ID   NDHL_PROM4              Reviewed;          84 AA.
AC   P0C8E5;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit L;
DE            EC=7.1.1.-;
DE   AltName: Full=NAD(P)H dehydrogenase I subunit L;
DE   AltName: Full=NDH-1 subunit L;
DE   AltName: Full=NDH-L;
GN   Name=ndhL; OrderedLocusNames=P9211_05731.1;
OS   Prochlorococcus marinus (strain MIT 9211).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=93059;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9211;
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 (By similarity). {ECO:0000250}.
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   -!- 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   -!- 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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000250}; Multi-
CC       pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the complex I NdhL subunit family.
CC       {ECO:0000305}.
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DR   EMBL; CP000878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P0C8E5; -.
DR   SMR; P0C8E5; -.
DR   Proteomes; UP000000788; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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_01355; NDH1_NDH1L; 1.
DR   InterPro; IPR019654; NADH-quinone_OxRdatse_su_L.
DR   Pfam; PF10716; NdhL; 1.
PE   3: Inferred from homology;
KW   Membrane; NAD; NADP; Plastoquinone; Quinone; Reference proteome; Thylakoid;
KW   Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..84
FT                   /note="NAD(P)H-quinone oxidoreductase subunit L"
FT                   /id="PRO_0000353673"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   84 AA;  10079 MW;  B7939B9B8E05C629 CRC64;
     MASQFASNSL LVLGAYGIIG FLYLVVIPLF LYFWMNIRWN FMNKFERLCL YGLVFLFFPW
     FDFICSFFKP KNSWARRDLA IDSH