NDH_ECOLI
ID NDH_ECOLI Reviewed; 434 AA.
AC P00393;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Type II NADH:quinone oxidoreductase {ECO:0000305};
DE EC=1.6.5.9 {ECO:0000269|PubMed:10664466, ECO:0000269|PubMed:2679883, ECO:0000269|PubMed:6362717, ECO:0000269|PubMed:6784762, ECO:0000269|PubMed:7009604, ECO:0000269|PubMed:7020757};
DE AltName: Full=Cupric reductase {ECO:0000303|PubMed:10510271};
DE EC=1.16.1.- {ECO:0000269|PubMed:10510271};
DE AltName: Full=NADH dehydrogenase-2 {ECO:0000303|PubMed:12176061};
DE Short=NADH dh II {ECO:0000303|PubMed:3122832};
DE Short=NDH-2 {ECO:0000303|PubMed:2679883};
DE AltName: Full=NADH-quinone reductase {ECO:0000303|PubMed:2679883};
DE Short=NQR {ECO:0000303|PubMed:2679883};
DE AltName: Full=NADH:ubiquinone oxidoreductase {ECO:0000303|PubMed:6784762};
DE AltName: Full=Respiratory NADH dehydrogenase {ECO:0000303|PubMed:6265208};
GN Name=ndh {ECO:0000303|PubMed:6265208}; OrderedLocusNames=b1109, JW1095;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-20.
RC STRAIN=K12;
RX PubMed=6265208; DOI=10.1111/j.1432-1033.1981.tb05314.x;
RA Young J.G., Rogers B.L., Campbell H.D., Jaworowski A., Shaw D.C.;
RT "Nucleotide sequence coding for the respiratory NADH dehydrogenase of
RT Escherichia coli. UUG initiation codon.";
RL Eur. J. Biochem. 116:165-170(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=6784762; DOI=10.1021/bi00510a047;
RA Jaworowski A., Campbell H.D., Poulis M.I., Young I.G.;
RT "Genetic identification and purification of the respiratory NADH
RT dehydrogenase of Escherichia coli.";
RL Biochemistry 20:2041-2047(1981).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=7009604; DOI=10.1016/s0021-9258(19)69726-7;
RA Thomson J.W., Shapiro B.M.;
RT "The respiratory chain NADH dehydrogenase of Escherichia coli. Isolation of
RT an NADH:quinone oxidoreductase from membranes and comparison with the
RT membrane-bound NADH:dichlorophenolindophenol oxidoreductase.";
RL J. Biol. Chem. 256:3077-3084(1981).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=7020757; DOI=10.1021/bi00515a049;
RA Jaworowski A., Mayo G., Shaw D.C., Campbell H.D., Young I.G.;
RT "Characterization of the respiratory NADH dehydrogenase of Escherichia coli
RT and reconstitution of NADH oxidase in ndh mutant membrane vesicles.";
RL Biochemistry 20:3621-3628(1981).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=6362717; DOI=10.1021/bi00294a012;
RA Campbell H.D., Young I.G.;
RT "Stereospecificity and requirements for activity of the respiratory NADH
RT dehydrogenase of Escherichia coli.";
RL Biochemistry 22:5754-5760(1983).
RN [9]
RP FUNCTION.
RX PubMed=3122832; DOI=10.1021/bi00398a029;
RA Matsushita K., Ohnishi T., Kaback H.R.;
RT "NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic
RT respiratory chain.";
RL Biochemistry 26:7732-7737(1987).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=2679883; DOI=10.1016/s0005-2728(89)80009-x;
RA Hayashi M., Miyoshi T., Takashina S., Unemoto T.;
RT "Purification of NADH-ferricyanide dehydrogenase and NADH-quinone reductase
RT from Escherichia coli membranes and their roles in the respiratory chain.";
RL Biochim. Biophys. Acta 977:62-69(1989).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=8387992; DOI=10.1128/jb.175.10.3013-3019.1993;
RA Calhoun M.W., Gennis R.B.;
RT "Demonstration of separate genetic loci encoding distinct membrane-bound
RT respiratory NADH dehydrogenases in Escherichia coli.";
RL J. Bacteriol. 175:3013-3019(1993).
RN [12]
RP FUNCTION.
RX PubMed=7487066; DOI=10.1006/abbi.1995.0004;
RA Rodriguez-Montelongo L., Farias R.N., Massa E.M.;
RT "Sites of electron transfer to membrane-bound copper and hydroperoxide-
RT induced damage in the respiratory chain of Escherichia coli.";
RL Arch. Biochem. Biophys. 323:19-26(1995).
RN [13]
RP TRANSCRIPTIONAL REGULATION BY FIS.
RX PubMed=8809757; DOI=10.1111/j.1365-2958.1996.tb02545.x;
RA Green J., Anjum M.F., Guest J.R.;
RT "The ndh-binding protein (Nbp) regulates the ndh gene of Escherichia coli
RT in response to growth phase and is identical to Fis.";
RL Mol. Microbiol. 20:1043-1055(1996).
RN [14]
RP TRANSCRIPTIONAL REGULATION BY FNR.
RX PubMed=9168602; DOI=10.1099/00221287-143-5-1521;
RA Meng W., Green J., Guest J.R.;
RT "FNR-dependent repression of ndh gene expression requires two upstream FNR-
RT binding sites.";
RL Microbiology 143:1521-1532(1997).
RN [15]
RP TRANSCRIPTIONAL REGULATION.
RX PubMed=9308170; DOI=10.1099/00221287-143-9-2865;
RA Green J., Anjum M.F., Guest J.R.;
RT "Regulation of the ndh gene of Escherichia coli by integration host factor
RT and a novel regulator, Arr.";
RL Microbiology 143:2865-2875(1997).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=10510271; DOI=10.1006/abbi.1999.1398;
RA Rapisarda V.A., Montelongo L.R., Farias R.N., Massa E.M.;
RT "Characterization of an NADH-linked cupric reductase activity from the
RT Escherichia coli respiratory chain.";
RL Arch. Biochem. Biophys. 370:143-150(1999).
RN [17]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10664466; DOI=10.1016/s0014-5793(00)01130-3;
RA Bjoerkloef K., Zickermann V., Finel M.;
RT "Purification of the 45 kDa, membrane bound NADH dehydrogenase of
RT Escherichia coli (NDH-2) and analysis of its interaction with ubiquinone
RT analogues.";
RL FEBS Lett. 467:105-110(2000).
RN [18]
RP FUNCTION, COPPER-BINDING, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=12176061; DOI=10.1016/s0003-9861(02)00277-1;
RA Rapisarda V.A., Chehin R.N., De Las Rivas J., Rodriguez-Montelongo L.,
RA Farias R.N., Massa E.M.;
RT "Evidence for Cu(I)-thiolate ligation and prediction of a putative copper-
RT binding site in the Escherichia coli NADH dehydrogenase-2.";
RL Arch. Biochem. Biophys. 405:87-94(2002).
RN [19]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16759635; DOI=10.1016/j.abb.2006.04.019;
RA Rodriguez-Montelongo L., Volentini S.I., Farias R.N., Massa E.M.,
RA Rapisarda V.A.;
RT "The Cu(II)-reductase NADH dehydrogenase-2 of Escherichia coli improves the
RT bacterial growth in extreme copper concentrations and increases the
RT resistance to the damage caused by copper and hydroperoxide.";
RL Arch. Biochem. Biophys. 451:1-7(2006).
RN [20]
RP SUBUNIT.
RX PubMed=21040753; DOI=10.1016/j.biochi.2010.10.014;
RA Sousa P.M., Silva S.T., Hood B.L., Charro N., Carita J.N., Vaz F.,
RA Penque D., Conrads T.P., Melo A.M.;
RT "Supramolecular organizations in the aerobic respiratory chain of
RT Escherichia coli.";
RL Biochimie 93:418-425(2011).
RN [21]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21390523; DOI=10.1007/s10534-011-9436-3;
RA Volentini S.I., Farias R.N., Rodriguez-Montelongo L., Rapisarda V.A.;
RT "Cu(II)-reduction by Escherichia coli cells is dependent on respiratory
RT chain components.";
RL BioMetals 24:827-835(2011).
RN [22]
RP 3D MODELING, AND SUBCELLULAR LOCATION.
RX PubMed=15581635; DOI=10.1016/j.febslet.2004.10.093;
RA Schmid R., Gerloff D.L.;
RT "Functional properties of the alternative NADH:ubiquinone oxidoreductase
RT from E. coli through comparative 3-D modelling.";
RL FEBS Lett. 578:163-168(2004).
CC -!- FUNCTION: Alternative, nonproton pumping NADH:quinone oxidoreductase
CC that delivers electrons to the respiratory chain by oxidation of NADH
CC and reduction of quinones (PubMed:6784762, PubMed:7009604,
CC PubMed:7020757, PubMed:6362717, PubMed:3122832, PubMed:2679883,
CC PubMed:10664466). Utilizes NADH exclusively, and electron flow from
CC NADH to ubiquinone does not generate an electrochemical gradient
CC (PubMed:3122832, PubMed:2679883). {ECO:0000269|PubMed:10664466,
CC ECO:0000269|PubMed:2679883, ECO:0000269|PubMed:3122832,
CC ECO:0000269|PubMed:6362717, ECO:0000269|PubMed:6784762,
CC ECO:0000269|PubMed:7009604, ECO:0000269|PubMed:7020757}.
CC -!- FUNCTION: It may also contribute to copper homeostasis and bacterial
CC oxidative protection (PubMed:7487066, PubMed:10510271, PubMed:16759635,
CC PubMed:21390523). Shows cupric reductase activity, and catalyzes the
CC reduction of Cu(2+) to Cu(+) with NADH as electron donor
CC (PubMed:10510271). Exhibits Cu(2+) reductase activity in the presence
CC of either FAD or quinone, but is unable to reduce Fe(3+)
CC (PubMed:10510271). Contains thiolate-bound copper (PubMed:12176061).
CC {ECO:0000269|PubMed:10510271, ECO:0000269|PubMed:12176061,
CC ECO:0000269|PubMed:16759635, ECO:0000269|PubMed:21390523,
CC ECO:0000269|PubMed:7487066}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.9;
CC Evidence={ECO:0000269|PubMed:10664466, ECO:0000269|PubMed:2679883,
CC ECO:0000269|PubMed:6362717, ECO:0000269|PubMed:6784762,
CC ECO:0000269|PubMed:7009604, ECO:0000269|PubMed:7020757};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + H(+) + NADH = a ubiquinol + NAD(+);
CC Xref=Rhea:RHEA:23152, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:10664466, ECO:0000269|PubMed:2679883,
CC ECO:0000269|PubMed:6362717, ECO:0000269|PubMed:6784762,
CC ECO:0000269|PubMed:7009604, ECO:0000269|PubMed:7020757};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADH + ubiquinone-8 = NAD(+) + ubiquinol-8;
CC Xref=Rhea:RHEA:29107, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:61682, ChEBI:CHEBI:61683;
CC Evidence={ECO:0000269|PubMed:7020757};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Cu(2+) + NADH = 2 Cu(+) + H(+) + NAD(+);
CC Xref=Rhea:RHEA:66848, ChEBI:CHEBI:15378, ChEBI:CHEBI:29036,
CC ChEBI:CHEBI:49552, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:10510271};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66849;
CC Evidence={ECO:0000269|PubMed:10510271};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:2679883, ECO:0000269|PubMed:6362717,
CC ECO:0000269|PubMed:6784762, ECO:0000269|PubMed:7009604,
CC ECO:0000269|PubMed:7020757};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:6362717};
CC -!- ACTIVITY REGULATION: Requires Mg2(+) for activity in vitro
CC (PubMed:2679883). Inhibited by 3-n-dodecylmercapto-2-hydroxy-1,4-
CC naphthoquinone (PubMed:7009604). The quinone-dependent Cu(2+) reduction
CC is partially inhibited by superoxide dismutase (PubMed:10510271).
CC {ECO:0000269|PubMed:10510271, ECO:0000269|PubMed:2679883,
CC ECO:0000269|PubMed:7009604}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 uM for NADH (for NADH:quinone oxidoreductase activity)
CC {ECO:0000269|PubMed:7009604};
CC KM=6.1 uM for NADH (for cupric reductase activity, in the presence of
CC FAD) {ECO:0000269|PubMed:10510271};
CC KM=6.9 uM for NADH (for cupric reductase activity, in the presence of
CC duroquinone) {ECO:0000269|PubMed:10510271};
CC KM=34 uM for NADH (for NADH:quinone oxidoreductase activity)
CC {ECO:0000269|PubMed:10664466};
CC KM=5.9 uM for ubiquinone-1 {ECO:0000269|PubMed:10664466};
CC KM=2.3 uM for ubiquinone-2 {ECO:0000269|PubMed:10664466};
CC KM=40 uM for ubiquinone-3 (for NADH:quinone oxidoreductase activity)
CC {ECO:0000269|PubMed:7009604};
CC KM=32 uM for duroquinone (for cupric reductase activity)
CC {ECO:0000269|PubMed:10510271};
CC KM=18.7 uM for decylbenzoquinone {ECO:0000269|PubMed:10664466};
CC KM=1.8 uM for idebenone {ECO:0000269|PubMed:10664466};
CC KM=20 uM for dichlorophenolindophenol {ECO:0000269|PubMed:10664466};
CC KM=12 uM for decylbenzoquinone (for NADH:quinone oxidoreductase
CC activity) {ECO:0000269|PubMed:7009604};
CC KM=0.022 nM for Cu(2+) (in the presence of FAD)
CC {ECO:0000269|PubMed:10510271};
CC KM=0.032 nM for Cu(2+) (in the presence of duroquinone)
CC {ECO:0000269|PubMed:10510271};
CC KM=102 uM for FAD (for cupric reductase activity)
CC {ECO:0000269|PubMed:10510271};
CC Vmax=106 mmol/min/mg enzyme with NADH as substrate
CC {ECO:0000269|PubMed:10664466};
CC Vmax=106 mmol/min/mg enzyme with ubiquinone-1 as substrate
CC {ECO:0000269|PubMed:10664466};
CC Vmax=190 mmol/min/mg enzyme with ubiquinone-2 as substrate
CC {ECO:0000269|PubMed:10664466};
CC Vmax=191 mmol/min/mg enzyme with decylbenzoquinone as substrate
CC {ECO:0000269|PubMed:10664466};
CC Vmax=107 mmol/min/mg enzyme with idebenone as substrate
CC {ECO:0000269|PubMed:10664466};
CC Vmax=19.5 mmol/min/mg enzyme with dichlorophenolindophenol as
CC substrate {ECO:0000269|PubMed:10664466};
CC Vmax=8.8 umol/min/mg enzyme (for cupric reductase activity, in the
CC presence of FAD) {ECO:0000269|PubMed:10510271};
CC Vmax=21.1 umol/min/mg enzyme (for cupric reductase activity, in the
CC presence of duroquinone) {ECO:0000269|PubMed:10510271};
CC -!- SUBUNIT: Monomer (PubMed:7020757). Forms a supercomplex with the
CC NADH:quinone oxidoreductase NDH-1 in the aerobic respiratory chain
CC (PubMed:21040753). {ECO:0000269|PubMed:21040753,
CC ECO:0000269|PubMed:7020757}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:10664466,
CC ECO:0000269|PubMed:2679883, ECO:0000269|PubMed:6362717,
CC ECO:0000269|PubMed:6784762, ECO:0000269|PubMed:7009604,
CC ECO:0000269|PubMed:7020757}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10664466, ECO:0000305|PubMed:12176061}; Cytoplasmic
CC side {ECO:0000305|PubMed:12176061}. Note=Membrane-bound
CC (PubMed:10664466). Interaction with the membrane is probably mediated
CC by amphipathic helices and electrostatic interactions
CC (PubMed:15581635). Copurifies with phospholipids (PubMed:7020757,
CC PubMed:6362717). {ECO:0000269|PubMed:10664466,
CC ECO:0000269|PubMed:15581635, ECO:0000269|PubMed:6362717,
CC ECO:0000269|PubMed:7020757}.
CC -!- INDUCTION: Expression is subject to a complex network of regulatory
CC controls at the transcriptional level (PubMed:8809757, PubMed:9168602).
CC Under anaerobic conditions, is repressed by the global transcriptional
CC regulator FNR, which binds at two sites in the ndh promoter region
CC (PubMed:9168602). Transcription can be activated or repressed by the
CC DNA-binding protein Fis (Nbp): at high concentrations, during early-
CC exponential phase, Fis represses ndh transcription by binding to at
CC least three sites in the ndb promoter, whereas at low concentrations
CC Fis activates ndh expression by binding solely to the far upstream
CC high-affinity site (PubMed:8809757). Also regulated by the integration
CC host factor (IHF) and the histone-like protein HU (PubMed:9308170).
CC {ECO:0000269|PubMed:8809757, ECO:0000269|PubMed:9168602,
CC ECO:0000269|PubMed:9308170}.
CC -!- DOMAIN: Contains four structural/functional domains: the FAD-binding
CC domain, the NAD(H)-binding domain, the copper-binding domain and the
CC domain of anchorage to the membrane at the C-terminus.
CC {ECO:0000305|PubMed:12176061}.
CC -!- DISRUPTION PHENOTYPE: Disruption mutant retains membrane-bound NADH
CC dehydrogenase activity and shows no obvious growth defects. Mutations
CC at two sites, one in ndh and one in nuo locus, remove the NADH oxidase
CC activity from E.coli membranes (PubMed:8387992). The ndh deficient
CC strain is more sensitive than the wild-type to Cu(II)/tert-butyl
CC hydroperoxide (t-BOOH). Furthermore, several ndh deficient mutants grew
CC less well than the corresponding parental strains in media containing
CC either high or low copper concentrations (PubMed:16759635). The Cu(II)-
CC reduction rate of the cell decreases by about 10% in the absence of
CC NDH-2 and by about 85% in a strain lacking both NDH-2 and quinones
CC (PubMed:21390523). {ECO:0000269|PubMed:16759635,
CC ECO:0000269|PubMed:21390523, ECO:0000269|PubMed:8387992}.
CC -!- MISCELLANEOUS: Activity in vitro is generally measured with ubiquinone-
CC 1 as the electron acceptor. The physiological electron acceptor is
CC probably ubiquinone-8. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family. {ECO:0000305}.
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DR EMBL; V00306; CAA23586.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74193.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35924.1; -; Genomic_DNA.
DR PIR; A00461; DEECR.
DR RefSeq; NP_415627.1; NC_000913.3.
DR RefSeq; WP_000211045.1; NZ_STEB01000016.1.
DR AlphaFoldDB; P00393; -.
DR SMR; P00393; -.
DR BioGRID; 4260082; 82.
DR DIP; DIP-10325N; -.
DR IntAct; P00393; 9.
DR STRING; 511145.b1109; -.
DR PeroxiBase; 5949; EcoNadDH_K12.
DR jPOST; P00393; -.
DR PaxDb; P00393; -.
DR PRIDE; P00393; -.
DR EnsemblBacteria; AAC74193; AAC74193; b1109.
DR EnsemblBacteria; BAA35924; BAA35924; BAA35924.
DR GeneID; 66670625; -.
DR GeneID; 946792; -.
DR KEGG; ecj:JW1095; -.
DR KEGG; eco:b1109; -.
DR PATRIC; fig|1411691.4.peg.1158; -.
DR EchoBASE; EB0643; -.
DR eggNOG; COG1252; Bacteria.
DR HOGENOM; CLU_021377_7_0_6; -.
DR InParanoid; P00393; -.
DR OMA; DHCIFLD; -.
DR PhylomeDB; P00393; -.
DR BioCyc; EcoCyc:NADH-DHII-MON; -.
DR BioCyc; MetaCyc:NADH-DHII-MON; -.
DR PRO; PR:P00393; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030964; C:NADH dehydrogenase complex; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoCyc.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IDA:EcoCyc.
DR GO; GO:0019646; P:aerobic electron transport chain; IDA:EcoCyc.
DR GO; GO:0009060; P:aerobic respiration; IMP:EcoCyc.
DR GO; GO:0009061; P:anaerobic respiration; IMP:EcoCyc.
DR GO; GO:0055070; P:copper ion homeostasis; IMP:EcoCyc.
DR GO; GO:0006116; P:NADH oxidation; IEA:InterPro.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR045024; NDH-2.
DR PANTHER; PTHR43706; PTHR43706; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Direct protein sequencing;
KW Electron transport; FAD; Flavoprotein; Membrane; NAD; Oxidoreductase;
KW Reference proteome; Transport; Ubiquinone.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6265208"
FT CHAIN 2..434
FT /note="Type II NADH:quinone oxidoreductase"
FT /id="PRO_0000079890"
FT BINDING 12..16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000305|PubMed:15581635"
FT BINDING 42
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000305|PubMed:15581635"
FT BINDING 84
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000305|PubMed:15581635"
FT BINDING 124
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000305|PubMed:15581635"
FT BINDING 176..181
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000305|PubMed:15581635"
FT BINDING 275
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000305|PubMed:15581635"
FT BINDING 315
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000305|PubMed:15581635"
FT BINDING 331
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000305|PubMed:15581635"
SQ SEQUENCE 434 AA; 47359 MW; 3C3F4FA0E31E10E1 CRC64;
MTTPLKKIVI VGGGAGGLEM ATQLGHKLGR KKKAKITLVD RNHSHLWKPL LHEVATGSLD
EGVDALSYLA HARNHGFQFQ LGSVIDIDRE AKTITIAELR DEKGELLVPE RKIAYDTLVM
ALGSTSNDFN TPGVKENCIF LDNPHQARRF HQEMLNLFLK YSANLGANGK VNIAIVGGGA
TGVELSAELH NAVKQLHSYG YKGLTNEALN VTLVEAGERI LPALPPRISA AAHNELTKLG
VRVLTQTMVT SADEGGLHTK DGEYIEADLM VWAAGIKAPD FLKDIGGLET NRINQLVVEP
TLQTTRDPDI YAIGDCASCP RPEGGFVPPR AQAAHQMATC AMNNILAQMN GKPLKNYQYK
DHGSLVSLSN FSTVGSLMGN LTRGSMMIEG RIARFVYISL YRMHQIALHG YFKTGLMMLV
GSINRVIRPR LKLH
