NDHL_PAUCH
ID NDHL_PAUCH Reviewed; 83 AA.
AC B1X3F0;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit L, organellar chromatophore {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=PCC_0007;
OS Paulinella chromatophora.
OG Plastid; Organellar chromatophore.
OC Eukaryota; Sar; Rhizaria; Imbricatea; Silicofilosea; Euglyphida;
OC Paulinellidae; Paulinella.
OX NCBI_TaxID=39717;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18356055; DOI=10.1016/j.cub.2008.02.051;
RA Nowack E.C.M., Melkonian M., Gloeckner G.;
RT "Chromatophore genome sequence of Paulinella sheds light on acquisition of
RT photosynthesis by eukaryotes.";
RL Curr. Biol. 18:410-418(2008).
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 (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 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: Plastid, organellar chromatophore thylakoid
CC membrane {ECO:0000250}; 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; CP000815; ACB42469.1; -; Genomic_DNA.
DR RefSeq; YP_002048679.1; NC_011087.1.
DR AlphaFoldDB; B1X3F0; -.
DR SMR; B1X3F0; -.
DR GeneID; 6481625; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0070118; C:organellar chromatophore thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
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; Organellar chromatophore; Plastid; Plastoquinone;
KW Quinone; Thylakoid; Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..83
FT /note="NAD(P)H-quinone oxidoreductase subunit L, organellar
FT chromatophore"
FT /id="PRO_0000353695"
FT TRANSMEM 17..37
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; 9791 MW; 581844B8ECF33918 CRC64;
MSFFRYLSDI SSETRTLLLA YGVLGGLYLI LVPLALYWWM NRRWYIMGKI ERLFVYGLVF
LFFPGLILLS PFLNMRLKGQ GET
