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NU6C_HUPLU
ID   NU6C_HUPLU              Reviewed;         199 AA.
AC   Q5SCZ0;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 51.
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   Huperzia lucidula (Shining clubmoss) (Lycopodium lucidulum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Lycopodiales; Lycopodiaceae; Huperzioideae; Huperzia.
OX   NCBI_TaxID=37429;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15788152; DOI=10.1016/j.gene.2005.01.018;
RA   Wolf P.G., Karol K.G., Mandoli D.F., Kuehl J.V., Arumuganathan K.,
RA   Ellis M.W., Mishler B.D., Kelch D.G., Olmstead R.G., Boore J.L.;
RT   "The first complete chloroplast genome sequence of a lycophyte, Huperzia
RT   lucidula (Lycopodiaceae).";
RL   Gene 350:117-128(2005).
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; AY660566; AAT80760.1; -; Genomic_DNA.
DR   RefSeq; YP_209564.2; NC_006861.1.
DR   AlphaFoldDB; Q5SCZ0; -.
DR   SMR; Q5SCZ0; -.
DR   GeneID; 3283711; -.
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; IEA:InterPro.
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   Thylakoid; Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..199
FT                   /note="NAD(P)H-quinone oxidoreductase subunit 6,
FT                   chloroplastic"
FT                   /id="PRO_0000360258"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   199 AA;  21976 MW;  B06DD19BCB3934BD CRC64;
     MSVIDLPEFF YKAILLLIES GVILGSLGVV LFTNIVYSAF LLGWVPVCIS FLYILLNADF
     VAAVQILIYV GTINVLIVFA VMLINKPQYF RFLKYWTVGD GTALALCTSP FLSIIAAILS
     TPWSKISLIV LSNKIVEEPL TDNVQRIGFH SLTDSPLPFE LLSIILLVAP VGAITMARRE
     EAVEAEESEA LKTKDDFPF
 
 
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