ID   NU4LC_PAUCH             Reviewed;         103 AA.
AC   B1X495;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit 4L, organellar chromatophore {ECO:0000255|HAMAP-Rule:MF_01456};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01456};
DE   AltName: Full=NAD(P)H dehydrogenase subunit 4L {ECO:0000255|HAMAP-Rule:MF_01456};
DE   AltName: Full=NADH-plastoquinone oxidoreductase subunit 4L {ECO:0000255|HAMAP-Rule:MF_01456};
GN   Name=ndhE {ECO:0000255|HAMAP-Rule:MF_01456}; OrderedLocusNames=PCC_0323;
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 shuttles electrons from NAD(P)H:plastoquinone, via FMN
CC       and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain
CC       and possibly in a chloroplast respiratory chain. The immediate electron
CC       acceptor for the enzyme in this species is believed to be
CC       plastoquinone. Couples the redox reaction to proton translocation, and
CC       thus conserves the redox energy in a proton gradient.
CC       {ECO:0000255|HAMAP-Rule:MF_01456}.
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_01456};
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_01456};
CC   -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which
CC       are encoded in the nucleus. {ECO:0000255|HAMAP-Rule:MF_01456}.
CC   -!- SUBCELLULAR LOCATION: Plastid, organellar chromatophore thylakoid
CC       membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01456}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 4L family.
CC       {ECO:0000255|HAMAP-Rule:MF_01456}.
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DR   EMBL; CP000815; ACB42764.1; -; Genomic_DNA.
DR   RefSeq; YP_002048974.1; NC_011087.1.
DR   AlphaFoldDB; B1X495; -.
DR   SMR; B1X495; -.
DR   GeneID; 6481773; -.
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:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR   GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   HAMAP; MF_01456; NDH1_NuoK; 1.
DR   InterPro; IPR001133; NADH_UbQ_OxRdtase_chain4L/K.
DR   InterPro; IPR039428; NUOK/Mnh_C1-like.
DR   PANTHER; PTHR11434; PTHR11434; 1.
DR   Pfam; PF00420; Oxidored_q2; 1.
PE   3: Inferred from homology;
KW   Membrane; NAD; NADP; Organellar chromatophore; Plastid; Plastoquinone;
KW   Quinone; Thylakoid; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..103
FT                   /note="NAD(P)H-quinone oxidoreductase subunit 4L,
FT                   organellar chromatophore"
FT                   /id="PRO_0000360372"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
SQ   SEQUENCE   103 AA;  11540 MW;  07D9B9EBF4C87FAE CRC64;
     MTIMLEAYLT LAAVLFCIGV WGLINSRNAV RVLMSIELML NAVNINLMAF SNYLDGELIR
     GQVFAIFVIT VAAAEAAVGL AILLSLYRNR QTVDMERFNL LRW