{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P00393","uniProtkbId":"NDH_ECOLI","entryAudit":{"firstPublicDate":"1986-07-21","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2007-01-23","entryVersion":194,"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":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Type II NADH:quinone oxidoreductase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10664466"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2679883"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6362717"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6784762"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7009604"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7020757"}],"value":"1.6.5.9"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10510271"}],"value":"Cupric reductase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10510271"}],"value":"1.16.1.-"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12176061"}],"value":"NADH dehydrogenase-2"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"3122832"}],"value":"NADH dh II"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"2679883"}],"value":"NDH-2"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"2679883"}],"value":"NADH-quinone reductase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"2679883"}],"value":"NQR"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"6784762"}],"value":"NADH:ubiquinone oxidoreductase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"6265208"}],"value":"Respiratory NADH dehydrogenase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"6265208"}],"value":"ndh"},"orderedLocusNames":[{"value":"b1109"},{"value":"JW1095"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10664466"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2679883"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3122832"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6362717"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6784762"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7009604"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7020757"}],"value":"Alternative, nonproton pumping NADH:quinone oxidoreductase that delivers electrons to the respiratory chain by oxidation of NADH and reduction of quinones (PubMed:10664466, PubMed:2679883, PubMed:3122832, PubMed:6362717, PubMed:6784762, PubMed:7009604, PubMed:7020757). Utilizes NADH exclusively, and electron flow from NADH to ubiquinone does not generate an electrochemical gradient (PubMed:2679883, PubMed:3122832)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10510271"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12176061"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16759635"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21390523"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7487066"}],"value":"It may also contribute to copper homeostasis and bacterial oxidative protection (PubMed:10510271, PubMed:16759635, PubMed:21390523, PubMed:7487066). Shows cupric reductase activity, and catalyzes the reduction of Cu(2+) to Cu(+) with NADH as electron donor (PubMed:10510271). Exhibits Cu(2+) reductase activity in the presence of either FAD or quinone, but is unable to reduce Fe(3+) (PubMed:10510271). Contains thiolate-bound copper (PubMed:12176061)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a quinone + NADH + H(+) = a quinol + NAD(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46160"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:24646"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:132124"}],"ecNumber":"1.6.5.9","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10664466"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2679883"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6362717"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6784762"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7009604"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7020757"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a ubiquinone + NADH + H(+) = a ubiquinol + NAD(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23152"},{"database":"Rhea","id":"RHEA-COMP:9565"},{"database":"Rhea","id":"RHEA-COMP:9566"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16389"},{"database":"ChEBI","id":"CHEBI:17976"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10664466"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2679883"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6362717"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6784762"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7009604"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7020757"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ubiquinone-8 + NADH + H(+) = ubiquinol-8 + NAD(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:29107"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:61682"},{"database":"ChEBI","id":"CHEBI:61683"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7020757"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 Cu(2+) + NADH = 2 Cu(+) + NAD(+) + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:66848"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29036"},{"database":"ChEBI","id":"CHEBI:49552"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10510271"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:66849"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10510271"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2679883"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6362717"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6784762"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7009604"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7020757"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6362717"}],"value":"Binds 1 FAD per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10510271"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2679883"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7009604"}],"value":"Requires Mg2(+) for activity in vitro (PubMed:2679883). Inhibited by 3-n-dodecylmercapto-2-hydroxy-1,4-naphthoquinone (PubMed:7009604). The quinone-dependent Cu(2+) reduction is partially inhibited by superoxide dismutase (PubMed:10510271)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"maximumVelocities":[{"velocity":106.0,"unit":"mmol/min/mg","enzyme":"enzyme with NADH as substrate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10664466"}]},{"velocity":106.0,"unit":"mmol/min/mg","enzyme":"enzyme with ubiquinone-1 as substrate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10664466"}]},{"velocity":190.0,"unit":"mmol/min/mg","enzyme":"enzyme with ubiquinone-2 as substrate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10664466"}]},{"velocity":191.0,"unit":"mmol/min/mg","enzyme":"enzyme with decylbenzoquinone as substrate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10664466"}]},{"velocity":107.0,"unit":"mmol/min/mg","enzyme":"enzyme with idebenone as substrate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10664466"}]},{"velocity":19.5,"unit":"mmol/min/mg","enzyme":"enzyme with dichlorophenolindophenol as substrate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10664466"}]},{"velocity":8.8,"unit":"umol/min/mg","enzyme":"enzyme (for cupric reductase activity, in the presence of FAD)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10510271"}]},{"velocity":21.1,"unit":"umol/min/mg","enzyme":"enzyme (for cupric reductase activity, in the presence of duroquinone)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10510271"}]}],"michaelisConstants":[{"constant":50.0,"unit":"uM","substrate":"NADH (for NADH:quinone oxidoreductase activity)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7009604"}]},{"constant":6.1,"unit":"uM","substrate":"NADH (for cupric reductase activity, in the presence of FAD)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10510271"}]},{"constant":6.9,"unit":"uM","substrate":"NADH (for cupric reductase activity, in the presence of duroquinone)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10510271"}]},{"constant":34.0,"unit":"uM","substrate":"NADH (for NADH:quinone oxidoreductase activity)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10664466"}]},{"constant":5.9,"unit":"uM","substrate":"ubiquinone-1","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10664466"}]},{"constant":2.3,"unit":"uM","substrate":"ubiquinone-2","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10664466"}]},{"constant":40.0,"unit":"uM","substrate":"ubiquinone-3 (for NADH:quinone oxidoreductase activity)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7009604"}]},{"constant":32.0,"unit":"uM","substrate":"duroquinone (for cupric reductase activity)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10510271"}]},{"constant":18.7,"unit":"uM","substrate":"decylbenzoquinone","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10664466"}]},{"constant":1.8,"unit":"uM","substrate":"idebenone","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10664466"}]},{"constant":20.0,"unit":"uM","substrate":"dichlorophenolindophenol","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10664466"}]},{"constant":12.0,"unit":"uM","substrate":"decylbenzoquinone (for NADH:quinone oxidoreductase activity)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7009604"}]},{"constant":0.022,"unit":"nM","substrate":"Cu(2+) (in the presence of FAD)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10510271"}]},{"constant":0.032,"unit":"nM","substrate":"Cu(2+) (in the presence of duroquinone)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10510271"}]},{"constant":102.0,"unit":"uM","substrate":"FAD (for cupric reductase activity)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10510271"}]}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21040753"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7020757"}],"value":"Monomer (PubMed:7020757). Forms a supercomplex with the NADH:quinone oxidoreductase NDH-1 in the aerobic respiratory chain (PubMed:21040753)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10664466"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15581635"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6362717"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7020757"}],"value":"Membrane-bound (PubMed:10664466). Interaction with the membrane is probably mediated by amphipathic helices and electrostatic interactions (PubMed:15581635). Copurifies with phospholipids (PubMed:6362717, PubMed:7020757)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10664466"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2679883"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6362717"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6784762"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7009604"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7020757"}],"value":"Cell inner membrane","id":"SL-0037"},"topology":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10664466"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12176061"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12176061"}],"value":"Cytoplasmic side","id":"SL-9910"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8809757"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9168602"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9308170"}],"value":"Expression is subject to a complex network of regulatory controls at the transcriptional level (PubMed:8809757, PubMed:9168602). Under anaerobic conditions, is repressed by the global transcriptional regulator FNR, which binds at two sites in the ndh promoter region (PubMed:9168602). Transcription can be activated or repressed by the DNA-binding protein Fis (Nbp): at high concentrations, during early-exponential phase, Fis represses ndh transcription by binding to at least three sites in the ndb promoter, whereas at low concentrations Fis activates ndh expression by binding solely to the far upstream high-affinity site (PubMed:8809757). Also regulated by the integration host factor (IHF) and the histone-like protein HU (PubMed:9308170)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12176061"}],"value":"Contains four structural/functional domains: the FAD-binding domain, the NAD(H)-binding domain, the copper-binding domain and the domain of anchorage to the membrane at the C-terminus"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16759635"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21390523"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8387992"}],"value":"Disruption mutant retains membrane-bound NADH dehydrogenase activity and shows no obvious growth defects. Mutations at two sites, one in ndh and one in nuo locus, remove the NADH oxidase activity from E.coli membranes (PubMed:8387992). The ndh deficient strain is more sensitive than the wild-type to Cu(II)/tert-butyl hydroperoxide (t-BOOH). Furthermore, several ndh deficient mutants grew less well than the corresponding parental strains in media containing either high or low copper concentrations (PubMed:16759635). The Cu(II)-reduction rate of the cell decreases by about 10% in the absence of NDH-2 and by about 85% in a strain lacking both NDH-2 and quinones (PubMed:21390523)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Activity in vitro is generally measured with ubiquinone-1 as the electron acceptor. The physiological electron acceptor is probably ubiquinone-8"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the NADH dehydrogenase 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":"6265208"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":434,"modifier":"EXACT"}},"description":"Type II NADH:quinone oxidoreductase","featureId":"PRO_0000079890"},{"type":"Binding site","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":16,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"15581635"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"15581635"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":84,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"15581635"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"15581635"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"15581635"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":275,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"15581635"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":315,"modifier":"EXACT"},"end":{"value":315,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"15581635"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":331,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"15581635"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}}],"keywords":[{"id":"KW-0997","category":"Cellular component","name":"Cell inner membrane"},{"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"id":"KW-0274","category":"Ligand","name":"FAD"},{"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0520","category":"Ligand","name":"NAD"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0813","category":"Biological process","name":"Transport"},{"id":"KW-0830","category":"Ligand","name":"Ubiquinone"}],"references":[{"referenceNumber":1,"citation":{"id":"6265208","citationType":"journal article","authors":["Young J.G.","Rogers B.L.","Campbell H.D.","Jaworowski A.","Shaw D.C."],"citationCrossReferences":[{"database":"PubMed","id":"6265208"},{"database":"DOI","id":"10.1111/j.1432-1033.1981.tb05314.x"}],"title":"Nucleotide sequence coding for the respiratory NADH dehydrogenase of Escherichia coli. UUG initiation codon.","publicationDate":"1981","journal":"Eur. J. Biochem.","firstPage":"165","lastPage":"170","volume":"116"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PROTEIN SEQUENCE OF 2-20"],"referenceComments":[{"value":"K12","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"8905232","citationType":"journal article","authors":["Oshima T.","Aiba H.","Baba T.","Fujita K.","Hayashi K.","Honjo A.","Ikemoto K.","Inada T.","Itoh T.","Kajihara M.","Kanai K.","Kashimoto K.","Kimura S.","Kitagawa M.","Makino K.","Masuda S.","Miki T.","Mizobuchi K.","Mori H.","Motomura K.","Nakamura Y.","Nashimoto H.","Nishio Y.","Saito N.","Sampei G.","Seki Y.","Tagami H.","Takemoto K.","Wada C.","Yamamoto Y.","Yano M.","Horiuchi T."],"citationCrossReferences":[{"database":"PubMed","id":"8905232"},{"database":"DOI","id":"10.1093/dnares/3.3.137"}],"title":"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map.","publicationDate":"1996","journal":"DNA Res.","firstPage":"137","lastPage":"155","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"K12 / W3110 / ATCC 27325 / DSM 5911","type":"STRAIN"}]},{"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":"6784762","citationType":"journal article","authors":["Jaworowski A.","Campbell H.D.","Poulis M.I.","Young I.G."],"citationCrossReferences":[{"database":"PubMed","id":"6784762"},{"database":"DOI","id":"10.1021/bi00510a047"}],"title":"Genetic identification and purification of the respiratory NADH dehydrogenase of Escherichia coli.","publicationDate":"1981","journal":"Biochemistry","firstPage":"2041","lastPage":"2047","volume":"20"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","COFACTOR","SUBCELLULAR LOCATION"],"referenceComments":[{"value":"K12","type":"STRAIN"}]},{"referenceNumber":6,"citation":{"id":"7009604","citationType":"journal article","authors":["Thomson J.W.","Shapiro B.M."],"citationCrossReferences":[{"database":"PubMed","id":"7009604"},{"database":"DOI","id":"10.1016/s0021-9258(19)69726-7"}],"title":"The respiratory chain NADH dehydrogenase of Escherichia coli. Isolation of an NADH:quinone oxidoreductase from membranes and comparison with the membrane-bound NADH:dichlorophenolindophenol oxidoreductase.","publicationDate":"1981","journal":"J. Biol. Chem.","firstPage":"3077","lastPage":"3084","volume":"256"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","COFACTOR","ACTIVITY REGULATION","BIOPHYSICOCHEMICAL PROPERTIES","SUBCELLULAR LOCATION"]},{"referenceNumber":7,"citation":{"id":"7020757","citationType":"journal article","authors":["Jaworowski A.","Mayo G.","Shaw D.C.","Campbell H.D.","Young I.G."],"citationCrossReferences":[{"database":"PubMed","id":"7020757"},{"database":"DOI","id":"10.1021/bi00515a049"}],"title":"Characterization of the respiratory NADH dehydrogenase of Escherichia coli and reconstitution of NADH oxidase in ndh mutant membrane vesicles.","publicationDate":"1981","journal":"Biochemistry","firstPage":"3621","lastPage":"3628","volume":"20"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","COFACTOR","SUBUNIT","SUBCELLULAR LOCATION"],"referenceComments":[{"value":"K12","type":"STRAIN"}]},{"referenceNumber":8,"citation":{"id":"6362717","citationType":"journal article","authors":["Campbell H.D.","Young I.G."],"citationCrossReferences":[{"database":"PubMed","id":"6362717"},{"database":"DOI","id":"10.1021/bi00294a012"}],"title":"Stereospecificity and requirements for activity of the respiratory NADH dehydrogenase of Escherichia coli.","publicationDate":"1983","journal":"Biochemistry","firstPage":"5754","lastPage":"5760","volume":"22"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","COFACTOR","SUBCELLULAR LOCATION"],"referenceComments":[{"value":"K12","type":"STRAIN"}]},{"referenceNumber":9,"citation":{"id":"3122832","citationType":"journal article","authors":["Matsushita K.","Ohnishi T.","Kaback H.R."],"citationCrossReferences":[{"database":"PubMed","id":"3122832"},{"database":"DOI","id":"10.1021/bi00398a029"}],"title":"NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain.","publicationDate":"1987","journal":"Biochemistry","firstPage":"7732","lastPage":"7737","volume":"26"},"referencePositions":["FUNCTION"]},{"referenceNumber":10,"citation":{"id":"2679883","citationType":"journal article","authors":["Hayashi M.","Miyoshi T.","Takashina S.","Unemoto T."],"citationCrossReferences":[{"database":"PubMed","id":"2679883"},{"database":"DOI","id":"10.1016/s0005-2728(89)80009-x"}],"title":"Purification of NADH-ferricyanide dehydrogenase and NADH-quinone reductase from Escherichia coli membranes and their roles in the respiratory chain.","publicationDate":"1989","journal":"Biochim. Biophys. Acta","firstPage":"62","lastPage":"69","volume":"977"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","COFACTOR","ACTIVITY REGULATION","SUBCELLULAR LOCATION"]},{"referenceNumber":11,"citation":{"id":"8387992","citationType":"journal article","authors":["Calhoun M.W.","Gennis R.B."],"citationCrossReferences":[{"database":"PubMed","id":"8387992"},{"database":"DOI","id":"10.1128/jb.175.10.3013-3019.1993"}],"title":"Demonstration of separate genetic loci encoding distinct membrane-bound respiratory NADH dehydrogenases in Escherichia coli.","publicationDate":"1993","journal":"J. Bacteriol.","firstPage":"3013","lastPage":"3019","volume":"175"},"referencePositions":["DISRUPTION PHENOTYPE"]},{"referenceNumber":12,"citation":{"id":"7487066","citationType":"journal article","authors":["Rodriguez-Montelongo L.","Farias R.N.","Massa E.M."],"citationCrossReferences":[{"database":"PubMed","id":"7487066"},{"database":"DOI","id":"10.1006/abbi.1995.0004"}],"title":"Sites of electron transfer to membrane-bound copper and hydroperoxide-induced damage in the respiratory chain of Escherichia coli.","publicationDate":"1995","journal":"Arch. Biochem. Biophys.","firstPage":"19","lastPage":"26","volume":"323"},"referencePositions":["FUNCTION"]},{"referenceNumber":13,"citation":{"id":"8809757","citationType":"journal article","authors":["Green J.","Anjum M.F.","Guest J.R."],"citationCrossReferences":[{"database":"PubMed","id":"8809757"},{"database":"DOI","id":"10.1111/j.1365-2958.1996.tb02545.x"}],"title":"The ndh-binding protein (Nbp) regulates the ndh gene of Escherichia coli in response to growth phase and is identical to Fis.","publicationDate":"1996","journal":"Mol. Microbiol.","firstPage":"1043","lastPage":"1055","volume":"20"},"referencePositions":["TRANSCRIPTIONAL REGULATION BY FIS"]},{"referenceNumber":14,"citation":{"id":"9168602","citationType":"journal article","authors":["Meng W.","Green J.","Guest J.R."],"citationCrossReferences":[{"database":"PubMed","id":"9168602"},{"database":"DOI","id":"10.1099/00221287-143-5-1521"}],"title":"FNR-dependent repression of ndh gene expression requires two upstream FNR-binding sites.","publicationDate":"1997","journal":"Microbiology","firstPage":"1521","lastPage":"1532","volume":"143"},"referencePositions":["TRANSCRIPTIONAL REGULATION BY FNR"]},{"referenceNumber":15,"citation":{"id":"9308170","citationType":"journal article","authors":["Green J.","Anjum M.F.","Guest J.R."],"citationCrossReferences":[{"database":"PubMed","id":"9308170"},{"database":"DOI","id":"10.1099/00221287-143-9-2865"}],"title":"Regulation of the ndh gene of Escherichia coli by integration host factor and a novel regulator, Arr.","publicationDate":"1997","journal":"Microbiology","firstPage":"2865","lastPage":"2875","volume":"143"},"referencePositions":["TRANSCRIPTIONAL REGULATION"]},{"referenceNumber":16,"citation":{"id":"10510271","citationType":"journal article","authors":["Rapisarda V.A.","Montelongo L.R.","Farias R.N.","Massa E.M."],"citationCrossReferences":[{"database":"PubMed","id":"10510271"},{"database":"DOI","id":"10.1006/abbi.1999.1398"}],"title":"Characterization of an NADH-linked cupric reductase activity from the Escherichia coli respiratory chain.","publicationDate":"1999","journal":"Arch. Biochem. Biophys.","firstPage":"143","lastPage":"150","volume":"370"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","ACTIVITY REGULATION","BIOPHYSICOCHEMICAL PROPERTIES"]},{"referenceNumber":17,"citation":{"id":"10664466","citationType":"journal article","authors":["Bjoerkloef K.","Zickermann V.","Finel M."],"citationCrossReferences":[{"database":"PubMed","id":"10664466"},{"database":"DOI","id":"10.1016/s0014-5793(00)01130-3"}],"title":"Purification of the 45 kDa, membrane bound NADH dehydrogenase of Escherichia coli (NDH-2) and analysis of its interaction with ubiquinone analogues.","publicationDate":"2000","journal":"FEBS Lett.","firstPage":"105","lastPage":"110","volume":"467"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES","SUBCELLULAR LOCATION"]},{"referenceNumber":18,"citation":{"id":"12176061","citationType":"journal article","authors":["Rapisarda V.A.","Chehin R.N.","De Las Rivas J.","Rodriguez-Montelongo L.","Farias R.N.","Massa E.M."],"citationCrossReferences":[{"database":"PubMed","id":"12176061"},{"database":"DOI","id":"10.1016/s0003-9861(02)00277-1"}],"title":"Evidence for Cu(I)-thiolate ligation and prediction of a putative copper-binding site in the Escherichia coli NADH dehydrogenase-2.","publicationDate":"2002","journal":"Arch. Biochem. Biophys.","firstPage":"87","lastPage":"94","volume":"405"},"referencePositions":["FUNCTION","COPPER-BINDING","SUBCELLULAR LOCATION","DOMAIN"]},{"referenceNumber":19,"citation":{"id":"16759635","citationType":"journal article","authors":["Rodriguez-Montelongo L.","Volentini S.I.","Farias R.N.","Massa E.M.","Rapisarda V.A."],"citationCrossReferences":[{"database":"PubMed","id":"16759635"},{"database":"DOI","id":"10.1016/j.abb.2006.04.019"}],"title":"The Cu(II)-reductase NADH dehydrogenase-2 of Escherichia coli improves the bacterial growth in extreme copper concentrations and increases the resistance to the damage caused by copper and hydroperoxide.","publicationDate":"2006","journal":"Arch. Biochem. Biophys.","firstPage":"1","lastPage":"7","volume":"451"},"referencePositions":["FUNCTION","DISRUPTION PHENOTYPE"]},{"referenceNumber":20,"citation":{"id":"21040753","citationType":"journal article","authors":["Sousa P.M.","Silva S.T.","Hood B.L.","Charro N.","Carita J.N.","Vaz F.","Penque D.","Conrads T.P.","Melo A.M."],"citationCrossReferences":[{"database":"PubMed","id":"21040753"},{"database":"DOI","id":"10.1016/j.biochi.2010.10.014"}],"title":"Supramolecular organizations in the aerobic respiratory chain of Escherichia coli.","publicationDate":"2011","journal":"Biochimie","firstPage":"418","lastPage":"425","volume":"93"},"referencePositions":["SUBUNIT"]},{"referenceNumber":21,"citation":{"id":"21390523","citationType":"journal article","authors":["Volentini S.I.","Farias R.N.","Rodriguez-Montelongo L.","Rapisarda V.A."],"citationCrossReferences":[{"database":"PubMed","id":"21390523"},{"database":"DOI","id":"10.1007/s10534-011-9436-3"}],"title":"Cu(II)-reduction by Escherichia coli cells is dependent on respiratory chain components.","publicationDate":"2011","journal":"BioMetals","firstPage":"827","lastPage":"835","volume":"24"},"referencePositions":["FUNCTION","DISRUPTION PHENOTYPE"]},{"referenceNumber":22,"citation":{"id":"15581635","citationType":"journal article","authors":["Schmid R.","Gerloff D.L."],"citationCrossReferences":[{"database":"PubMed","id":"15581635"},{"database":"DOI","id":"10.1016/j.febslet.2004.10.093"}],"title":"Functional properties of the alternative NADH:ubiquinone oxidoreductase from E. coli through comparative 3-D modelling.","publicationDate":"2004","journal":"FEBS Lett.","firstPage":"163","lastPage":"168","volume":"578"},"referencePositions":["3D MODELING","SUBCELLULAR LOCATION"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"V00306","properties":[{"key":"ProteinId","value":"CAA23586.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"U00096","properties":[{"key":"ProteinId","value":"AAC74193.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AP009048","properties":[{"key":"ProteinId","value":"BAA35924.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"A00461","properties":[{"key":"EntryName","value":"DEECR"}]},{"database":"RefSeq","id":"NP_415627.1","properties":[{"key":"NucleotideSequenceId","value":"NC_000913.3"}]},{"database":"RefSeq","id":"WP_000211045.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP009789.1"}]},{"database":"AlphaFoldDB","id":"P00393","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P00393","properties":[{"key":"Description","value":"-"}]},{"database":"BioGRID","id":"4260082","properties":[{"key":"Interactions","value":"91"}]},{"database":"DIP","id":"DIP-10325N","properties":[{"key":"Description","value":"-"}]},{"database":"FunCoup","id":"P00393","properties":[{"key":"Number of interactors","value":"520"}]},{"database":"IntAct","id":"P00393","properties":[{"key":"Interactions","value":"9"}]},{"database":"STRING","id":"511145.b1109","properties":[{"key":"Description","value":"-"}]},{"database":"PeroxiBase","id":"5949","properties":[{"key":"EntryName","value":"EcoNadDH_K12"}]},{"database":"jPOST","id":"P00393","properties":[{"key":"Description","value":"-"}]},{"database":"PaxDb","id":"511145-b1109","properties":[{"key":"Description","value":"-"}]},{"database":"EnsemblBacteria","id":"AAC74193","properties":[{"key":"ProteinId","value":"AAC74193"},{"key":"GeneId","value":"b1109"}]},{"database":"GeneID","id":"93776299","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"946792","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ecj:JW1095","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"eco:b1109","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ecoc:C3026_06690","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1411691.4.peg.1158","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"EchoBASE","id":"EB0643","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG1252","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"HOGENOM","id":"CLU_021377_7_0_6","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"P00393","properties":[{"key":"Description","value":"-"}]},{"database":"OMA","id":"DHCIFLD","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"OrthoDB","id":"9781621at2","properties":[{"key":"Description","value":"-"}]},{"database":"PhylomeDB","id":"P00393","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"EcoCyc:NADH-DHII-MONOMER","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"MetaCyc:NADH-DHII-MONOMER","properties":[{"key":"Description","value":"-"}]},{"database":"PRO","id":"PR:P00393","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000000625","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"AbasyAtlas","id":"P00393","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0030964","properties":[{"key":"GoTerm","value":"C:NADH dehydrogenase complex"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"7020757"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"7020757"}]},{"database":"GO","id":"GO:0008823","properties":[{"key":"GoTerm","value":"F:cupric reductase (NADH) activity"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10510271"}]},{"database":"GO","id":"GO:0050660","properties":[{"key":"GoTerm","value":"F:flavin adenine dinucleotide binding"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"2679883"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"7020757"}]},{"database":"GO","id":"GO:0050136","properties":[{"key":"GoTerm","value":"F:NADH dehydrogenase (quinone) (non-electrogenic) activity"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10664466"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2679883"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6362717"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6784762"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7009604"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7020757"}]},{"database":"GO","id":"GO:0120555","properties":[{"key":"GoTerm","value":"F:NADH dehydrogenase (ubiquinone) (non-electrogenic) activity"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10664466"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2679883"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6362717"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6784762"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7009604"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7020757"}]},{"database":"GO","id":"GO:0008137","properties":[{"key":"GoTerm","value":"F:NADH dehydrogenase (ubiquinone) activity"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"7020757"}]},{"database":"GO","id":"GO:0019646","properties":[{"key":"GoTerm","value":"P:aerobic electron transport chain"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"3122832"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"6784762"}]},{"database":"GO","id":"GO:0009060","properties":[{"key":"GoTerm","value":"P:aerobic respiration"},{"key":"GoEvidenceType","value":"IMP:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"9063459"}]},{"database":"GO","id":"GO:0009061","properties":[{"key":"GoTerm","value":"P:anaerobic respiration"},{"key":"GoEvidenceType","value":"IMP:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"9063459"}]},{"database":"GO","id":"GO:0055070","properties":[{"key":"GoTerm","value":"P:copper ion homeostasis"},{"key":"GoEvidenceType","value":"IMP:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"16759635"},{"evidenceCode":"ECO:0000315","source":"PubMed","id":"21390523"}]},{"database":"FunFam","id":"3.50.50.100:FF:000001","properties":[{"key":"EntryName","value":"NADH dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.50.50.100","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036188","properties":[{"key":"EntryName","value":"FAD/NAD-bd_sf"}]},{"database":"InterPro","id":"IPR023753","properties":[{"key":"EntryName","value":"FAD/NAD-binding_dom"}]},{"database":"InterPro","id":"IPR051169","properties":[{"key":"EntryName","value":"NADH-Q_oxidoreductase"}]},{"database":"PANTHER","id":"PTHR42913:SF3","properties":[{"key":"EntryName","value":"64 KDA MITOCHONDRIAL NADH DEHYDROGENASE (EUROFUNG)"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42913","properties":[{"key":"EntryName","value":"APOPTOSIS-INDUCING FACTOR 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07992","properties":[{"key":"EntryName","value":"Pyr_redox_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00368","properties":[{"key":"EntryName","value":"FADPNR"}]},{"database":"PRINTS","id":"PR00411","properties":[{"key":"EntryName","value":"PNDRDTASEI"}]},{"database":"SUPFAM","id":"SSF51905","properties":[{"key":"EntryName","value":"FAD/NAD(P)-binding domain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTTPLKKIVIVGGGAGGLEMATQLGHKLGRKKKAKITLVDRNHSHLWKPLLHEVATGSLDEGVDALSYLAHARNHGFQFQLGSVIDIDREAKTITIAELRDEKGELLVPERKIAYDTLVMALGSTSNDFNTPGVKENCIFLDNPHQARRFHQEMLNLFLKYSANLGANGKVNIAIVGGGATGVELSAELHNAVKQLHSYGYKGLTNEALNVTLVEAGERILPALPPRISAAAHNELTKLGVRVLTQTMVTSADEGGLHTKDGEYIEADLMVWAAGIKAPDFLKDIGGLETNRINQLVVEPTLQTTRDPDIYAIGDCASCPRPEGGFVPPRAQAAHQMATCAMNNILAQMNGKPLKNYQYKDHGSLVSLSNFSTVGSLMGNLTRGSMMIEGRIARFVYISLYRMHQIALHGYFKTGLMMLVGSINRVIRPRLKLH","length":434,"molWeight":47359,"crc64":"3C3F4FA0E31E10E1","md5":"D24034B9ACE40A5FD0C0A6D3C8EC0E21"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":4,"COFACTOR":1,"ACTIVITY REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"INDUCTION":1,"DOMAIN":1,"DISRUPTION PHENOTYPE":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Initiator methionine":1,"Chain":1,"Binding site":8},"uniParcId":"UPI000011DD2D"}}