{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P0AB71","secondaryAccessions":["P11604","Q2M9R7"],"uniProtkbId":"ALF_ECOLI","entryAudit":{"firstPublicDate":"2005-11-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2007-01-23","entryVersion":153,"sequenceVersion":2},"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":{"value":"Fructose-bisphosphate aldolase class 2"},"shortNames":[{"value":"FBP aldolase"},{"value":"FBPA"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10712619"}],"value":"4.1.2.13"}]},"alternativeNames":[{"fullName":{"value":"Fructose-1,6-bisphosphate aldolase"}},{"fullName":{"value":"Fructose-bisphosphate aldolase class II"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Sedoheptulose bisphosphate aldolase"}}]},"genes":[{"geneName":{"value":"fbaA"},"synonyms":[{"value":"fba"},{"value":"fda"}],"orderedLocusNames":[{"value":"b2925"},{"value":"JW2892"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10712619"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19756045"}],"value":"Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis (PubMed:10712619). In addition, is involved in the utilization of D-sedoheptulose 7-phosphate, an intermediate of the pentose phosphate pathway, via the sedoheptulose bisphosphate bypass pathway (PubMed:19756045). Catalyzes the cleavage of D-sedoheptulose 1,7-bisphosphate to glyceraldehyde 3-phosphate and erythrose 4-phosphate (PubMed:19756045)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:14729"},{"database":"ChEBI","id":"CHEBI:32966"},{"database":"ChEBI","id":"CHEBI:57642"},{"database":"ChEBI","id":"CHEBI:59776"}],"ecNumber":"4.1.2.13","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10712619"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-erythrose 4-phosphate + dihydroxyacetone phosphate = D-sedoheptulose 1,7-bisphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30167"},{"database":"ChEBI","id":"CHEBI:16897"},{"database":"ChEBI","id":"CHEBI:57642"},{"database":"ChEBI","id":"CHEBI:58335"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19756045"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:30169"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19756045"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10080900"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8836102"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8939754"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10080900"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8836102"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8939754"}],"value":"Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution."}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":0.17,"unit":"mM","substrate":"fructose-1,6-bisphosphate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10712619"}]},{"constant":0.35,"unit":"mM","substrate":"tagatose-1,6-bisphosphate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10712619"}]}],"note":{"texts":[{"value":"The catalytic efficiency measured with fructose-1,6-bisphosphate as substrate is 1440-fold higher than that with tagatose-1,6-bisphosphate."}]}}},{"texts":[{"value":"Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10080900"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12595741"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8836102"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8939754"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P0AB71","intActId":"EBI-370916"},"interactantTwo":{"uniProtKBAccession":"P0A6Y8","geneName":"dnaK","intActId":"EBI-542092"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P0AB71","intActId":"EBI-370916"},"interactantTwo":{"uniProtKBAccession":"P0AB71","geneName":"fbaA","intActId":"EBI-370916"},"numberOfExperiments":4,"organismDiffer":false}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the class II fructose-bisphosphate aldolase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2649077"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9298646"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9600841"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":359,"modifier":"EXACT"}},"description":"Fructose-bisphosphate aldolase class 2","featureId":"PRO_0000178713"},{"type":"Active site","location":{"start":{"value":110,"modifier":"EXACT"},"end":{"value":110,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10080900"}]},{"type":"Binding site","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59776"}],"evidences":[{"evidenceCode":"ECO:0000305"}],"ligand":{"name":"D-glyceraldehyde 3-phosphate","id":"ChEBI:CHEBI:59776"}},{"type":"Binding site","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":111,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10080900"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8836102"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8939754"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":145,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10080900"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8836102"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8939754"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10080900"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8836102"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8939754"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":227,"modifier":"EXACT"},"end":{"value":227,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10080900"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8836102"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8939754"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":228,"modifier":"EXACT"},"end":{"value":228,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57642"}],"ligand":{"name":"dihydroxyacetone phosphate","id":"ChEBI:CHEBI:57642"}},{"type":"Binding site","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10080900"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8836102"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8939754"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":266,"modifier":"EXACT"},"end":{"value":268,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57642"}],"ligand":{"name":"dihydroxyacetone phosphate","id":"ChEBI:CHEBI:57642"}},{"type":"Binding site","location":{"start":{"value":287,"modifier":"EXACT"},"end":{"value":290,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57642"}],"ligand":{"name":"dihydroxyacetone phosphate","id":"ChEBI:CHEBI:57642"}},{"type":"Modified residue","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":9,"modifier":"EXACT"}},"description":"N6-acetyllysine; alternate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18723842"}]},{"type":"Modified residue","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":9,"modifier":"EXACT"}},"description":"N6-malonyllysine; alternate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21908771"}]},{"type":"Modified residue","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":9,"modifier":"EXACT"}},"description":"N6-succinyllysine; alternate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21151122"}]},{"type":"Modified residue","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":72,"modifier":"EXACT"}},"description":"N6-succinyllysine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21151122"}]},{"type":"Modified residue","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":115,"modifier":"EXACT"}},"description":"N6-succinyllysine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21151122"}]},{"type":"Modified residue","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":231,"modifier":"EXACT"}},"description":"N6-succinyllysine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21151122"}]},{"type":"Modified residue","location":{"start":{"value":251,"modifier":"EXACT"},"end":{"value":251,"modifier":"EXACT"}},"description":"N6-succinyllysine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21151122"}]},{"type":"Modified residue","location":{"start":{"value":319,"modifier":"EXACT"},"end":{"value":319,"modifier":"EXACT"}},"description":"N6-succinyllysine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21151122"}]},{"type":"Modified residue","location":{"start":{"value":326,"modifier":"EXACT"},"end":{"value":326,"modifier":"EXACT"}},"description":"N6-succinyllysine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21151122"}]},{"type":"Modified residue","location":{"start":{"value":348,"modifier":"EXACT"},"end":{"value":348,"modifier":"EXACT"}},"description":"N6-succinyllysine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21151122"}]},{"type":"Mutagenesis","location":{"start":{"value":36,"modifier":"EXACT"},"end":{"value":36,"modifier":"EXACT"}},"description":"1.5% of wild-type activity. 5-fold decrease in FBP affinity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10712619"}],"alternativeSequence":{"originalSequence":"N","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":60,"modifier":"EXACT"}},"description":"81% of wild-type activity. 1.3-fold decrease in FBP affinity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10712619"}],"alternativeSequence":{"originalSequence":"Q","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"8% of wild-type activity. 16-fold decrease in FBP affinity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10712619"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"60% of wild-type activity. 2.5-fold decrease in FBP affinity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10712619"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["T"]}},{"type":"Mutagenesis","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":108,"modifier":"EXACT"}},"description":"Loss of activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8436219"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":111,"modifier":"EXACT"}},"description":"Loss of activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8436219"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"Partial loss of activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8436219"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":326,"modifier":"EXACT"},"end":{"value":326,"modifier":"EXACT"}},"description":"6% of wild-type activity. 2.2-fold decrease in FBP affinity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10712619"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["A"]}},{"type":"Helix","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":7,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJE"}]},{"type":"Beta strand","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJE"}]},{"type":"Helix","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJE"}]},{"type":"Beta strand","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":36,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJE"}]},{"type":"Helix","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":53,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJE"}]},{"type":"Beta strand","location":{"start":{"value":57,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJE"}]},{"type":"Helix","location":{"start":{"value":63,"modifier":"EXACT"},"end":{"value":70,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJE"}]},{"type":"Helix","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJE"}]},{"type":"Beta strand","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":109,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJE"}]},{"type":"Helix","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":116,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJE"}]},{"type":"Helix","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":134,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJE"}]},{"type":"Beta strand","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":144,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJE"}]},{"type":"Helix","location":{"start":{"value":151,"modifier":"EXACT"},"end":{"value":166,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJE"}]},{"type":"Turn","location":{"start":{"value":167,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJE"}]},{"type":"Beta strand","location":{"start":{"value":171,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJE"}]},{"type":"Helix","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":211,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJE"}]},{"type":"Beta strand","location":{"start":{"value":217,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJE"}]},{"type":"Beta strand","location":{"start":{"value":226,"modifier":"EXACT"},"end":{"value":228,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJD"}]},{"type":"Helix","location":{"start":{"value":232,"modifier":"EXACT"},"end":{"value":234,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1ZEN"}]},{"type":"Helix","location":{"start":{"value":240,"modifier":"EXACT"},"end":{"value":253,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJE"}]},{"type":"Beta strand","location":{"start":{"value":262,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJE"}]},{"type":"Helix","location":{"start":{"value":272,"modifier":"EXACT"},"end":{"value":280,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJE"}]},{"type":"Beta strand","location":{"start":{"value":283,"modifier":"EXACT"},"end":{"value":288,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJE"}]},{"type":"Helix","location":{"start":{"value":290,"modifier":"EXACT"},"end":{"value":306,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJE"}]},{"type":"Helix","location":{"start":{"value":308,"modifier":"EXACT"},"end":{"value":310,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJE"}]},{"type":"Beta strand","location":{"start":{"value":311,"modifier":"EXACT"},"end":{"value":317,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJE"}]},{"type":"Beta strand","location":{"start":{"value":320,"modifier":"EXACT"},"end":{"value":324,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJE"}]},{"type":"Helix","location":{"start":{"value":326,"modifier":"EXACT"},"end":{"value":329,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJE"}]},{"type":"Helix","location":{"start":{"value":331,"modifier":"EXACT"},"end":{"value":352,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5VJE"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0007","category":"PTM","name":"Acetylation"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"2546007","citationType":"journal article","authors":["Alefounder P.R.","Perham R.N."],"citationCrossReferences":[{"database":"PubMed","id":"2546007"},{"database":"DOI","id":"10.1111/j.1365-2958.1989.tb00221.x"}],"title":"Identification, molecular cloning and sequence analysis of a gene cluster encoding the class II fructose 1,6-bisphosphate aldolase, 3-phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate dehydrogenase of Escherichia coli.","publicationDate":"1989","journal":"Mol. Microbiol.","firstPage":"723","lastPage":"732","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"K12 / CS520","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"2649077","citationType":"journal article","authors":["Alefounder P.R.","Baldwin S.A.","Perham R.N.","Short N.J."],"citationCrossReferences":[{"database":"PubMed","id":"2649077"},{"database":"DOI","id":"10.1042/bj2570529"}],"title":"Cloning, sequence analysis and over-expression of the gene for the class II fructose 1,6-bisphosphate aldolase of Escherichia coli.","publicationDate":"1989","journal":"Biochem. J.","firstPage":"529","lastPage":"534","volume":"257"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PROTEIN SEQUENCE OF 2-27"]},{"referenceNumber":3,"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":4,"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":5,"citation":{"id":"9298646","citationType":"journal article","authors":["Link A.J.","Robison K.","Church G.M."],"citationCrossReferences":[{"database":"PubMed","id":"9298646"},{"database":"DOI","id":"10.1002/elps.1150180807"}],"title":"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.","publicationDate":"1997","journal":"Electrophoresis","firstPage":"1259","lastPage":"1313","volume":"18"},"referencePositions":["PROTEIN SEQUENCE OF 2-13"],"referenceComments":[{"value":"K12 / EMG2","type":"STRAIN"}]},{"referenceNumber":6,"citation":{"id":"9600841","citationType":"journal article","authors":["Wilkins M.R.","Gasteiger E.","Tonella L.","Ou K.","Tyler M.","Sanchez J.-C.","Gooley A.A.","Walsh B.J.","Bairoch A.","Appel R.D.","Williams K.L.","Hochstrasser D.F."],"citationCrossReferences":[{"database":"PubMed","id":"9600841"},{"database":"DOI","id":"10.1006/jmbi.1998.1726"}],"title":"Protein identification with N and C-terminal sequence tags in proteome projects.","publicationDate":"1998","journal":"J. Mol. Biol.","firstPage":"599","lastPage":"608","volume":"278"},"referencePositions":["PROTEIN SEQUENCE OF 2-5"],"referenceComments":[{"value":"K12 / W3110 / ATCC 27325 / DSM 5911","type":"STRAIN"}]},{"referenceNumber":7,"citation":{"id":"8436219","citationType":"journal article","authors":["Berry A.","Marshall K.E."],"citationCrossReferences":[{"database":"PubMed","id":"8436219"},{"database":"DOI","id":"10.1016/0014-5793(93)81317-s"}],"title":"Identification of zinc-binding ligands in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli.","publicationDate":"1993","journal":"FEBS Lett.","firstPage":"11","lastPage":"16","volume":"318"},"referencePositions":["MUTAGENESIS OF HIS-108; HIS-111 AND CYS-112"]},{"referenceNumber":8,"citation":{"id":"10712619","citationType":"journal article","authors":["Zgiby S.M.","Thomson G.J.","Qamar S.","Berry A."],"citationCrossReferences":[{"database":"PubMed","id":"10712619"},{"database":"DOI","id":"10.1046/j.1432-1327.2000.01191.x"}],"title":"Exploring substrate binding and discrimination in fructose 1,6-bisphosphate and tagatose 1,6-bisphosphate aldolases.","publicationDate":"2000","journal":"Eur. J. Biochem.","firstPage":"1858","lastPage":"1868","volume":"267"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","SUBSTRATE SPECIFICITY","KINETIC PARAMETERS","REACTION MECHANISM","MUTAGENESIS OF ASN-36; GLN-60; SER-62 AND LYS-326"],"referenceComments":[{"value":"K12 / MG1655 / ATCC 47076","type":"STRAIN"}]},{"referenceNumber":9,"citation":{"id":"18723842","citationType":"journal article","authors":["Zhang J.","Sprung R.","Pei J.","Tan X.","Kim S.","Zhu H.","Liu C.F.","Grishin N.V.","Zhao Y."],"citationCrossReferences":[{"database":"PubMed","id":"18723842"},{"database":"DOI","id":"10.1074/mcp.m800187-mcp200"}],"title":"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.","publicationDate":"2009","journal":"Mol. Cell. Proteomics","firstPage":"215","lastPage":"225","volume":"8"},"referencePositions":["ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9","IDENTIFICATION BY MASS SPECTROMETRY"],"referenceComments":[{"value":"K12 / JW1106","type":"STRAIN"},{"value":"K12 / MG1655 / ATCC 47076","type":"STRAIN"}]},{"referenceNumber":10,"citation":{"id":"19756045","citationType":"journal article","authors":["Nakahigashi K.","Toya Y.","Ishii N.","Soga T.","Hasegawa M.","Watanabe H.","Takai Y.","Honma M.","Mori H.","Tomita M."],"citationCrossReferences":[{"database":"PubMed","id":"19756045"},{"database":"DOI","id":"10.1038/msb.2009.65"}],"title":"Systematic phenome analysis of Escherichia coli multiple-knockout mutants reveals hidden reactions in central carbon metabolism.","publicationDate":"2009","journal":"Mol. Syst. Biol.","firstPage":"306","lastPage":"306","volume":"5"},"referencePositions":["FUNCTION IN SEDOHEPTULOSE BISPHOSPHATE BYPASS PATHWAY","CATALYTIC ACTIVITY"],"referenceComments":[{"value":"K12 / BW25113","type":"STRAIN"}]},{"referenceNumber":11,"citation":{"id":"21908771","citationType":"journal article","authors":["Peng C.","Lu Z.","Xie Z.","Cheng Z.","Chen Y.","Tan M.","Luo H.","Zhang Y.","He W.","Yang K.","Zwaans B.M.","Tishkoff D.","Ho L.","Lombard D.","He T.C.","Dai J.","Verdin E.","Ye Y.","Zhao Y."],"citationCrossReferences":[{"database":"PubMed","id":"21908771"},{"database":"DOI","id":"10.1074/mcp.m111.012658"}],"title":"The first identification of lysine malonylation substrates and its regulatory enzyme.","publicationDate":"2011","journal":"Mol. Cell. Proteomics","firstPage":"M111.012658.01","lastPage":"M111.012658.12","volume":"10"},"referencePositions":["MALONYLATION AT LYS-9"],"referenceComments":[{"value":"K12","type":"STRAIN"}]},{"referenceNumber":12,"citation":{"id":"21151122","citationType":"journal article","authors":["Zhang Z.","Tan M.","Xie Z.","Dai L.","Chen Y.","Zhao Y."],"citationCrossReferences":[{"database":"PubMed","id":"21151122"},{"database":"DOI","id":"10.1038/nchembio.495"}],"title":"Identification of lysine succinylation as a new post-translational modification.","publicationDate":"2011","journal":"Nat. Chem. Biol.","firstPage":"58","lastPage":"63","volume":"7"},"referencePositions":["SUCCINYLATION AT LYS-9; LYS-72; LYS-115; LYS-231; LYS-251; LYS-319; LYS-326 AND LYS-348"],"referenceComments":[{"value":"K12","type":"STRAIN"}]},{"referenceNumber":13,"citation":{"id":"8836102","citationType":"journal article","authors":["Blom N.S.","Tetreault S.","Coulombe R.","Sygusch J."],"citationCrossReferences":[{"database":"PubMed","id":"8836102"},{"database":"DOI","id":"10.1038/nsb1096-856"}],"title":"Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase.","publicationDate":"1996","journal":"Nat. Struct. Biol.","firstPage":"856","lastPage":"862","volume":"3"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) IN COMPLEX WITH ZINC"]},{"referenceNumber":14,"citation":{"id":"8939754","citationType":"journal article","authors":["Cooper S.J.","Leonard G.A.","McSweeney S.M.","Thompson A.W.","Naismith J.H.","Qamar S.","Plater A.","Berry A.","Hunter W.N."],"citationCrossReferences":[{"database":"PubMed","id":"8939754"},{"database":"DOI","id":"10.1016/s0969-2126(96)00138-4"}],"title":"The crystal structure of a class II fructose-1,6-bisphosphate aldolase shows a novel binuclear metal-binding active site embedded in a familiar fold.","publicationDate":"1996","journal":"Structure","firstPage":"1303","lastPage":"1315","volume":"4"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH ZINC"]},{"referenceNumber":15,"citation":{"id":"10080900","citationType":"journal article","authors":["Hall D.R.","Leonard G.A.","Reed C.D.","Watt C.I.","Berry A.","Hunter W.N."],"citationCrossReferences":[{"database":"PubMed","id":"10080900"},{"database":"DOI","id":"10.1006/jmbi.1999.2609"}],"title":"The crystal structure of Escherichia coli class II fructose-1, 6-bisphosphate aldolase in complex with phosphoglycolohydroxamate reveals details of mechanism and specificity.","publicationDate":"1999","journal":"J. Mol. Biol.","firstPage":"383","lastPage":"394","volume":"287"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC AND TRANSITION STATE ANALOG","ACTIVE SITE"]},{"referenceNumber":16,"citation":{"id":"12595741","citationType":"journal article","authors":["Hall D.R.","Kemp L.E.","Leonard G.A.","Marshall K.","Berry A.","Hunter W.N."],"citationCrossReferences":[{"database":"PubMed","id":"12595741"},{"database":"DOI","id":"10.1107/s0907444902023661"}],"title":"The organization of divalent cations in the active site of cadmium Escherichia coli fructose-1,6-bisphosphate aldolase.","publicationDate":"2003","journal":"Acta Crystallogr. D","firstPage":"611","lastPage":"614","volume":"59"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH CADMIUM","METAL BINDING SITES"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X14436","properties":[{"key":"ProteinId","value":"CAA32605.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"U28377","properties":[{"key":"ProteinId","value":"AAA69092.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"U00096","properties":[{"key":"ProteinId","value":"AAC75962.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AP009048","properties":[{"key":"ProteinId","value":"BAE76989.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"S02177","properties":[{"key":"EntryName","value":"ADEC2A"}]},{"database":"RefSeq","id":"NP_417400.1","properties":[{"key":"NucleotideSequenceId","value":"NC_000913.3"}]},{"database":"RefSeq","id":"WP_000034372.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP009789.1"}]},{"database":"PDB","id":"1B57","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.00 A"},{"key":"Chains","value":"A/B=2-359"}]},{"database":"PDB","id":"1DOS","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.67 A"},{"key":"Chains","value":"A/B=2-359"}]},{"database":"PDB","id":"1GYN","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.00 A"},{"key":"Chains","value":"A=2-359"}]},{"database":"PDB","id":"1ZEN","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.50 A"},{"key":"Chains","value":"A=2-359"}]},{"database":"PDB","id":"5GK3","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.80 A"},{"key":"Chains","value":"A/B=1-359"}]},{"database":"PDB","id":"5GK4","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.00 A"},{"key":"Chains","value":"A/B=1-359"}]},{"database":"PDB","id":"5GK5","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.90 A"},{"key":"Chains","value":"A/B/C/D/E/F/G/H=1-359"}]},{"database":"PDB","id":"5GK6","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.80 A"},{"key":"Chains","value":"A/B=1-359"}]},{"database":"PDB","id":"5GK7","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.80 A"},{"key":"Chains","value":"A/B=1-359"}]},{"database":"PDB","id":"5GK8","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.00 A"},{"key":"Chains","value":"A/B=1-359"}]},{"database":"PDB","id":"5VJD","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.70 A"},{"key":"Chains","value":"A/B=2-359"}]},{"database":"PDB","id":"5VJE","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.65 A"},{"key":"Chains","value":"A/B=2-359"}]},{"database":"PDBsum","id":"1B57","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"1DOS","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"1GYN","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"1ZEN","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"5GK3","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"5GK4","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"5GK5","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"5GK6","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"5GK7","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"5GK8","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"5VJD","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"5VJE","properties":[{"key":"Description","value":"-"}]},{"database":"AlphaFoldDB","id":"P0AB71","properties":[{"key":"Description","value":"-"}]},{"database":"MDRepo","id":"P0AB71","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P0AB71","properties":[{"key":"Description","value":"-"}]},{"database":"BioGRID","id":"4262069","properties":[{"key":"Interactions","value":"20"}]},{"database":"BioGRID","id":"851736","properties":[{"key":"Interactions","value":"2"}]},{"database":"DIP","id":"DIP-31872N","properties":[{"key":"Description","value":"-"}]},{"database":"FunCoup","id":"P0AB71","properties":[{"key":"Number of interactors","value":"586"}]},{"database":"IntAct","id":"P0AB71","properties":[{"key":"Interactions","value":"7"}]},{"database":"STRING","id":"511145.b2925","properties":[{"key":"Description","value":"-"}]},{"database":"BindingDB","id":"P0AB71","properties":[{"key":"Description","value":"-"}]},{"database":"ChEMBL","id":"CHEMBL4912","properties":[{"key":"Description","value":"-"}]},{"database":"DrugBank","id":"DB03026","properties":[{"key":"GenericName","value":"Phosphoglycolohydroxamic Acid"}]},{"database":"iPTMnet","id":"P0AB71","properties":[{"key":"Description","value":"-"}]},{"database":"jPOST","id":"P0AB71","properties":[{"key":"Description","value":"-"}]},{"database":"PaxDb","id":"511145-b2925","properties":[{"key":"Description","value":"-"}]},{"database":"EnsemblBacteria","id":"AAC75962","properties":[{"key":"ProteinId","value":"AAC75962"},{"key":"GeneId","value":"b2925"}]},{"database":"GeneID","id":"93779073","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"947415","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ecj:JW2892","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"eco:b2925","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ecoc:C3026_16025","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1411691.4.peg.3807","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"EchoBASE","id":"EB0278","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG0191","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"HOGENOM","id":"CLU_036923_0_0_6","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"P0AB71","properties":[{"key":"Description","value":"-"}]},{"database":"OMA","id":"HIDFVFH","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"OrthoDB","id":"9803995at2","properties":[{"key":"Description","value":"-"}]},{"database":"PhylomeDB","id":"P0AB71","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"EcoCyc:FRUCTBISALD-CLASSII-MONOMER","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"MetaCyc:FRUCTBISALD-CLASSII-MONOMER","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"4.1.2.13","properties":[{"key":"OrganismId","value":"2026"}]},{"database":"SABIO-RK","id":"P0AB71","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00109","properties":[{"key":"RectionId","value":"UER00183"}]},{"database":"EvolutionaryTrace","id":"P0AB71","properties":[{"key":"Description","value":"-"}]},{"database":"PRO","id":"PR:P0AB71","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000000625","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"AbasyAtlas","id":"P0AB71","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:0004332","properties":[{"key":"GoTerm","value":"F:fructose-bisphosphate aldolase activity"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"6996735"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"8436219"}]},{"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":"24561554"},{"evidenceCode":"ECO:0000353","source":"PubMed","id":"8836102"},{"evidenceCode":"ECO:0000353","source":"PubMed","id":"8939754"}]},{"database":"GO","id":"GO:0042803","properties":[{"key":"GoTerm","value":"F:protein homodimerization activity"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"8436219"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IDA:EcoliWiki"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"11985624"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"8436219"}]},{"database":"GO","id":"GO:0006094","properties":[{"key":"GoTerm","value":"P:gluconeogenesis"},{"key":"GoEvidenceType","value":"IBA:GO_Central"}]},{"database":"GO","id":"GO:0006096","properties":[{"key":"GoTerm","value":"P:glycolytic process"},{"key":"GoEvidenceType","value":"IMP:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"16562136"}]},{"database":"CDD","id":"cd00946","properties":[{"key":"EntryName","value":"FBP_aldolase_IIA"},{"key":"MatchStatus","value":"1"}]},{"database":"DisProt","id":"DP03662","properties":[{"key":"Description","value":"-"}]},{"database":"FunFam","id":"3.20.20.70:FF:000013","properties":[{"key":"EntryName","value":"Class II fructose-bisphosphate 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":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR000771","properties":[{"key":"EntryName","value":"FBA_II"}]},{"database":"InterPro","id":"IPR006411","properties":[{"key":"EntryName","value":"Fruct_bisP_bact"}]},{"database":"NCBIfam","id":"TIGR00167","properties":[{"key":"EntryName","value":"cbbA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01520","properties":[{"key":"EntryName","value":"FruBisAldo_II_A"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF006628","properties":[{"key":"EntryName","value":"PRK09197.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30559:SF0","properties":[{"key":"EntryName","value":"FRUCTOSE-BISPHOSPHATE ALDOLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30559","properties":[{"key":"EntryName","value":"FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01116","properties":[{"key":"EntryName","value":"F_bP_aldolase"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001359","properties":[{"key":"EntryName","value":"F_bP_aldolase_II"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51569","properties":[{"key":"EntryName","value":"Aldolase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00602","properties":[{"key":"EntryName","value":"ALDOLASE_CLASS_II_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00806","properties":[{"key":"EntryName","value":"ALDOLASE_CLASS_II_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSKIFDFVKPGVITGDDVQKVFQVAKENNFALPAVNCVGTDSINAVLETAAKVKAPVIVQFSNGGASFIAGKGVKSDVPQGAAILGAISGAHHVHQMAEHYGVPVILHTDHCAKKLLPWIDGLLDAGEKHFAATGKPLFSSHMIDLSEESLQENIEICSKYLERMSKIGMTLEIELGCTGGEEDGVDNSHMDASALYTQPEDVDYAYTELSKISPRFTIAASFGNVHGVYKPGNVVLTPTILRDSQEYVSKKHNLPHNSLNFVFHGGSGSTAQEIKDSVSYGVVKMNIDTDTQWATWEGVLNYYKANEAYLQGQLGNPKGEDQPNKKYYDPRVWLRAGQTSMIARLEKAFQELNAIDVL","length":359,"molWeight":39147,"crc64":"7A076D9EA62FBEC4","md5":"2850D15FF93041E80764356A1CB98B51"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":1,"SUBUNIT":1,"INTERACTION":2,"SIMILARITY":1},"countByFeatureType":{"Initiator methionine":1,"Chain":1,"Active site":1,"Binding site":9,"Modified residue":10,"Mutagenesis":8,"Helix":16,"Beta strand":12,"Turn":1},"uniParcId":"UPI00000380F1"}}