ID   NU6C_ANGEV              Reviewed;         197 AA.
AC   A2T386;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 39.
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   Angiopteris evecta (Mule's foot fern) (Polypodium evectum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Polypodiopsida; Marattiidae; Marattiales; Marattiaceae; Angiopteris.
OX   NCBI_TaxID=13825;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Roper J.M., Hansen S.K., Wolf P.G., Karol K.G., Mandoli D.F.,
RA   Everett K.D.E., Kuehl J., Boore J.L.;
RT   "The complete plastid genome sequence of Angiopteris evecta (G. Forst.)
RT   Hoffm. (Marattiaceae).";
RL   Am. Fern J. 97:95-106(2007).
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; DQ821119; ABG79653.1; -; Genomic_DNA.
DR   RefSeq; YP_001023754.1; NC_008829.1.
DR   AlphaFoldDB; A2T386; -.
DR   SMR; A2T386; -.
DR   GeneID; 4788129; -.
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..197
FT                   /note="NAD(P)H-quinone oxidoreductase subunit 6,
FT                   chloroplastic"
FT                   /id="PRO_0000360227"
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        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   197 AA;  21525 MW;  CA1B27C52B25F9C7 CRC64;
     MILPEPIHKV ILVIIELGIL LGSLGVVLLT NIVYSALLLG LVFICISLLY LVLNADFVAA
     AQVLIYVGAV NVLTVFAVML IDKPKNITLF SFSNVGDNIT LGVCTSLFIL LTIMIPDASW
     SEIYMTKQST KFVEQGLTTD VQLIGSQLLT KFLLPFELLS ILLLVALIGA ITIARQERIV
     EIDDNKASES KEDLSLF