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Can also use 5-deoxyribulose 1-phosphate to yield acetaldehyde and dihydroxyacetone phosphate (PubMed:31950558). Part of a bifunctional DHAP-shunt salvage pathway for SAM by-products (PubMed:31950558)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5-(methylsulfanyl)-D-ribulose 1-phosphate = 2-(methylsulfanyl)acetaldehyde + dihydroxyacetone phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:56940"},{"database":"ChEBI","id":"CHEBI:57642"},{"database":"ChEBI","id":"CHEBI:58548"},{"database":"ChEBI","id":"CHEBI:141184"}],"ecNumber":"4.1.2.62","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29133429"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31950558"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:56941"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31950558"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5-deoxy-D-ribulose 1-phosphate = dihydroxyacetone phosphate + acetaldehyde","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:61300"},{"database":"ChEBI","id":"CHEBI:15343"},{"database":"ChEBI","id":"CHEBI:57642"},{"database":"ChEBI","id":"CHEBI:144504"}],"ecNumber":"4.1.2.62","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31950558"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:61301"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31950558"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Co(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31950558"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:48828"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0AB87"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31950558"}],"value":"Binds 1 cobalt ion per subunit (By similarity). Can also use Ni(2+) (PubMed:31950558)."}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":288.0,"unit":"uM","substrate":"5-methylthioribulose-1-phosphate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31950558"}]},{"constant":229.0,"unit":"uM","substrate":"5-deoxyribulose 1-phosphate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31950558"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31950558"}],"value":"kcat is 0.94 sec(-1) with 5-methylthioribulose-1-phosphate as substrate. kcat is 1.94 sec(-1) with 5-deoxyribulose 1-phosphate as substrate. kcat is 0.44 sec(-1) with ribulose-1-phosphate as substrate."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"29133429"}],"value":"Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29133429"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31950558"}],"value":"Mutants produce only low levels of ethylene when grown on MTA (PubMed:29133429). Deletion mutant accumulates both S-methyl-5'-thioadenosine and 5'-deoxyadenosine extracellularly (PubMed:31950558)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the aldolase class II family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"5-methylthioribulose-1-phosphate/5-deoxyribulose-1-phosphate aldolase","featureId":"PRO_0000445035"},{"type":"Active site","location":{"start":{"value":75,"modifier":"EXACT"},"end":{"value":75,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0AB87"}]},{"type":"Binding site","location":{"start":{"value":75,"modifier":"EXACT"},"end":{"value":75,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:48828"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0AB87"}],"ligand":{"name":"Co(2+)","id":"ChEBI:CHEBI:48828","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":94,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:48828"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0AB87"}],"ligand":{"name":"Co(2+)","id":"ChEBI:CHEBI:48828","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":96,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:48828"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0AB87"}],"ligand":{"name":"Co(2+)","id":"ChEBI:CHEBI:48828","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:48828"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0AB87"}],"ligand":{"name":"Co(2+)","id":"ChEBI:CHEBI:48828","note":"catalytic"}},{"type":"Site","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":115,"modifier":"EXACT"}},"description":"Plays a key role in the stabilization of the transition state and positioning the aldehyde component","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0AB87"}]},{"type":"Site","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"Plays a key role in the stabilization of the transition state and positioning the aldehyde component","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0AB87"}]},{"type":"Site","location":{"start":{"value":210,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"Plays a key role in the stabilization of the transition state and positioning the aldehyde component","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0AB87"}]}],"keywords":[{"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"id":"KW-0170","category":"Ligand","name":"Cobalt"},{"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0486","category":"Biological process","name":"Methionine biosynthesis"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"21886856","citationType":"journal article","authors":["Munk A.C.","Copeland A.","Lucas S.","Lapidus A.","Del Rio T.G.","Barry K.","Detter J.C.","Hammon N.","Israni S.","Pitluck S.","Brettin T.","Bruce D.","Han C.","Tapia R.","Gilna P.","Schmutz J.","Larimer F.","Land M.","Kyrpides N.C.","Mavromatis K.","Richardson P.","Rohde M.","Goeker M.","Klenk H.P.","Zhang Y.","Roberts G.P.","Reslewic S.","Schwartz D.C."],"citationCrossReferences":[{"database":"PubMed","id":"21886856"},{"database":"DOI","id":"10.4056/sigs.1804360"}],"title":"Complete genome sequence of Rhodospirillum rubrum type strain (S1).","publicationDate":"2011","journal":"Stand. 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