ID   NUON_ERYLH              Reviewed;         487 AA.
AC   Q2NA79;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   29-APR-2015, entry version 70.
DE   RecName: Full=NADH-quinone oxidoreductase subunit N {ECO:0000255|HAMAP-Rule:MF_00445};
DE            EC=1.6.99.5 {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};
GN   OrderedLocusNames=ELI_06600;
OS   Erythrobacter litoralis (strain HTCC2594).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter.
OX   NCBI_TaxID=314225;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2594;
RX   PubMed=19168610; DOI=10.1128/JB.00026-09;
RA   Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.;
RT   "Complete genome sequence of Erythrobacter litoralis HTCC2594.";
RL   J. Bacteriol. 191:2419-2420(2009).
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-
CC       sulfur (Fe-S) centers, to quinones in the respiratory chain. The
CC       immediate electron acceptor for the enzyme in this species is
CC       believed to be ubiquinone. Couples the redox reaction to proton
CC       translocation (for every two electrons transferred, four hydrogen
CC       ions are translocated across the cytoplasmic membrane), and thus
CC       conserves the redox energy in a proton gradient.
CC       {ECO:0000255|HAMAP-Rule:MF_00445}.
CC   -!- CATALYTIC ACTIVITY: NADH + quinone = NAD(+) + quinol.
CC       {ECO:0000255|HAMAP-Rule:MF_00445}.
CC   -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits
CC       NuoA, H, J, K, L, M, N constitute the membrane sector of the
CC       complex. {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; CP000157; ABC63412.1; -; Genomic_DNA.
DR   RefSeq; WP_011414248.1; NC_007722.1.
DR   RefSeq; YP_458209.1; NC_007722.1.
DR   STRING; 314225.ELI_06600; -.
DR   EnsemblBacteria; ABC63412; ABC63412; ELI_06600.
DR   KEGG; eli:ELI_06600; -.
DR   PATRIC; 21859772; VBIEryLit102657_1312.
DR   eggNOG; COG1007; -.
DR   HOGENOM; HOG000100795; -.
DR   KO; K00343; -.
DR   OMA; YALILMT; -.
DR   OrthoDB; EOG64JFNZ; -.
DR   BioCyc; ELIT314225:GHLE-1350-MONOMER; -.
DR   Proteomes; UP000008808; 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   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
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; Oxidored_q1; 1.
DR   TIGRFAMs; TIGR01770; NDH_I_N; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Complete proteome; Membrane; NAD;
KW   Oxidoreductase; Quinone; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Ubiquinone.
FT   CHAIN         1    487       NADH-quinone oxidoreductase subunit N.
FT                                /FTId=PRO_0000391144.
FT   TRANSMEM      7     27       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00445}.
FT   TRANSMEM     37     57       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00445}.
FT   TRANSMEM     81    101       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00445}.
FT   TRANSMEM    112    132       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00445}.
FT   TRANSMEM    166    186       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00445}.
FT   TRANSMEM    207    227       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00445}.
FT   TRANSMEM    237    257       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00445}.
FT   TRANSMEM    276    296       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00445}.
FT   TRANSMEM    307    327       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00445}.
FT   TRANSMEM    329    349       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00445}.
FT   TRANSMEM    373    393       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00445}.
FT   TRANSMEM    407    427       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00445}.
FT   TRANSMEM    452    472       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00445}.
SQ   SEQUENCE   487 AA;  50816 MW;  960143C306A107D5 CRC64;
     MELNASLTLI LPEIVMAISA MALILITAYV GDKTARLVSI LAAATLGAAA VMVAPALTSG
     ASGPDTVAFG GQFLADSFAS FAKILIYLSA IGCLMIAPAF FDRLKAMRPE YPVLVLLATL
     GMSIMVSAGD LITLYIGLEL NSLAAYVLAS FLRNDTRSAE AGLKYFVLGA LASGILLYGM
     SLVYGFTGTT DFEGVRGALT GDMSTGALFG VIFVLAGLAF KIAAVPFHMW TPDVYEGAPT
     PVTTFFATAP KVAAVALTAR VALSPFGEQT EAWQQIVIFA ALASIVLGAL GAIGQTNLKR
     LLAYSSINNV GFILIGLAAS TVAGLSAMLT YLAIYVVMAL GSFVALLMLK DEDGTPLETF
     DDIAGLSTTR PALAWCLLFL MFSLAGIPPL LGFWGKFVVF QAAVQADMVL LAALGIAASV
     IGAFYYIKFV KVMFFDDAVD RVKGTSDTAH WVLLILAAVV VSPLGYLLTG WLGGLTDSAA
     SALFIAS
//