NUON_BUCBP
ID NUON_BUCBP Reviewed; 494 AA.
AC Q89AT4;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=bbp_155;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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 13 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; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the complex I subunit 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_00445}.
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DR EMBL; AE016826; AAO26889.1; -; Genomic_DNA.
DR RefSeq; WP_011091290.1; NC_004545.1.
DR AlphaFoldDB; Q89AT4; -.
DR SMR; Q89AT4; -.
DR STRING; 224915.bbp_155; -.
DR EnsemblBacteria; AAO26889; AAO26889; bbp_155.
DR GeneID; 56470699; -.
DR KEGG; bab:bbp_155; -.
DR eggNOG; COG1007; Bacteria.
DR HOGENOM; CLU_007100_1_5_6; -.
DR OMA; FYIRVIV; -.
DR OrthoDB; 1664448at2; -.
DR Proteomes; UP000000601; 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.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; NAD; Quinone; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..494
FT /note="NADH-quinone oxidoreductase subunit N"
FT /id="PRO_0000117692"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 273..295
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 332..352
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 414..434
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ SEQUENCE 494 AA; 56016 MW; F21CCAF5DC7B45C0 CRC64;
MIITGQQLVA LSPLLILMSI AIVVMLFIAY NRNRYIVFLL TSFGFLSVFI SLFIVKKIVP
IHATTLFHID KYSLLYIGIV IISSFLACIF SHYCSLTNYL YNFEEFYLLL LFCTIGCVSI
IISNNLCTFF IGSELISLSS IGLISYTFFE KKALEASIKY MVLSGIMSTL LLFGIALIYS
VSGSLEFSSI IYELTMITKS FHNAIILFFG VSLFIIACSF KLSLFPFHIW TPDVYQGMSS
EALMIFSTSV KIAIFSVLFK IFIVLSYFHI EEVFYYLVSI ISCLSMIFGN IMAINQTSIK
RLMGYSSISQ LGYLFIVLVI SRNMQFSLEV TGIYLINYAL SNIGMFGIMS VLSSLYKNFN
VDSIFSYRSL FWSSPILSGV MTVVMLSLSG IPMTVGFLGK FYLMSLVVKE HMWLFICLFI
ISTIIGFCAY LKIISCLFVA PSDSYCHKNI IISSQNINNK FLIGLLTTIS IFVLFLGIFP
QITIHLVKYF WIQW
