ID   NDHN_PROM5              Reviewed;         156 AA.
AC   A2BYT7;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=P9515_17411;
OS   Prochlorococcus marinus (strain MIT 9515).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167542;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9515;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000552; ABM72948.1; -; Genomic_DNA.
DR   RefSeq; WP_011821038.1; NC_008817.1.
DR   AlphaFoldDB; A2BYT7; -.
DR   SMR; A2BYT7; -.
DR   STRING; 167542.P9515_17411; -.
DR   EnsemblBacteria; ABM72948; ABM72948; P9515_17411.
DR   KEGG; pmc:P9515_17411; -.
DR   eggNOG; ENOG5033TWM; Bacteria.
DR   HOGENOM; CLU_087432_0_0_3; -.
DR   OMA; HGIRPPH; -.
DR   OrthoDB; 1804108at2; -.
DR   Proteomes; UP000001589; 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..156
FT                   /note="NAD(P)H-quinone oxidoreductase subunit N"
FT                   /id="PRO_0000352227"
SQ   SEQUENCE   156 AA;  17639 MW;  9C59F23B7643D63B CRC64;
     MPLLLSGKKF HNDLKKNKCL AMFAPLEGGY ETRLLRRMRA KGFKTYITSA RGLGDPEVFL
     LNLHGIRPPH LGHQSIGRNG ALGEVQQVIP QASELFNEND KDKLLWLLEG QVLSQSELEN
     LIKLPTADNK LKIVVEMGGS RKLEWKSLND YVLNEF