ID   F6KAF1_9STRA            Unreviewed;       497 AA.
AC   F6KAF1;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   03-OCT-2012, entry version 5.
DE   RecName: Full=NADH-quinone oxidoreductase subunit N;
DE            EC=1.6.99.5;
DE   AltName: Full=NADH dehydrogenase I subunit N;
DE   AltName: Full=NDH-1 subunit N;
GN   Name=nad2; Synonyms=nuoN;
OS   Phytophthora mirabilis.
OG   Mitochondrion.
OC   Eukaryota; stramenopiles; Oomycetes; Peronosporales; Phytophthora.
OX   NCBI_TaxID=129356;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PIC99114;
RA   Lassiter E.S., Russ C., Nusbaum C., Zeng Q., Hu C.-H., Thorne J.L.,
RA   Ristaino J.B.;
RT   "Mitochondrial genome sequences and evolution of the Phytophthora Ic
RT   clade.";
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: NADH + quinone = NAD(+) + quinol.
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 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the complex I subunit 2 family.
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DR   EMBL; HM590421; ADK76339.1; -; Genomic_DNA.
DR   RefSeq; YP_004563944.1; NC_015606.1.
DR   GeneID; 10743629; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
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; NADH_UbQ/plastoQ_OxRdtase.
DR   Pfam; PF00361; Oxidored_q1; 1.
DR   TIGRFAMs; TIGR01770; NDH_I_N; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Mitochondrion; NAD; Oxidoreductase; Quinone;
KW   Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT   TRANSMEM     13     33       Helical; (By similarity).
FT   TRANSMEM     43     63       Helical; (By similarity).
FT   TRANSMEM     78     98       Helical; (By similarity).
FT   TRANSMEM    112    132       Helical; (By similarity).
FT   TRANSMEM    137    157       Helical; (By similarity).
FT   TRANSMEM    172    192       Helical; (By similarity).
FT   TRANSMEM    216    236       Helical; (By similarity).
FT   TRANSMEM    258    278       Helical; (By similarity).
FT   TRANSMEM    285    305       Helical; (By similarity).
FT   TRANSMEM    314    334       Helical; (By similarity).
FT   TRANSMEM    338    358       Helical; (By similarity).
FT   TRANSMEM    385    405       Helical; (By similarity).
FT   TRANSMEM    422    442       Helical; (By similarity).
FT   TRANSMEM    465    485       Helical; (By similarity).
SQ   SEQUENCE   497 AA;  57074 MW;  5BE74E7B49408D83 CRC64;
     MIFQEIFNNN FEIIIPEFFL TTILLILLLF GVFYKKNQNM QKILIIKNIT TIIIYLLLIL
     LILTLNITNI SNNILNGVLI INNFTQFIKV ILILSTIVCF LIQQKYLIQQ KINAYEINIL
     MLISLLGLML LVSTNHLITL YLAIELQSLS FYILTSTQKK SILSIEAGLK YFILGSIASG
     FILFGSSIIY AITGSLNFNN IFLILSNINF LENINILISL SYGLIFILVG ILFKVGASPF
     HFWLPDVYEG APNNISSFFA IVPKIAFIGI LIRLFFEIFF NISYFFEIFF YIISFLSMLI
     GALSALQQKK IKRLLAYSSI SHVGFILIGF TSNMLNNIPF ILLYVLIYII TSINLWTSYL
     SLNINHKPIK YLTDLSNIHT INKLIAIIII INIFSLAGIP PLAGFFSKLF IFFSAIKNNY
     FSLVFFGILI SVLSSFYYLK IIKIIYFEKI LRKMYISKIN KMQSIVLIIN TQFILFLFIS
     PNIILVNLNK VYLYLLI
//