NUON1_AQUAE
ID NUON1_AQUAE Reviewed; 464 AA.
AC O67342;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=NADH-quinone oxidoreductase subunit N 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00445};
DE AltName: Full=NDH-1 subunit N 1 {ECO:0000255|HAMAP-Rule:MF_00445};
GN Name=nuoN1 {ECO:0000255|HAMAP-Rule:MF_00445}; OrderedLocusNames=aq_1322;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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; AE000657; AAC07305.1; -; Genomic_DNA.
DR PIR; C70414; C70414.
DR RefSeq; NP_213906.1; NC_000918.1.
DR RefSeq; WP_010880844.1; NC_000918.1.
DR AlphaFoldDB; O67342; -.
DR SMR; O67342; -.
DR STRING; 224324.aq_1322; -.
DR EnsemblBacteria; AAC07305; AAC07305; aq_1322.
DR KEGG; aae:aq_1322; -.
DR PATRIC; fig|224324.8.peg.1030; -.
DR eggNOG; COG1007; Bacteria.
DR HOGENOM; CLU_007100_1_4_0; -.
DR InParanoid; O67342; -.
DR OMA; FYIRVIV; -.
DR OrthoDB; 1664448at2; -.
DR Proteomes; UP000000798; 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;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport; Ubiquinone.
FT CHAIN 1..464
FT /note="NADH-quinone oxidoreductase subunit N 1"
FT /id="PRO_0000391098"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ SEQUENCE 464 AA; 51286 MW; 5C72D12A83E8FF26 CRC64;
MNWNAILPEA ILAIGILTVF ILELFLERKH YKFLSVLAFI FVVLSGYSIF FVNYPAKLFF
DGFSVDALNL IGKLFILAVT GFVLLSSYDY FSKKNSQYGE LPYLYLIATL GLMVMISSDN
LAIIFTGLEL ASITMYILVG LFRREYLSKE GAFKYLVIGT TGTSMYALGS ALVYASSGSM
VLSPVKEENT LFALGVILII SALALKVSAV PFHFWTPDAY EGAPTPTTAY LSTVPKIGMY
FLFVKLTMYL FSAFPDWKYV VMLLAVLSMF YGNIVAYAQK SVKRLLAYSS IAHAGYFLTA
LTAVDKHLFS ALLFYVFVYA LATVGAFTVL AILEKKEGWT HHFLDFKGLK EENPVLASML
ALFLFALIGI PPAAVFLGKL GIFFGLVKTD MFALGILFAI ASLISAGYYL KVIVYMFLYS
GEVRHGQTTV SAGEAFTVLG TAFLVIFFGL FPHVVLDFIL RALS
