NUON_GEOSW
ID NUON_GEOSW Reviewed; 492 AA.
AC C5D978;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 64.
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=GWCH70_3291;
OS Geobacillus sp. (strain WCH70).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC unclassified Geobacillus.
OX NCBI_TaxID=471223;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCH70;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Brumm P., Mead D.A., Richardson P.;
RT "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
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 a
CC menaquinone. 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 membrane {ECO:0000255|HAMAP-Rule:MF_00445};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-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; CP001638; ACS25931.1; -; Genomic_DNA.
DR RefSeq; WP_015865298.1; NC_012793.1.
DR AlphaFoldDB; C5D978; -.
DR SMR; C5D978; -.
DR STRING; 471223.GWCH70_3291; -.
DR EnsemblBacteria; ACS25931; ACS25931; GWCH70_3291.
DR KEGG; gwc:GWCH70_3291; -.
DR eggNOG; COG1007; Bacteria.
DR HOGENOM; CLU_007100_1_1_9; -.
DR OMA; FYIRVIV; -.
DR OrthoDB; 1664448at2; -.
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 membrane; Membrane; NAD; Quinone; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..492
FT /note="NADH-quinone oxidoreductase subunit N"
FT /id="PRO_0000391151"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 318..340
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 344..366
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ SEQUENCE 492 AA; 53709 MW; 748DBE4A76A0EDE5 CRC64;
MSMHTLLQYK WEMMTPEFIV LGTALILSLM DLFMPDDKDR RPLAWIAFVG VAIALIATIG
LIPAKAVSIL NDTFRLDAFG KAFKLLLLAG GALSLLLAFD YRPKEGLKDR GEFYYLLLCA
LLGAMIMASS GDLITLFVGL ELLSISSYIL AGIRKTSMQA NESAMKYVIN GGISTAITLF
GMSYIFGLTG TTNIKEIALE VQKLTDSGYQ YILAIAFLMM LVGLSFKISS VPFHMWTPDV
YQGAPTPVTA FLSVVSKTAG FVIVLRLFIT IFTQAPAQGK DPSSLLFSMQ DYIAFLAGAT
MIIGNTIALK QRSMKRLFAY SSIAHAGYIL VGFAAMSWVM IDSIWFYLLA YLFMNLGAFA
ILQRISDEAD SDDLSHFAGL YQRNPLLAVA MGIFLLSLAG IPGTAGFIGK LNIFLGALMT
EPGHYVLAAV MIATTVVSYV YYFGIFVQIF FRPADETTSL RMPIGLAMVV VLCALGTLLF
GVVPGLAYHF LE
