NUON1_HYDS0
ID NUON1_HYDS0 Reviewed; 493 AA.
AC B4U8I1;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 69.
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};
GN OrderedLocusNames=HY04AAS1_0755;
OS Hydrogenobaculum sp. (strain Y04AAS1).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Hydrogenobaculum;
OC unclassified Hydrogenobaculum.
OX NCBI_TaxID=380749;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y04AAS1;
RX PubMed=19136599; DOI=10.1128/jb.01645-08;
RA Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT "Complete and draft genome sequences of six members of the Aquificales.";
RL J. Bacteriol. 191:1992-1993(2009).
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; CP001130; ACG57442.1; -; Genomic_DNA.
DR RefSeq; WP_012513798.1; NC_011126.1.
DR AlphaFoldDB; B4U8I1; -.
DR SMR; B4U8I1; -.
DR STRING; 380749.HY04AAS1_0755; -.
DR PRIDE; B4U8I1; -.
DR EnsemblBacteria; ACG57442; ACG57442; HY04AAS1_0755.
DR KEGG; hya:HY04AAS1_0755; -.
DR eggNOG; COG1007; Bacteria.
DR HOGENOM; CLU_007100_1_4_0; -.
DR OMA; HFWVPEV; -.
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 inner membrane; Cell membrane; Membrane; NAD; Quinone; Translocase;
KW Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..493
FT /note="NADH-quinone oxidoreductase subunit N 1"
FT /id="PRO_0000391167"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 82..102
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 137..157
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 412..434
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 456..476
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ SEQUENCE 493 AA; 55394 MW; 5CF58C94DB2C3582 CRC64;
MDIRLLLGST NLYEFKYLLP EITVFIGAFV LFLLDIVMKN SETKKRIFLW ISILFLALSM
LSFSFKNAFF KDVFSGTYTI DTLGMFSKIF EIVLTLMVLP FLHTYMNKKN TFYYEVYYIT
FLSLLGMMTL SSSYNLIVIY VSLEMVSISF YIMTALFRGS FISKEGAYKY LIIGGISIII
ALYGAAFMYG ASKSLDIRAI MFSYNDTNSV YLIVGMILFL LAFAIKIGII PFHFWLPDAY
TAAPTPITGF MASAGKLAFF IPLLRLVPYV NQYLYSSWMI SVSILAAITM IVGNALALVQ
SDLKRLLAYS SIAHSGYILS VLSSNSSMGL KAAIYFVFVY SIMGLGAFLV LSVLEQSDEW
NNQLSEIGGL YRNTGFLSIS FAVFIFALLG IPPTIGFVGK ALVFLGLAIK NIYWLGFVLI
LATAISTGYY VRIVVLMFMK DVEIHFKPHY DILENVSIGL LVFLTFALGM LPFVLWNGIS
NISEFLFKIA NLR
