ID   A0A8K1PHC2_9LAMI        Unreviewed;       176 AA.
AC   A0A8K1PHC2;
DT   03-AUG-2022, integrated into UniProtKB/TrEMBL.
DT   03-AUG-2022, sequence version 1.
DT   27-NOV-2024, entry version 13.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit 6, chloroplastic {ECO:0000256|ARBA:ARBA00018131, ECO:0000256|RuleBase:RU004431};
DE            EC=7.1.1.- {ECO:0000256|RuleBase:RU004431};
GN   Name=ndhG {ECO:0000313|EMBL:UDN44237.1};
OS   Buddleja officinalis.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:UDN44237.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Scrophulariaceae; Buddlejeae; Buddleja.
OX   NCBI_TaxID=714454 {ECO:0000313|EMBL:UDN44237.1};
RN   [1] {ECO:0000313|EMBL:UDN44237.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Ding S.J., Wang S.J., Deng R.Y., Ma F.X., Zhang H.Y.;
RL   Submitted (AUG-2021) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00004059, ECO:0000256|RuleBase:RU004431}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + NADH + (n+1) H(+)(in) = a plastoquinol +
CC         NAD(+) + n H(+)(out); 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:0000256|ARBA:ARBA00001230,
CC         ECO:0000256|RuleBase:RU004431};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + NADPH + (n+1) H(+)(in) = a plastoquinol +
CC         NADP(+) + n H(+)(out); 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:0000256|ARBA:ARBA00001558,
CC         ECO:0000256|RuleBase:RU004431};
CC   -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which
CC       are encoded in the nucleus. {ECO:0000256|ARBA:ARBA00011199,
CC       ECO:0000256|RuleBase:RU004431}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000256|ARBA:ARBA00004454}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004454}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 6 family.
CC       {ECO:0000256|ARBA:ARBA00005698, ECO:0000256|RuleBase:RU004431}.
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DR   EMBL; MZ955034; UDN44237.1; -; Genomic_DNA.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   FunFam; 1.20.120.1200:FF:000002; NAD(P)H-quinone oxidoreductase subunit 6, chloroplastic; 1.
DR   Gene3D; 1.20.120.1200; NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ; 1.
DR   InterPro; IPR050290; NAD(P)H-Q_Oxidoreductase_6.
DR   InterPro; IPR001457; NADH_UbQ/plastoQ_OxRdtase_su6.
DR   InterPro; IPR042106; Nuo/plastoQ_OxRdtase_6_NuoJ.
DR   PANTHER; PTHR48391; NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT 6, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR48391:SF1; NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT 6, CHLOROPLASTIC; 1.
DR   Pfam; PF00499; Oxidored_q3; 1.
PE   3: Inferred from homology;
KW   Chloroplast {ECO:0000256|ARBA:ARBA00022528, ECO:0000256|RuleBase:RU004431};
KW   Membrane {ECO:0000256|RuleBase:RU004431};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU004431};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU004431};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000256|RuleBase:RU004431};
KW   Plastoquinone {ECO:0000256|ARBA:ARBA00022957,
KW   ECO:0000256|RuleBase:RU004431};
KW   Quinone {ECO:0000256|ARBA:ARBA00022719, ECO:0000256|RuleBase:RU004431};
KW   Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|RuleBase:RU004431};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU004431};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU004431}.
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004431"
FT   TRANSMEM        36..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004431"
FT   TRANSMEM        59..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004431"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004431"
FT   TRANSMEM        152..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004431"
SQ   SEQUENCE   176 AA;  19347 MW;  3AA2A19991CF651F CRC64;
     MDLPGPIHDF LLVFLGSGLI LGSLAVVLLP NPIYSAFSLG LVLFCISLFY ILSNSYFVAA
     AQLLIYVGAI NVLIIFAVMF MNGSEYYKDF HLWTVGDGVT SMVCTSLFIS LITTIPDTSW
     YGIIWTTKSN QILEQDLISN SQQIGIHLST DFFLPFELIS IILLVALIGA IAIARQ
//