ID   NDHL_TRIEI              Reviewed;          78 AA.
AC   Q10W93;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=Tery_4495;
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Trichodesmium.
OX   NCBI_TaxID=203124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMS101;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Richardson P.;
RT   "Complete sequence of Trichodesmium erythraeum IMS101.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP000393; ABG53481.1; -; Genomic_DNA.
DR   RefSeq; WP_011613803.1; NC_008312.1.
DR   AlphaFoldDB; Q10W93; -.
DR   SMR; Q10W93; -.
DR   STRING; 203124.Tery_4495; -.
DR   EnsemblBacteria; ABG53481; ABG53481; Tery_4495.
DR   KEGG; ter:Tery_4495; -.
DR   eggNOG; ENOG5032ZM4; Bacteria.
DR   HOGENOM; CLU_171077_0_0_3; -.
DR   OMA; YWMNNRW; -.
DR   OrthoDB; 2075884at2; -.
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; Thylakoid; Translocase;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..78
FT                   /note="NAD(P)H-quinone oxidoreductase subunit L"
FT                   /id="PRO_5000127100"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01355"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01355"
SQ   SEQUENCE   78 AA;  9209 MW;  D29C44B1F957A56B CRC64;
     MNLDLDTNLI ILIIYAALAG AYFLVMPAIV YAYLKTRWYV VSSIERVFMY FLMFLFFPGM
     LVLSPFLNFR PRKQQIES