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Database: UniProt
Entry: E3W0P5_PRUPE
LinkDB: E3W0P5_PRUPE
Original site: E3W0P5_PRUPE 
ID   E3W0P5_PRUPE            Unreviewed;       176 AA.
AC   E3W0P5;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
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:ADO65027.1};
OS   Prunus persica (Peach) (Amygdalus persica).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:ADO65027.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=3760 {ECO:0000313|Proteomes:UP000006882};
RN   [1] {ECO:0000313|EMBL:ADO65027.1, ECO:0000313|Proteomes:UP000006882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX   PubMed=20935065; DOI=10.1093/molbev/msq261;
RA   Jansen R.K., Saski C., Lee S.B., Hansen A.K., Daniell H.;
RT   "Complete plastid genome sequences of three Rosids (Castanea, Prunus,
RT   Theobroma): evidence for at least two independent transfers of rpl22 to the
RT   nucleus.";
RL   Mol. Biol. Evol. 28:835-847(2011).
RN   [2] {ECO:0000313|EMBL:AZZ71098.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Magdy M.;
RT   "Comparative Plastogeniomic analysis in Peach.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:QQO80901.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Xin L., Fei R.;
RL   Submitted (SEP-2020) 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 + (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:0000256|ARBA:ARBA00001230,
CC         ECO:0000256|RuleBase:RU004431};
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: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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Plastid,
CC       chloroplast thylakoid membrane {ECO:0000256|ARBA:ARBA00004454}; Multi-
CC       pass membrane protein {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; HQ336405; ADO65027.1; -; Genomic_DNA.
DR   EMBL; MH169125; AZZ71098.1; -; Genomic_DNA.
DR   EMBL; MH169126; AZZ71180.1; -; Genomic_DNA.
DR   EMBL; MW042696; QQO80901.1; -; Genomic_DNA.
DR   RefSeq; YP_004021717.1; NC_014697.1.
DR   AlphaFoldDB; E3W0P5; -.
DR   STRING; 3760.E3W0P5; -.
DR   GeneID; 9978788; -.
DR   KEGG; pper:9978788; -.
DR   OrthoDB; 781518at2759; -.
DR   Proteomes; UP000006882; Chloroplast.
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   Gene3D; 1.20.120.1200; NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ; 1.
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|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   Reference proteome {ECO:0000313|Proteomes:UP000006882};
KW   Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|RuleBase:RU004431};
KW   Transmembrane {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..115
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;  19352 MW;  B6755CC2DFDCFC54 CRC64;
     MDLPGPIHDF LLVFLGSVLI LGGMGVVLFT NPIYSAFSLG LVLVCISLFY ILLNSYFVAA
     AQLLIYVGAI NVLIVFAVMF MNGSEYYKDL NLWTVGDGVT LPVCTSIFVL LMITITDTSW
     YGIIWTTRSN QIIEQDLISN SQQIGIHLST DFFLPFEFVS IILLAALIGA IAVARQ
//
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