NUON_METI4
ID NUON_METI4 Reviewed; 474 AA.
AC B3DZT0;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 70.
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};
GN Name=nuoN {ECO:0000255|HAMAP-Rule:MF_00445}; OrderedLocusNames=Minf_2211;
OS Methylacidiphilum infernorum (isolate V4) (Methylokorus infernorum (strain
OS V4)).
OC Bacteria; Verrucomicrobia; Methylacidiphilae; Methylacidiphilales;
OC Methylacidiphilaceae; Methylacidiphilum.
OX NCBI_TaxID=481448;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate V4;
RX PubMed=18593465; DOI=10.1186/1745-6150-3-26;
RA Hou S., Makarova K.S., Saw J.H., Senin P., Ly B.V., Zhou Z., Ren Y.,
RA Wang J., Galperin M.Y., Omelchenko M.V., Wolf Y.I., Yutin N., Koonin E.V.,
RA Stott M.B., Mountain B.W., Crowe M.A., Smirnova A.V., Dunfield P.F.,
RA Feng L., Wang L., Alam M.;
RT "Complete genome sequence of the extremely acidophilic methanotroph isolate
RT V4, Methylacidiphilum infernorum, a representative of the bacterial phylum
RT Verrucomicrobia.";
RL Biol. Direct 3:26-26(2008).
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. {ECO:0000255|HAMAP-Rule:MF_00445}.
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 14 different subunits. Subunits NuoA, H,
CC J, K, L, M, N constitute the membrane sector of the complex.
CC {ECO:0000255|HAMAP-Rule:MF_00445}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00445}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00445}.
CC -!- SIMILARITY: Belongs to the complex I subunit 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_00445}.
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DR EMBL; CP000975; ACD84265.1; -; Genomic_DNA.
DR RefSeq; WP_012464545.1; NC_010794.1.
DR AlphaFoldDB; B3DZT0; -.
DR SMR; B3DZT0; -.
DR STRING; 481448.Minf_2211; -.
DR EnsemblBacteria; ACD84265; ACD84265; Minf_2211.
DR KEGG; min:Minf_2211; -.
DR eggNOG; COG1007; Bacteria.
DR HOGENOM; CLU_007100_1_3_0; -.
DR OMA; FYIRVIV; -.
DR OrthoDB; 1664448at2; -.
DR Proteomes; UP000009149; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; NAD; Quinone; Translocase;
KW Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..474
FT /note="NADH-quinone oxidoreductase subunit N"
FT /id="PRO_0000391177"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 103..120
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 296..313
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 366..388
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ SEQUENCE 474 AA; 51980 MW; 02CFD6F670F1D0E9 CRC64;
MNAFFVFCTP ECFLSLSALV LLLWQALAKI HDKSIGILVL ADYLVAGVLL LPFVENQGIF
WNGLYVWDKM AVLWKVFFLI TGFLVSYLSL ESDRLIPKAR SEFYILPLFT TAGMALLASV
RDFILLFVGL EIVTVSFYVF VAFQREFPSA LEAGVKYLII GALASSFLVM GIAFVFGITG
STQFDEVARF AQNNPVNGPL ILGLVFILVG LGFKASAVPF HVWTPDVYQG ASTPITTYLA
VGSKAAGFVV LLRILNLPFY DPGFQKHWIP LISLMALLSV IVGNLAAIPQ RNIKRMLGYS
SISHGGFLLM GLSAHNKIGC AAVIYYFFAY MVAIFAAFLV VILLEKNQPS GVSIKDFNGL
YLKNSLMAWS MAFSMISLAG LPPLMGFFGK LMVFFAAWDS GQHLLVIVGA LCAAAGLYYY
IGVVRAMFWT EPDNVQRIDL SPATKLLLWI LSVGSILLGF YAEPVIKLVG SVLS
