ID   NDHJ_SOLTU              Reviewed;         158 AA.
AC   Q2VEH4;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit J, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01357};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01357};
DE   AltName: Full=NAD(P)H dehydrogenase subunit J;
DE   AltName: Full=NADH-plastoquinone oxidoreductase subunit J {ECO:0000255|HAMAP-Rule:MF_01357};
GN   Name=ndhJ {ECO:0000255|HAMAP-Rule:MF_01357};
OS   Solanum tuberosum (Potato).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Desiree;
RX   PubMed=16835751; DOI=10.1007/s00299-006-0196-4;
RA   Chung H.-J., Jung J.D., Park H.-W., Kim J.-H., Cha H.W., Min S.R.,
RA   Jeong W.-J., Liu J.R.;
RT   "The complete chloroplast genome sequences of Solanum tuberosum and
RT   comparative analysis with Solanaceae species identified the presence of a
RT   241-bp deletion in cultivated potato chloroplast DNA sequence.";
RL   Plant Cell Rep. 25:1369-1379(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Desiree;
RA   Gargano D., Scotti N., Vezzi A., Bilardi A., Valle G., Grillo S., Cardi T.;
RT   "Complete chloroplast genome sequences of Solanum tuberosum cultivar
RT   Desiree and comparative analyses with other Solanaceae genomes.";
RL   Submitted (FEB-2006) 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:0000255|HAMAP-Rule:MF_01357}.
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:0000255|HAMAP-Rule:MF_01357};
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:0000255|HAMAP-Rule:MF_01357};
CC   -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which
CC       are encoded in the nucleus. {ECO:0000255|HAMAP-Rule:MF_01357}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_01357}; Peripheral membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01357}; Stromal side {ECO:0000255|HAMAP-
CC       Rule:MF_01357}.
CC   -!- SIMILARITY: Belongs to the complex I 30 kDa subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01357}.
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DR   EMBL; DQ231562; ABB90044.1; -; Genomic_DNA.
DR   EMBL; DQ386163; ABD47060.1; -; Genomic_DNA.
DR   RefSeq; YP_635642.1; NC_008096.2.
DR   AlphaFoldDB; Q2VEH4; -.
DR   SMR; Q2VEH4; -.
DR   STRING; 4113.PGSC0003DMT400006828; -.
DR   GeneID; 4099977; -.
DR   KEGG; sot:4099977; -.
DR   eggNOG; KOG1713; Eukaryota.
DR   InParanoid; Q2VEH4; -.
DR   OrthoDB; 1276923at2759; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.460.80; -; 1.
DR   HAMAP; MF_01357; NDH1_NuoC; 1.
DR   InterPro; IPR010218; NADH_DH_suC.
DR   InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like.
DR   InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su.
DR   InterPro; IPR020396; NADH_UbQ_OxRdtase_CS.
DR   Pfam; PF00329; Complex1_30kDa; 1.
DR   SUPFAM; SSF143243; SSF143243; 1.
DR   PROSITE; PS00542; COMPLEX1_30K; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW   Reference proteome; Thylakoid; Translocase; Transport.
FT   CHAIN           1..158
FT                   /note="NAD(P)H-quinone oxidoreductase subunit J,
FT                   chloroplastic"
FT                   /id="PRO_0000277563"
SQ   SEQUENCE   158 AA;  18667 MW;  74B399D31C639FE3 CRC64;
     MQGRLSAWLV KHGLIHRSLG FDYQGIETLQ IKPEDWHSIA VIFYVYGYNY LRSQCAYDVA
     PGGLLASVYH LTRIEDDVDQ PEELCIKVFA SRRNPRIPSV FWVWKSVDFQ ERESYDMLGI
     SYDNHPRLKR ILMPESWIGW PLRKDYIAPN FYEIQDAH