ID   NDHN_TRIV2              Reviewed;         162 AA.
AC   Q3MFC2;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit N {ECO:0000255|HAMAP-Rule:MF_01353};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01353};
DE   AltName: Full=NAD(P)H dehydrogenase I subunit N {ECO:0000255|HAMAP-Rule:MF_01353};
DE            Short=NDH-1 subunit N {ECO:0000255|HAMAP-Rule:MF_01353};
DE            Short=NDH-N {ECO:0000255|HAMAP-Rule:MF_01353};
GN   Name=ndhN {ECO:0000255|HAMAP-Rule:MF_01353}; OrderedLocusNames=Ava_0690;
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937;
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA   Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
CC   -!- FUNCTION: NDH-1 shuttles electrons from an unknown electron donor, via
CC       FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory
CC       and/or the photosynthetic chain. The immediate electron acceptor for
CC       the enzyme in this species is believed to be plastoquinone. Couples the
CC       redox reaction to proton translocation, and thus conserves the redox
CC       energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in
CC       inorganic carbon-concentration. {ECO:0000255|HAMAP-Rule:MF_01353}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n
CC         H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA-COMP:9561,
CC         Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62192;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01353};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol + n
CC         H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-COMP:9561,
CC         Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62192;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01353};
CC   -!- SUBUNIT: NDH-1 can be composed of about 15 different subunits;
CC       different subcomplexes with different compositions have been identified
CC       which probably have different functions. {ECO:0000255|HAMAP-
CC       Rule:MF_01353}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01353}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01353}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01353}.
CC   -!- SIMILARITY: Belongs to the complex I NdhN subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01353}.
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DR   EMBL; CP000117; ABA20314.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3MFC2; -.
DR   SMR; Q3MFC2; -.
DR   STRING; 240292.Ava_0690; -.
DR   EnsemblBacteria; ABA20314; ABA20314; Ava_0690.
DR   KEGG; ava:Ava_0690; -.
DR   eggNOG; ENOG502ZBMI; Bacteria.
DR   HOGENOM; CLU_087432_0_0_3; -.
DR   OMA; HGIRPPH; -.
DR   Proteomes; UP000002533; Chromosome.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   HAMAP; MF_01353; NDH1_NDH1N; 1.
DR   InterPro; IPR020874; NAD(P)H-quinone_OxRdtase_su_N.
DR   PANTHER; PTHR35515; PTHR35515; 1.
DR   Pfam; PF11909; NdhN; 1.
PE   3: Inferred from homology;
KW   Membrane; NAD; NADP; Plastoquinone; Quinone; Thylakoid; Translocase;
KW   Transport.
FT   CHAIN           1..162
FT                   /note="NAD(P)H-quinone oxidoreductase subunit N"
FT                   /id="PRO_0000352214"
SQ   SEQUENCE   162 AA;  17706 MW;  6064A9CC7A8DCFA4 CRC64;
     MALITTGNGL IRDLEKFGSV GVYVPLEGGF EGRYRRRLRA AGYTTLQFTA RGLGDVAAYL
     TGVHGVRPPH LGKKSSGNGA AVGNVYYLPP IVGSQLEHLP PKSKGLVLWI IEGHILSDQE
     VEFLTDLPKL EPRVKVVVER GGDRTFRWKA LKDTFSASYQ AV