NUON_ECOLI
ID NUON_ECOLI Reviewed; 485 AA.
AC P0AFF0; P33608; P78281;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=NADH-quinone oxidoreductase subunit N {ECO:0000255|HAMAP-Rule:MF_00445};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_00445};
DE AltName: Full=NADH dehydrogenase I subunit N {ECO:0000255|HAMAP-Rule:MF_00445};
DE AltName: Full=NDH-1 subunit N {ECO:0000255|HAMAP-Rule:MF_00445};
DE AltName: Full=NUO14;
GN Name=nuoN {ECO:0000255|HAMAP-Rule:MF_00445};
GN OrderedLocusNames=b2276, JW2271;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / AN387;
RX PubMed=7690854; DOI=10.1006/jmbi.1993.1488;
RA Weidner U., Geier S., Ptock A., Friedrich T., Leif H., Weiss H.;
RT "The gene locus of the proton-translocating NADH: ubiquinone oxidoreductase
RT in Escherichia coli. Organization of the 14 genes and relationship between
RT the derived proteins and subunits of mitochondrial complex I.";
RL J. Mol. Biol. 233:109-122(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
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 IDENTIFICATION OF START CODON, MUTAGENESIS OF MET-1; LYS-158; LYS-217;
RP HIS-224; LYS-247; GLY-391 AND LYS-395, AND DISRUPTION PHENOTYPE.
RX PubMed=12718520; DOI=10.1021/bi0340346;
RA Amarneh B., Vik S.B.;
RT "Mutagenesis of subunit N of the Escherichia coli complex I. Identification
RT of the initiation codon and the sensitivity of mutants to
RT decylubiquinone.";
RL Biochemistry 42:4800-4808(2003).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC electron acceptor for the enzyme in this species is believed to be
CC ubiquinone. Couples the redox reaction to proton translocation (for
CC every two electrons transferred, four hydrogen ions are translocated
CC across the cytoplasmic membrane), and thus conserves the redox energy
CC in a proton gradient.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00445};
CC -!- SUBUNIT: NDH-1 is composed of 13 different subunits. Subunits NuoA, H,
CC J, K, L, M, N constitute the membrane sector of the complex.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- DISRUPTION PHENOTYPE: Cells gene grow very poorly on M65 minimal medium
CC containing acetate but normally on rich medium (LB).
CC {ECO:0000269|PubMed:12718520}.
CC -!- MISCELLANEOUS: A construct which produces a protein lacking the first
CC amino acids has only 5% of the wild-type rate of deamino-NADH oxidase.
CC -!- SIMILARITY: Belongs to the complex I subunit 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_00445}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA16103.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA48373.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X68301; CAA48373.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75336.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA16103.1; ALT_INIT; Genomic_DNA.
DR PIR; B64999; B64999.
DR PIR; S38323; S38323.
DR RefSeq; NP_416779.2; NC_000913.3.
DR RefSeq; WP_000156701.1; NZ_SSZK01000006.1.
DR PDB; 7NYH; EM; 3.60 A; N=1-485.
DR PDB; 7NYR; EM; 3.30 A; N=1-485.
DR PDB; 7NYU; EM; 3.80 A; N=1-485.
DR PDB; 7NYV; EM; 3.70 A; N=1-485.
DR PDBsum; 7NYH; -.
DR PDBsum; 7NYR; -.
DR PDBsum; 7NYU; -.
DR PDBsum; 7NYV; -.
DR AlphaFoldDB; P0AFF0; -.
DR SMR; P0AFF0; -.
DR BioGRID; 4260885; 54.
DR ComplexPortal; CPX-243; Respiratory chain complex I.
DR DIP; DIP-59256N; -.
DR IntAct; P0AFF0; 1.
DR STRING; 511145.b2276; -.
DR TCDB; 3.D.1.1.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR jPOST; P0AFF0; -.
DR PaxDb; P0AFF0; -.
DR PRIDE; P0AFF0; -.
DR EnsemblBacteria; AAC75336; AAC75336; b2276.
DR EnsemblBacteria; BAA16103; BAA16103; BAA16103.
DR GeneID; 60904033; -.
DR GeneID; 945136; -.
DR KEGG; ecj:JW2271; -.
DR KEGG; eco:b2276; -.
DR PATRIC; fig|1411691.4.peg.4460; -.
DR EchoBASE; EB2017; -.
DR eggNOG; COG1007; Bacteria.
DR HOGENOM; CLU_007100_1_5_6; -.
DR InParanoid; P0AFF0; -.
DR OMA; FYIRVIV; -.
DR PhylomeDB; P0AFF0; -.
DR BioCyc; EcoCyc:NUON-MON; -.
DR BioCyc; MetaCyc:NUON-MON; -.
DR PRO; PR:P0AFF0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0030964; C:NADH dehydrogenase complex; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0045272; C:plasma membrane respiratory chain complex I; IDA:EcoCyc.
DR GO; GO:0045271; C:respiratory chain complex I; IC:ComplexPortal.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IMP:EcoCyc.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0009060; P:aerobic respiration; IMP:EcoCyc.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR GO; GO:0015990; P:electron transport coupled proton transport; IMP:EcoCyc.
DR GO; GO:0022904; P:respiratory electron transport chain; IDA:ComplexPortal.
DR HAMAP; MF_00445; NDH1_NuoN_1; 1.
DR InterPro; IPR010096; NADH-Q_OxRdtase_suN/2.
DR InterPro; IPR001750; ND/Mrp_mem.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR TIGRFAMs; TIGR01770; NDH_I_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport; Ubiquinone.
FT CHAIN 1..485
FT /note="NADH-quinone oxidoreductase subunit N"
FT /id="PRO_0000117688"
FT TOPO_DOM 1..7
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TOPO_DOM 29..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TOPO_DOM 56..70
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TOPO_DOM 92..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TOPO_DOM 126
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TOPO_DOM 148..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TOPO_DOM 180..202
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TOPO_DOM 224..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TOPO_DOM 256..270
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TOPO_DOM 292..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TOPO_DOM 318..325
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TOPO_DOM 347..372
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TOPO_DOM 394..407
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..430
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TOPO_DOM 431..454
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TOPO_DOM 476..485
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 1
FT /note="M->H: Shows 20% of the wild-type rate of deamino-
FT NADH oxidase."
FT /evidence="ECO:0000269|PubMed:12718520"
FT MUTAGEN 158
FT /note="K->C: Shows 50% of the wild-type rate of deamino-
FT NADH oxidase. Inhibited by 30-50% upon addition of 0.25 mM
FT of decylubiquinone."
FT /evidence="ECO:0000269|PubMed:12718520"
FT MUTAGEN 217
FT /note="K->C: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12718520"
FT MUTAGEN 217
FT /note="K->R: Shows 40% of the wild-type rate of deamino-
FT NADH oxidase."
FT /evidence="ECO:0000269|PubMed:12718520"
FT MUTAGEN 224
FT /note="H->K: Shows 40% of the wild-type rate of deamino-
FT NADH oxidase. Inhibited by 20-30% upon addition of 0.25 mM
FT of decylubiquinone."
FT /evidence="ECO:0000269|PubMed:12718520"
FT MUTAGEN 247
FT /note="K->C: Shows 7% of the wild-type rate of deamino-NADH
FT oxidase."
FT /evidence="ECO:0000269|PubMed:12718520"
FT MUTAGEN 391
FT /note="G->S: Shows 90% of the wild-type rate of deamino-
FT NADH oxidase."
FT /evidence="ECO:0000269|PubMed:12718520"
FT MUTAGEN 395
FT /note="K->C: Shows 5% of the wild-type rate of deamino-NADH
FT oxidase."
FT /evidence="ECO:0000269|PubMed:12718520"
FT MUTAGEN 395
FT /note="K->R: Shows 30% of the wild-type rate of deamino-
FT NADH oxidase."
FT /evidence="ECO:0000269|PubMed:12718520"
FT CONFLICT 123..126
FT /note="NHLA -> TIWR (in Ref. 1; CAA48373)"
FT /evidence="ECO:0000305"
FT CONFLICT 200..201
FT /note="EP -> DA (in Ref. 1; CAA48373)"
FT /evidence="ECO:0000305"
FT CONFLICT 268..277
FT /note="AIRVVLAIIA -> QVRRGAGDYR (in Ref. 1; CAA48373)"
FT /evidence="ECO:0000305"
FT HELIX 5..10
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 12..30
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 34..57
FT /evidence="ECO:0007829|PDB:7NYR"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 71..95
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 104..119
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 125..141
FT /evidence="ECO:0007829|PDB:7NYR"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 152..178
FT /evidence="ECO:0007829|PDB:7NYR"
FT TURN 186..190
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 201..215
FT /evidence="ECO:0007829|PDB:7NYR"
FT TURN 216..219
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 226..233
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 236..243
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 245..260
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 267..285
FT /evidence="ECO:0007829|PDB:7NYR"
FT TURN 286..290
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 294..313
FT /evidence="ECO:0007829|PDB:7NYR"
FT TURN 314..317
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 322..347
FT /evidence="ECO:0007829|PDB:7NYR"
FT TURN 366..368
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 370..384
FT /evidence="ECO:0007829|PDB:7NYR"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 390..404
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 408..431
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 448..469
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 472..481
FT /evidence="ECO:0007829|PDB:7NYR"
SQ SEQUENCE 485 AA; 52044 MW; A15F4875B7D19D09 CRC64;
MTITPQNLIA LLPLLIVGLT VVVVMLSIAW RRNHFLNATL SVIGLNAALV SLWFVGQAGA
MDVTPLMRVD GFAMLYTGLV LLASLATCTF AYPWLEGYND NKDEFYLLVL IAALGGILLA
NANHLASLFL GIELISLPLF GLVGYAFRQK RSLEASIKYT ILSAAASSFL LFGMALVYAQ
SGDLSFVALG KNLGDGMLNE PLLLAGFGLM IVGLGFKLSL VPFHLWTPDV YQGAPAPVST
FLATASKIAI FGVVMRLFLY APVGDSEAIR VVLAIIAFAS IIFGNLMALS QTNIKRLLGY
SSISHLGYLL VALIALQTGE MSMEAVGVYL AGYLFSSLGA FGVVSLMSSP YRGPDADSLF
SYRGLFWHRP ILAAVMTVMM LSLAGIPMTL GFIGKFYVLA VGVQAHLWWL VGAVVVGSAI
GLYYYLRVAV SLYLHAPEQP GRDAPSNWQY SAGGIVVLIS ALLVLVLGVW PQPLISIVRL
AMPLM
