NUON1_THEYD
ID NUON1_THEYD Reviewed; 458 AA.
AC B5YKJ2;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=THEYE_A0921;
OS Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC Bacteria; Nitrospirae; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX NCBI_TaxID=289376;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51303 / DSM 11347 / YP87;
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT ATCC 51303 / DSM 11347 / YP87.";
RL Submitted (AUG-2008) 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
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; CP001147; ACI21104.1; -; Genomic_DNA.
DR RefSeq; WP_012545829.1; NC_011296.1.
DR RefSeq; YP_002248757.1; NC_011296.1.
DR AlphaFoldDB; B5YKJ2; -.
DR SMR; B5YKJ2; -.
DR STRING; 289376.THEYE_A0921; -.
DR PRIDE; B5YKJ2; -.
DR EnsemblBacteria; ACI21104; ACI21104; THEYE_A0921.
DR KEGG; tye:THEYE_A0921; -.
DR PATRIC; fig|289376.4.peg.907; -.
DR eggNOG; COG1007; Bacteria.
DR HOGENOM; CLU_007100_1_3_0; -.
DR InParanoid; B5YKJ2; -.
DR OMA; NAWAPDA; -.
DR OrthoDB; 1664448at2; -.
DR Proteomes; UP000000718; 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..458
FT /note="NADH-quinone oxidoreductase subunit N 1"
FT /id="PRO_0000391239"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 37..57
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 101..121
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ SEQUENCE 458 AA; 51071 MW; 6CBE2444B1772129 CRC64;
MNISQIPLQV EALIPEITLT GFASLILLAG LLKLKNEVLV WSSVLFLVIF AFFIPSFEGE
AFNGMFLNDF LTIYLKLIII IGTIISLLVL TSYLKEKLIR FNESIAFILF SALGMMLLVS
ARELISFFLS FELMSLSIYV LVGIRRYDVK SNEAAVKYFM LGGFSSAIML FGIAFIYGAT
NTTELSLILK VISNYNPLIL IGLGLFIVGL CFKIALVPFH MWAPDVYEGA PTPVTAFIST
LPKVAILGAF GRVLVEIFRD YYIDWSNFLI VLSIATMATG NFFALIQKNI KRMLAYSSIA
HAGYIIIGVI VGTQSGFNSV VAYMFIYTLM NIGAFAMVIA FNEESIENYK GLHKFHPALA
IAMLIFMFSL TGVPPTAGFI VKFNIFLQAV KAGFTWLVVI AVIFTVISAY YYLRIVMYMY
MKEPVKLPEP IYSRELEVAI LICTIGVTFL GILPLFLI
