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NUON_BUCCC
ID   NUON_BUCCC              Reviewed;         481 AA.
AC   Q057W3;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=BCc_109;
OS   Buchnera aphidicola subsp. Cinara cedri (strain Cc).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=372461;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cc;
RX   PubMed=17038625; DOI=10.1126/science.1130441;
RA   Perez-Brocal V., Gil R., Ramos S., Lamelas A., Postigo M., Michelena J.M.,
RA   Silva F.J., Moya A., Latorre A.;
RT   "A small microbial genome: the end of a long symbiotic relationship?";
RL   Science 314:312-313(2006).
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 {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}.
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DR   EMBL; CP000263; ABJ90586.1; -; Genomic_DNA.
DR   RefSeq; WP_011672505.1; NC_008513.1.
DR   AlphaFoldDB; Q057W3; -.
DR   SMR; Q057W3; -.
DR   STRING; 372461.BCc_109; -.
DR   EnsemblBacteria; ABJ90586; ABJ90586; BCc_109.
DR   KEGG; bcc:BCc_109; -.
DR   eggNOG; COG1007; Bacteria.
DR   HOGENOM; CLU_007100_1_5_6; -.
DR   OMA; FYIRVIV; -.
DR   OrthoDB; 1664448at2; -.
DR   Proteomes; UP000000669; 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..481
FT                   /note="NADH-quinone oxidoreductase subunit N"
FT                   /id="PRO_0000391116"
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        76..96
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        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        306..326
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        367..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        415..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        461..481
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ   SEQUENCE   481 AA;  56465 MW;  EAB13DA22C32F0A2 CRC64;
     MIRLFNDIIP IFPILMLIFS IIILFFILNN KNKVKSGCIV TTISIFFSII YILYIKRFFF
     NYSSDLIRID QYSFYFMILL LISSFFTCIF SYSWLLLEDN YSIEFYFFVL LSTIGGMLII
     ISNHFLSLFL GIELLFLPIL GILNFFSNSR KNLFSIVNYM ILSVFSSALL LLGVSFIYFV
     SGRLSFSFFP LIFMYYPSII LNSMMIFGIC MILLSLFFKL SLFPLHTWSP NIYQYSNPCS
     LIFFSTAVKI SIFSFLLRFL NFFPYIYKIK SIYYIIYLIS MFSVFFGNII GIIQNNVQRL
     IGYLSISNIG FLLIIIITQS YSFVFLNKLF IIYLFIYIFG LIGFFSIKSI IDINFIERKN
     NLLKENSLIG LFWYNPILGI LMSIILLSLS GFPITLGFWG KFFIFKHLIQ KKFFITTLLI
     MLSNIVGMQN YLYIIRSLYI KPIKFSNTSL VNNLYISILQ KFLLISIGFL FVILGFFPYI
     F
 
 
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