NUON_PAESJ
ID NUON_PAESJ Reviewed; 521 AA.
AC C6D5D2;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 63.
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=Pjdr2_5803;
OS Paenibacillus sp. (strain JDR-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=324057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JDR-2;
RX PubMed=22675593; DOI=10.4056/sigs.2374349;
RA Chow V., Nong G., St John F.J., Rice J.D., Dickstein E., Chertkov O.,
RA Bruce D., Detter C., Brettin T., Han J., Woyke T., Pitluck S., Nolan M.,
RA Pati A., Martin J., Copeland A., Land M.L., Goodwin L., Jones J.B.,
RA Ingram L.O., Shanmugam K.T., Preston J.F.;
RT "Complete genome sequence of Paenibacillus sp. strain JDR-2.";
RL Stand. Genomic Sci. 6:1-10(2012).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001656; ACT04409.1; -; Genomic_DNA.
DR RefSeq; WP_015847345.1; NC_012914.1.
DR AlphaFoldDB; C6D5D2; -.
DR SMR; C6D5D2; -.
DR STRING; 324057.Pjdr2_5803; -.
DR EnsemblBacteria; ACT04409; ACT04409; Pjdr2_5803.
DR KEGG; pjd:Pjdr2_5803; -.
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..521
FT /note="NADH-quinone oxidoreductase subunit N"
FT /id="PRO_0000391196"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 43..63
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 128..148
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ SEQUENCE 521 AA; 55623 MW; 21847365DA66E14B CRC64;
MTEFVPLTWH DTLYLAPELI LAAMFLILIV TDLILPGRTN RAIIGWLSLA GLLLSLAAVI
WRMIDMNPSG VSAAEAAEAG KAISLLGASY RVDDYGNLLK IIFLIGTSLV VLLGLGSTQK
DDAVTDKAEF YYLLLPAAAG AMIMASSGNL VTLYIGLELL SITTYVLVGL RKRSSLSAEA
AFKYVVTGGI ASAFVLFGMS YLYGVTGSVS LADFPTALPQ AFTDYKALVY VGFFFLIAGF
GIKIAAAPFH IWAADVYQGA PTPVSAFLAV IAKGAALAAV FRFLYSSAFF LTGGPGKQAG
DDVFFALLVI AAAAMIAGTV SALRQKQVKR LLALSGVANA GYLLVPIAIS VTIIHSNNFS
EFVFYLVAYL LMNVGAFAVV TVIARAAGHE ELKGFSGLYY RAPWTAAAML IFILSFSGLP
VTAGFFGKLF ILLGAASVKA YWLVAIMVVS TVISYYFYFG IIRQMFMRSN GEEEDRIHVP
AVTGTVIWIC AAATVALGVL PGPLMKWIDA VFTIQADLFV R
