{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P0A9V8","secondaryAccessions":["P32142","Q2M8H9"],"uniProtkbId":"SQUU_ECOLI","entryAudit":{"firstPublicDate":"2005-07-19","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2005-07-19","entryVersion":138,"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:0000255","source":"HAMAP-Rule","id":"MF_01913"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"24463506"}],"value":"3-sulfolactaldehyde reductase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01913"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"24463506"}],"value":"SLA reductase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01913"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24463506"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.6"}],"value":"1.1.1.373"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"4-hydroxybutyrate dehydrogenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19372223"}],"value":"1.1.1.61"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19372223"}],"value":"Gamma-hydroxybutyrate dehydrogenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19372223"}],"value":"GHBDH"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19372223"}],"value":"Succinic semialdehyde reductase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19372223"}],"value":"SSA reductase"}]}]},"genes":[{"geneName":{"value":"yihU"},"orderedLocusNames":[{"value":"b3882"},{"value":"JW3853"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19372223"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24463506"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.6"}],"value":"Reduces 3-sulfolactaldehyde (SLA) to 2,3-dihydroxypropane 1-sulfonate (DHPS) (PubMed:24463506, Ref.6). Metabolite profiling studies showed that the enzyme also catalyzes in vitro the NADH-dependent reduction of succinic semialdehyde (SSA) to 4-hydroxybutyrate (GHB), and that it could be involved in the metabolism of SSA, and other potentially toxic intermediates that may accumulate under stress conditions (PubMed:19372223). However, the enzyme exhibits a 42,000-fold greater catalytic efficiency for the reduction of SLA over SSA (Ref.6). Shows no detectable activity on the analogous glycolytic intermediate glyceraldehyde-3-phosphate (Ref.6)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2S)-3-sulfopropanediol + NAD(+) = (2S)-3-sulfolactaldehyde + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:40511"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:90109"},{"database":"ChEBI","id":"CHEBI:176527"}],"ecNumber":"1.1.1.373","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01913"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24463506"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.6"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:40513"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24463506"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.6"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"4-hydroxybutanoate + NAD(+) = succinate semialdehyde + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23948"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16724"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57706"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.1.1.61","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19372223"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.6"}],"value":"Inhibited by the NADH analogs tetrahydro-NADH and hexahydro-NADH"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"maximumVelocities":[{"velocity":0.2,"unit":"umol/min/mg","enzyme":"enzyme with succinic semialdehyde as substrate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19372223"}]},{"velocity":0.067,"unit":"umol/min/mg","enzyme":"enzyme with methylglyoxal as substrate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19372223"}]},{"velocity":0.062,"unit":"umol/min/mg","enzyme":"enzyme with 4-hydroxybutyrate as substrate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19372223"}]},{"velocity":9.0,"unit":"umol/min/mg","enzyme":"enzyme with 3-hydroxypropane sulfonate as substrate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19372223"}]}],"michaelisConstants":[{"constant":0.3,"unit":"mM","substrate":"3-sulfolactaldehyde","evidences":[{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.6"}]},{"constant":0.082,"unit":"mM","substrate":"NADH","evidences":[{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.6"}]},{"constant":4.3,"unit":"mM","substrate":"succinic semialdehyde","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19372223"}]},{"constant":9.0,"unit":"mM","substrate":"methylglyoxal","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19372223"}]},{"constant":102.0,"unit":"mM","substrate":"4-hydroxybutyrate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19372223"}]},{"constant":1.0,"unit":"mM","substrate":"3-hydroxypropane sulfonate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19372223"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.6"}],"value":"kcat is 332 sec(-1) with 3-sulfolactaldehyde as substrate. kcat is 548 sec(-1) with NADH as substrate."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19372223"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.6"}],"value":"Homotetramer (PubMed:19372223, Ref.6). Dimer of dimers (Ref.6)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24463506"}],"value":"Induced during growth with sulfoquinovose"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19372223"}],"value":"Deletion mutant displays reduced tolerance to the cytotoxic effects of exogenous addition of succinic semialdehyde"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01913"},{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the HIBADH-related family. 3-sulfolactaldehyde reductase subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"3-sulfolactaldehyde reductase","featureId":"PRO_0000173064"},{"type":"Active site","location":{"start":{"value":171,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01913"},{"evidenceCode":"ECO:0000305","source":"Reference","id":"Ref.6"}]},{"type":"Binding site","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01913"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.6"},{"evidenceCode":"ECO:0000312","source":"PDB","id":"6SMY"},{"evidenceCode":"ECO:0000312","source":"PDB","id":"6SMZ"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":31,"modifier":"EXACT"},"end":{"value":31,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01913"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.6"},{"evidenceCode":"ECO:0000312","source":"PDB","id":"6SMY"},{"evidenceCode":"ECO:0000312","source":"PDB","id":"6SMZ"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":65,"modifier":"EXACT"},"end":{"value":65,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01913"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.6"},{"evidenceCode":"ECO:0000312","source":"PDB","id":"6SMY"},{"evidenceCode":"ECO:0000312","source":"PDB","id":"6SMZ"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":96,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01913"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.6"},{"evidenceCode":"ECO:0000312","source":"PDB","id":"6SMY"},{"evidenceCode":"ECO:0000312","source":"PDB","id":"6SMZ"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:77138"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01913"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.6"},{"evidenceCode":"ECO:0000312","source":"PDB","id":"6SMY"}],"ligand":{"name":"2,3-dihydroxypropane-1-sulfonate","id":"ChEBI:CHEBI:77138"}},{"type":"Binding site","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":178,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:77138"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01913"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.6"},{"evidenceCode":"ECO:0000312","source":"PDB","id":"6SMY"}],"ligand":{"name":"2,3-dihydroxypropane-1-sulfonate","id":"ChEBI:CHEBI:77138"}},{"type":"Binding site","location":{"start":{"value":240,"modifier":"EXACT"},"end":{"value":240,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01913"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.6"},{"evidenceCode":"ECO:0000312","source":"PDB","id":"6SMY"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Mutagenesis","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"25-fold decrease in catalytic efficiency with SLA as substrate. 5-fold decrease in catalytic efficiency with NADH as substrate.","evidences":[{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.6"}],"alternativeSequence":{"originalSequence":"G","alternativeSequences":["S"]}},{"type":"Mutagenesis","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"130-fold decrease in catalytic efficiency with SLA as substrate. 3-fold decrease in catalytic efficiency with NADH as substrate.","evidences":[{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.6"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["G"]}},{"type":"Mutagenesis","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"230-fold decrease in catalytic efficiency with SLA as substrate. 12-fold decrease in catalytic efficiency with NADH as substrate.","evidences":[{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.6"}],"alternativeSequence":{"originalSequence":"T","alternativeSequences":["G"]}},{"type":"Beta strand","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":7,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Helix","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Beta strand","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Helix","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Helix","location":{"start":{"value":51,"modifier":"EXACT"},"end":{"value":55,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Beta strand","location":{"start":{"value":59,"modifier":"EXACT"},"end":{"value":63,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Helix","location":{"start":{"value":68,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Helix","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":84,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Beta strand","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Helix","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":111,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Beta strand","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Beta strand","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Helix","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":130,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Beta strand","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Helix","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":151,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Turn","location":{"start":{"value":152,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Beta strand","location":{"start":{"value":155,"modifier":"EXACT"},"end":{"value":160,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Helix","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Helix","location":{"start":{"value":199,"modifier":"EXACT"},"end":{"value":206,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Helix","location":{"start":{"value":210,"modifier":"EXACT"},"end":{"value":213,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Turn","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Turn","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Helix","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":226,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Beta strand","location":{"start":{"value":232,"modifier":"EXACT"},"end":{"value":234,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Helix","location":{"start":{"value":235,"modifier":"EXACT"},"end":{"value":251,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Helix","location":{"start":{"value":257,"modifier":"EXACT"},"end":{"value":271,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Helix","location":{"start":{"value":279,"modifier":"EXACT"},"end":{"value":281,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Helix","location":{"start":{"value":282,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]},{"type":"Helix","location":{"start":{"value":292,"modifier":"EXACT"},"end":{"value":294,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SMZ"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0520","category":"Ligand","name":"NAD"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"8346018","citationType":"journal article","authors":["Plunkett G. III","Burland V.","Daniels D.L.","Blattner F.R."],"citationCrossReferences":[{"database":"PubMed","id":"8346018"},{"database":"DOI","id":"10.1093/nar/21.15.3391"}],"title":"Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes.","publicationDate":"1993","journal":"Nucleic Acids Res.","firstPage":"3391","lastPage":"3398","volume":"21"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"K12 / MG1655 / ATCC 47076","type":"STRAIN"}]},{"referenceNumber":2,"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":3,"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":4,"citation":{"id":"19372223","citationType":"journal article","authors":["Saito N.","Robert M.","Kochi H.","Matsuo G.","Kakazu Y.","Soga T.","Tomita M."],"citationCrossReferences":[{"database":"PubMed","id":"19372223"},{"database":"DOI","id":"10.1074/jbc.m109.002089"}],"title":"Metabolite profiling reveals YihU as a novel hydroxybutyrate dehydrogenase for alternative succinic semialdehyde metabolism in Escherichia coli.","publicationDate":"2009","journal":"J. Biol. Chem.","firstPage":"16442","lastPage":"16451","volume":"284"},"referencePositions":["FUNCTION AS A SUCCINIC SEMIALDEHYDE REDUCTASE","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES","SUBUNIT","DISRUPTION PHENOTYPE"]},{"referenceNumber":5,"citation":{"id":"24463506","citationType":"journal article","authors":["Denger K.","Weiss M.","Felux A.K.","Schneider A.","Mayer C.","Spiteller D.","Huhn T.","Cook A.M.","Schleheck D."],"citationCrossReferences":[{"database":"PubMed","id":"24463506"},{"database":"DOI","id":"10.1038/nature12947"}],"title":"Sulphoglycolysis in Escherichia coli K-12 closes a gap in the biogeochemical sulphur cycle.","publicationDate":"2014","journal":"Nature","firstPage":"114","lastPage":"117","volume":"507"},"referencePositions":["FUNCTION AS A SULFOLACTALDEHYDE REDUCTASE","CATALYTIC ACTIVITY","INDUCTION","IDENTIFICATION BY MASS SPECTROMETRY"],"referenceComments":[{"value":"K12","type":"STRAIN"}]},{"referenceNumber":6,"citation":{"id":"CI-B6MBH1OM2MV07","citationType":"journal article","authors":["Sharma M.","Abayakoon P.","Lingford J.P.","Epa R.","John A.","Jin Y.","Goddard-Borger E.D.","Davies G.J.","Williams S.J."],"citationCrossReferences":[{"database":"DOI","id":"10.1021/acscatal.9b04427"}],"title":"Dynamic structural changes accompany the production of dihydroxypropanesulfonate by sulfolactaldehyde reductase.","publicationDate":"2020","journal":"ACS Catal.","firstPage":"2826","lastPage":"2836","volume":"10"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH NAD AND 2,3-DIHYDROXYPROPANE-1-SULFONATE","FUNCTION","CATALYTIC ACTIVITY","REACTION MECHANISM","ACTIVITY REGULATION","BIOPHYSICOCHEMICAL PROPERTIES","SUBUNIT","ACTIVE SITE","MUTAGENESIS OF GLY-122; ARG-123 AND THR-124"],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"6SM7"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"6SMY"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"6SMZ"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"L19201","properties":[{"key":"ProteinId","value":"AAB03015.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"U00096","properties":[{"key":"ProteinId","value":"AAD13444.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AP009048","properties":[{"key":"ProteinId","value":"BAE77427.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"S40826","properties":[{"key":"EntryName","value":"S40826"}]},{"database":"RefSeq","id":"NP_418318.1","properties":[{"key":"NucleotideSequenceId","value":"NC_000913.3"}]},{"database":"RefSeq","id":"WP_000718893.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP009789.1"}]},{"database":"PDB","id":"6SM7","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.88 A"},{"key":"Chains","value":"A/B/C/D=1-298"}]},{"database":"PDB","id":"6SMY","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.45 A"},{"key":"Chains","value":"A/B/C/D=1-298"}]},{"database":"PDB","id":"6SMZ","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.75 A"},{"key":"Chains","value":"A/B/C/D=1-298"}]},{"database":"PDBsum","id":"6SM7","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"6SMY","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"6SMZ","properties":[{"key":"Description","value":"-"}]},{"database":"AlphaFoldDB","id":"P0A9V8","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P0A9V8","properties":[{"key":"Description","value":"-"}]},{"database":"BioGRID","id":"4260959","properties":[{"key":"Interactions","value":"14"}]},{"database":"DIP","id":"DIP-48142N","properties":[{"key":"Description","value":"-"}]},{"database":"FunCoup","id":"P0A9V8","properties":[{"key":"Number of interactors","value":"280"}]},{"database":"IntAct","id":"P0A9V8","properties":[{"key":"Interactions","value":"7"}]},{"database":"STRING","id":"511145.b3882","properties":[{"key":"Description","value":"-"}]},{"database":"PaxDb","id":"511145-b3882","properties":[{"key":"Description","value":"-"}]},{"database":"EnsemblBacteria","id":"AAD13444","properties":[{"key":"ProteinId","value":"AAD13444"},{"key":"GeneId","value":"b3882"}]},{"database":"GeneID","id":"75204553","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"948372","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ecj:JW3853","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"eco:b3882","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ecoc:C3026_20985","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1411691.4.peg.2829","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"EchoBASE","id":"EB1793","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG2084","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"HOGENOM","id":"CLU_035117_1_1_6","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"P0A9V8","properties":[{"key":"Description","value":"-"}]},{"database":"OMA","id":"MGKKVWH","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"OrthoDB","id":"9786703at2","properties":[{"key":"Description","value":"-"}]},{"database":"PhylomeDB","id":"P0A9V8","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"EcoCyc:EG11847-MONOMER","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"MetaCyc:EG11847-MONOMER","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"1.1.1.373","properties":[{"key":"OrganismId","value":"2026"}]},{"database":"BRENDA","id":"1.1.1.61","properties":[{"key":"OrganismId","value":"2026"}]},{"database":"PRO","id":"PR:P0A9V8","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000000625","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"AbasyAtlas","id":"P0A9V8","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0032991","properties":[{"key":"GoTerm","value":"C:protein-containing complex"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"19372223"}]},{"database":"GO","id":"GO:0061596","properties":[{"key":"GoTerm","value":"F:3-sulfolactaldehyde reductase activity"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"24463506"}]},{"database":"GO","id":"GO:0047577","properties":[{"key":"GoTerm","value":"F:4-hydroxybutyrate dehydrogenase activity"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"19372223"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"19372223"}]},{"database":"GO","id":"GO:0051287","properties":[{"key":"GoTerm","value":"F:NAD binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0050661","properties":[{"key":"GoTerm","value":"F:NADP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:1902777","properties":[{"key":"GoTerm","value":"P:6-sulfoquinovose(1-) catabolic process"},{"key":"GoEvidenceType","value":"IEP:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000270","source":"PubMed","id":"24463506"}]},{"database":"GO","id":"GO:0061720","properties":[{"key":"GoTerm","value":"P:6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"24463506"}]},{"database":"GO","id":"GO:0051289","properties":[{"key":"GoTerm","value":"P:protein homotetramerization"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"19372223"}]},{"database":"GO","id":"GO:0009407","properties":[{"key":"GoTerm","value":"P:toxin catabolic process"},{"key":"GoEvidenceType","value":"IMP:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"19372223"}]},{"database":"FunFam","id":"1.10.1040.10:FF:000022","properties":[{"key":"EntryName","value":"3-sulfolactaldehyde reductase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.720:FF:000352","properties":[{"key":"EntryName","value":"3-sulfolactaldehyde reductase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1040.10","properties":[{"key":"EntryName","value":"N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01913","properties":[{"key":"EntryName","value":"SLA_reductase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002204","properties":[{"key":"EntryName","value":"3-OH-isobutyrate_DH-rel_CS"}]},{"database":"InterPro","id":"IPR008927","properties":[{"key":"EntryName","value":"6-PGluconate_DH-like_C_sf"}]},{"database":"InterPro","id":"IPR013328","properties":[{"key":"EntryName","value":"6PGD_dom2"}]},{"database":"InterPro","id":"IPR006115","properties":[{"key":"EntryName","value":"6PGDH_NADP-bd"}]},{"database":"InterPro","id":"IPR029154","properties":[{"key":"EntryName","value":"HIBADH-like_NADP-bd"}]},{"database":"InterPro","id":"IPR015815","properties":[{"key":"EntryName","value":"HIBADH-related"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"InterPro","id":"IPR030876","properties":[{"key":"EntryName","value":"SLA_reductase"}]},{"database":"NCBIfam","id":"NF012005","properties":[{"key":"EntryName","value":"PRK15461.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR22981:SF7","properties":[{"key":"EntryName","value":"3-HYDROXYISOBUTYRATE DEHYDROGENASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR22981","properties":[{"key":"EntryName","value":"3-HYDROXYISOBUTYRATE DEHYDROGENASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14833","properties":[{"key":"EntryName","value":"NAD_binding_11"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03446","properties":[{"key":"EntryName","value":"NAD_binding_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000103","properties":[{"key":"EntryName","value":"HIBADH"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48179","properties":[{"key":"EntryName","value":"6-phosphogluconate dehydrogenase C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00895","properties":[{"key":"EntryName","value":"3_HYDROXYISOBUT_DH"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAAIAFIGLGQMGSPMASNLLQQGHQLRVFDVNAEAVRHLVDKGATPAANPAQAAKDAEFIITMLPNGDLVRNVLFGENGVCEGLSTDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSANAITGTLLLLAGGTAEQVERATPILMAMGSELINAGGPGMGIRVKLINNYMSIALNALSAEAAVLCEALNLPFDVAVKVMSGTAAGKGHFTTSWPNKVLSGDLSPAFMIDLAHKDLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQVRVSAGMTAKVKM","length":298,"molWeight":31158,"crc64":"74FBC8C09FA7881C","md5":"679D405644FB92419F37416A17E37634"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"ACTIVITY REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"SUBUNIT":1,"INDUCTION":1,"DISRUPTION PHENOTYPE":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":1,"Binding site":7,"Mutagenesis":3,"Beta strand":9,"Helix":17,"Turn":3},"uniParcId":"UPI000013B404"}}