ID   NU6C_AMBTC              Reviewed;         177 AA.
AC   Q70XW1;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit 6, chloroplastic;
DE            EC=7.1.1.-;
DE   AltName: Full=NAD(P)H dehydrogenase subunit 6;
DE   AltName: Full=NADH-plastoquinone oxidoreductase subunit 6;
GN   Name=ndhG;
OS   Amborella trichopoda.
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX   NCBI_TaxID=13333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12832641; DOI=10.1093/molbev/msg159;
RA   Goremykin V.V., Hirsch-Ernst K.I., Wolfl S., Hellwig F.H.;
RT   "Analysis of the Amborella trichopoda chloroplast genome sequence suggests
RT   that Amborella is not a basal angiosperm.";
RL   Mol. Biol. Evol. 20:1499-1505(2003).
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 (By similarity).
CC       {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 is composed of at least 16 different subunits, 5 of which
CC       are encoded in the nucleus. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 6 family. {ECO:0000305}.
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DR   EMBL; AJ506156; CAD45159.1; -; Genomic_DNA.
DR   RefSeq; NP_904152.1; NC_005086.1.
DR   AlphaFoldDB; Q70XW1; -.
DR   SMR; Q70XW1; -.
DR   GeneID; 2546489; -.
DR   KEGG; atr:2546489; -.
DR   OrthoDB; 1388741at2759; -.
DR   Proteomes; UP000017836; Chloroplast.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:GO_Central.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.1200; -; 1.
DR   InterPro; IPR001457; NADH_UbQ/plastoQ_OxRdtase_su6.
DR   InterPro; IPR042106; Nuo/plastoQ_OxRdtase_6_NuoJ.
DR   Pfam; PF00499; Oxidored_q3; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW   Reference proteome; Thylakoid; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..177
FT                   /note="NAD(P)H-quinone oxidoreductase subunit 6,
FT                   chloroplastic"
FT                   /id="PRO_0000360226"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   177 AA;  19255 MW;  66386F4D4EF57A78 CRC64;
     MDLLGPIHDI LLVSLGSGII LGSLGVVLLT NPIYSAFSSG LVLVRISLFH ILSNSYFVAA
     AQLLIYVGAI NVLIIFAVMF MNGSEYYNNF HLWTVGDGIS SVVCTSILFS LIATILDTSW
     YGIIWTTRSN QIIEQDLTSN VQQIGIHLST DFFLPFELIS IILLVALVGA IAMARAE