ID   NDHN_GLOVI              Reviewed;         159 AA.
AC   Q7NEV8;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=gll3770;
OS   Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC   Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC   Gloeobacter.
OX   NCBI_TaxID=251221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29082 / PCC 7421;
RX   PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA   Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA   Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA   Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT   cyanobacterium that lacks thylakoids.";
RL   DNA Res. 10:137-145(2003).
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: Cell inner 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; BA000045; BAC91711.1; -; Genomic_DNA.
DR   RefSeq; NP_926716.1; NC_005125.1.
DR   RefSeq; WP_011143759.1; NC_005125.1.
DR   AlphaFoldDB; Q7NEV8; -.
DR   SMR; Q7NEV8; -.
DR   STRING; 251221.35214343; -.
DR   EnsemblBacteria; BAC91711; BAC91711; BAC91711.
DR   KEGG; gvi:gll3770; -.
DR   PATRIC; fig|251221.4.peg.3805; -.
DR   eggNOG; ENOG502ZBMI; Bacteria.
DR   HOGENOM; CLU_087432_0_0_3; -.
DR   InParanoid; Q7NEV8; -.
DR   OMA; HGIRPPH; -.
DR   OrthoDB; 1804108at2; -.
DR   PhylomeDB; Q7NEV8; -.
DR   Proteomes; UP000000557; Chromosome.
DR   GO; GO:0005886; C:plasma 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   Cell inner membrane; Cell membrane; Membrane; NAD; NADP; Plastoquinone;
KW   Quinone; Reference proteome; Translocase; Transport.
FT   CHAIN           1..159
FT                   /note="NAD(P)H-quinone oxidoreductase subunit N"
FT                   /id="PRO_0000352216"
SQ   SEQUENCE   159 AA;  17562 MW;  AE297617222AB4D3 CRC64;
     MPLLNLVLDN GSRFVADVEK HSSIALWAPP EGGIEGNYQR RLRGIGYRTQ IITAKGLGDI
     SRFLLESHGV RPAHLGKKDK RVFTLPPELA IYMDTLPASA KGFVLWIIEG KVLSLFELES
     LVGLPAAVPK LKVIVEVGSD YNIRWMPLEQ AVSKMAEGR