.","Henderson D.","Mehta N.","Botting C.H.","Pocivavsek L.","Fierke C.A.","Toone E.J.","Naismith J.H."],"citationCrossReferences":[{"database":"PubMed","id":"11342129"},{"database":"DOI","id":"10.1016/s0969-2126(00)00555-4"}],"title":"Directed evolution of a new catalytic site in 2-keto-3-deoxy-6-phosphogluconate aldolase from Escherichia coli.","publicationDate":"2001","journal":"Structure","firstPage":"1","lastPage":"9","volume":"9"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF WILD-TYPE AND DOUBLE MUTANT GLN-133/LYS-161 IN COMPLEXES WITH CITRATE","FUNCTION AS A KDPG ALDOLASE","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES","SUBUNIT","ACTIVE SITE","BIOTECHNOLOGY","MUTAGENESIS OF LYS-133; THR-161 AND ASN-168"],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"1FQ0"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1FWR"}]},{"referenceNumber":20,"citation":{"id":"16403639","citationType":"journal article","authors":["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."],"citationCrossReferences":[{"database":"PubMed","id":"16403639"},{"database":"DOI","id":"10.1016/j.bmc.2005.12.022"}],"title":"Mechanism of the Class I KDPG aldolase.","publicationDate":"2006","journal":"Bioorg. Med. Chem.","firstPage":"3002","lastPage":"3010","volume":"14"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF WILD-TYPE AND MUTANT ASN-45 IN COMPLEX WITH PHOSPHATE","REACTION MECHANISM","SUBUNIT","ACTIVE SITE","MUTAGENESIS OF GLU-45"],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"1WAU"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1WBH"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2C0A"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X68871","properties":[{"key":"ProteinId","value":"CAA48732.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"M87458","properties":[{"key":"ProteinId","value":"AAA23723.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"L20897","properties":[{"key":"ProteinId","value":"AAA23862.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"X63694","properties":[{"key":"ProteinId","value":"CAA45222.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"U00096","properties":[{"key":"ProteinId","value":"AAC74920.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AP009048","properties":[{"key":"ProteinId","value":"BAA15658.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"B42986","properties":[{"key":"EntryName","value":"ADECOG"}]},{"database":"RefSeq","id":"NP_416364.1","properties":[{"key":"NucleotideSequenceId","value":"NC_000913.3"}]},{"database":"RefSeq","id":"WP_000800512.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP009789.1"}]},{"database":"PDB","id":"1EUA","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.95 A"},{"key":"Chains","value":"A/B/C=1-213"}]},{"database":"PDB","id":"1EUN","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.00 A"},{"key":"Chains","value":"A/B/C=1-213"}]},{"database":"PDB","id":"1FQ0","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.10 A"},{"key":"Chains","value":"A/B/C=1-213"}]},{"database":"PDB","id":"1FWR","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.70 A"},{"key":"Chains","value":"A/B/C=1-213"}]},{"database":"PDB","id":"1WAU","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.80 A"},{"key":"Chains","value":"A=1-213"}]},{"database":"PDB","id":"1WBH","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.55 A"},{"key":"Chains","value":"A/B/C=1-213"}]},{"database":"PDB","id":"2C0A","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.55 A"},{"key":"Chains","value":"A/B/C=1-213"}]},{"database":"PDBsum","id":"1EUA","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"1EUN","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"1FQ0","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"1FWR","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"1WAU","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"1WBH","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"2C0A","properties":[{"key":"Description","value":"-"}]},{"database":"AlphaFoldDB","id":"P0A955","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P0A955","properties":[{"key":"Description","value":"-"}]},{"database":"BioGRID","id":"4259153","properties":[{"key":"Interactions","value":"37"}]},{"database":"BioGRID","id":"850724","properties":[{"key":"Interactions","value":"2"}]},{"database":"DIP","id":"DIP-36196N","properties":[{"key":"Description","value":"-"}]},{"database":"FunCoup","id":"P0A955","properties":[{"key":"Number of interactors","value":"397"}]},{"database":"IntAct","id":"P0A955","properties":[{"key":"Interactions","value":"10"}]},{"database":"STRING","id":"511145.b1850","properties":[{"key":"Description","value":"-"}]},{"database":"ChEMBL","id":"CHEMBL4296292","properties":[{"key":"Description","value":"-"}]},{"database":"jPOST","id":"P0A955","properties":[{"key":"Description","value":"-"}]},{"database":"PaxDb","id":"511145-b1850","properties":[{"key":"Description","value":"-"}]},{"database":"EnsemblBacteria","id":"AAC74920","properties":[{"key":"ProteinId","value":"AAC74920"},{"key":"GeneId","value":"b1850"}]},{"database":"GeneID","id":"67172877","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"93776117","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"946367","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ecj:JW1839","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"eco:b1850","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ecoc:C3026_10540","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1411691.4.peg.399","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"EchoBASE","id":"EB0252","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG0800","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"HOGENOM","id":"CLU_077795_1_1_6","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"P0A955","properties":[{"key":"Description","value":"-"}]},{"database":"OMA","id":"FFPAEYC","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"OrthoDB","id":"9805177at2","properties":[{"key":"Description","value":"-"}]},{"database":"PhylomeDB","id":"P0A955","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"EcoCyc:KDPGALDOL-4OH2OXOGLUTARALDOL-MONOMER","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"MetaCyc:KDPGALDOL-4OH2OXOGLUTARALDOL-MONOMER","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"4.1.2.14","properties":[{"key":"OrganismId","value":"2026"}]},{"database":"BRENDA","id":"4.1.3.16","properties":[{"key":"OrganismId","value":"2026"}]},{"database":"BRENDA","id":"4.1.3.42","properties":[{"key":"OrganismId","value":"2026"}]},{"database":"UniPathway","id":"UPA00227","properties":[{"key":"RectionId","value":"-"}]},{"database":"UniPathway","id":"UPA00856","properties":[{"key":"RectionId","value":"UER00829"}]},{"database":"EvolutionaryTrace","id":"P0A955","properties":[{"key":"Description","value":"-"}]},{"database":"PRO","id":"PR:P0A955","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000000625","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"AbasyAtlas","id":"P0A955","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"15911532"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"18304323"}]},{"database":"GO","id":"GO:0016020","properties":[{"key":"GoTerm","value":"C:membrane"},{"key":"GoEvidenceType","value":"HDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0007005","source":"PubMed","id":"16858726"}]},{"database":"GO","id":"GO:0106009","properties":[{"key":"GoTerm","value":"F:(4S)-4-hydroxy-2-oxoglutarate aldolase activity"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"4560498"}]},{"database":"GO","id":"GO:0008700","properties":[{"key":"GoTerm","value":"F:(R,S)-4-hydroxy-2-oxoglutarate aldolase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"17981470"}]},{"database":"GO","id":"GO:0008675","properties":[{"key":"GoTerm","value":"F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"11094340"}]},{"database":"GO","id":"GO:0016832","properties":[{"key":"GoTerm","value":"F:aldehyde-lyase activity"},{"key":"GoEvidenceType","value":"IBA:GO_Central"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IPI:IntAct"}],"evidences":[{"evidenceCode":"ECO:0000353","source":"PubMed","id":"16858726"},{"evidenceCode":"ECO:0000353","source":"PubMed","id":"24561554"}]},{"database":"GO","id":"GO:0008948","properties":[{"key":"GoTerm","value":"F:oxaloacetate decarboxylase activity"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"4560498"}]},{"database":"GO","id":"GO:0016833","properties":[{"key":"GoTerm","value":"F:oxo-acid-lyase activity"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"1339418"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"4560498"}]},{"database":"GO","id":"GO:0009255","properties":[{"key":"GoTerm","value":"P:Entner-Doudoroff pathway through 6-phosphogluconate"},{"key":"GoEvidenceType","value":"EXP:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9503620"}]},{"database":"CDD","id":"cd00452","properties":[{"key":"EntryName","value":"KDPG_aldolase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000054","properties":[{"key":"EntryName","value":"KHG/KDPG aldolase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000887","properties":[{"key":"EntryName","value":"Aldlse_KDPG_KHG"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR031337","properties":[{"key":"EntryName","value":"KDPG/KHG_AS_1"}]},{"database":"InterPro","id":"IPR031338","properties":[{"key":"EntryName","value":"KDPG/KHG_AS_2"}]},{"database":"NCBIfam","id":"TIGR01182","properties":[{"key":"EntryName","value":"eda"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004325","properties":[{"key":"EntryName","value":"PRK05718.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30246:SF1","properties":[{"key":"EntryName","value":"2-DEHYDRO-3-DEOXY-6-PHOSPHOGALACTONATE ALDOLASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30246","properties":[{"key":"EntryName","value":"2-KETO-3-DEOXY-6-PHOSPHOGLUCONATE ALDOLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01081","properties":[{"key":"EntryName","value":"Aldolase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51569","properties":[{"key":"EntryName","value":"Aldolase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00159","properties":[{"key":"EntryName","value":"ALDOLASE_KDPG_KHG_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00160","properties":[{"key":"EntryName","value":"ALDOLASE_KDPG_KHG_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKNWKTSAESILTTGPVVPVIVVKKLEHAVPMAKALVAGGVRVLEVTLRTECAVDAIRAIAKEVPEAIVGAGTVLNPQQLAEVTEAGAQFAISPGLTEPLLKAATEGTIPLIPGISTVSELMLGMDYGLKEFKFFPAEANGGVKALQAIAGPFSQVRFCPTGGISPANYRDYLALKSVLCIGGSWLVPADALEAGDYDRITKLAREAVEGAKL","length":213,"molWeight":22284,"crc64":"CC8D51B50480D0B7","md5":"B314DA7703A0F4533ABC0E706147208F"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"ACTIVITY REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":2,"SUBUNIT":1,"INTERACTION":1,"SUBCELLULAR LOCATION":1,"INDUCTION":1,"DISRUPTION PHENOTYPE":1,"BIOTECHNOLOGY":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":2,"Binding site":3,"Site":1,"Mutagenesis":9,"Helix":12,"Beta strand":9,"Turn":2},"uniParcId":"UPI0000111422"}}