ID   NDHL_PROMM              Reviewed;          83 AA.
AC   Q7V897;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 2.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit L {ECO:0000255|HAMAP-Rule:MF_01355};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01355};
DE   AltName: Full=NAD(P)H dehydrogenase I subunit L {ECO:0000255|HAMAP-Rule:MF_01355};
DE   AltName: Full=NDH-1 subunit L;
DE   AltName: Full=NDH-L;
GN   Name=ndhL {ECO:0000255|HAMAP-Rule:MF_01355}; OrderedLocusNames=PMT_0467;
OS   Prochlorococcus marinus (strain MIT 9313).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9313;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(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_01355}.
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_01355};
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_01355};
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_01355}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01355}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01355}.
CC   -!- SIMILARITY: Belongs to the complex I NdhL subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01355}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAE20642.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX548175; CAE20642.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041384930.1; NC_005071.1.
DR   AlphaFoldDB; Q7V897; -.
DR   SMR; Q7V897; -.
DR   STRING; 74547.PMT_0467; -.
DR   EnsemblBacteria; CAE20642; CAE20642; PMT_0467.
DR   KEGG; pmt:PMT_0467; -.
DR   eggNOG; ENOG5030RAT; Bacteria.
DR   HOGENOM; CLU_171077_1_0_3; -.
DR   OrthoDB; 2075884at2; -.
DR   Proteomes; UP000001423; 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..83
FT                   /note="NAD(P)H-quinone oxidoreductase subunit L"
FT                   /id="PRO_0000353678"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01355"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01355"
SQ   SEQUENCE   83 AA;  9397 MW;  A40A4CCB6B98ED7A CRC64;
     MFLQAVTSPI SINSLMVLAA YALLGGLYLI VVPLLLYSWM NRRWHCMGKF ERLSAYGLVF
     LFFPGLILFA PFLNLRLNGQ GEV