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NDHJ_NYMAL
ID   NDHJ_NYMAL              Reviewed;         158 AA.
AC   Q6EW45;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 68.
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   Nymphaea alba (White water-lily) (Castalia alba).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Nymphaeales; Nymphaeaceae; Nymphaea.
OX   NCBI_TaxID=34301;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15084683; DOI=10.1093/molbev/msh147;
RA   Goremykin V.V., Hirsch-Ernst K.I., Woelfl S., Hellwig F.H.;
RT   "The chloroplast genome of Nymphaea alba: whole-genome analyses and the
RT   problem of identifying the most basal angiosperm.";
RL   Mol. Biol. Evol. 21:1445-1454(2004).
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; AJ627251; CAF28596.1; -; Genomic_DNA.
DR   RefSeq; YP_053158.1; NC_006050.1.
DR   AlphaFoldDB; Q6EW45; -.
DR   SMR; Q6EW45; -.
DR   GeneID; 2896170; -.
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   Thylakoid; Translocase; Transport.
FT   CHAIN           1..158
FT                   /note="NAD(P)H-quinone oxidoreductase subunit J,
FT                   chloroplastic"
FT                   /id="PRO_0000358288"
SQ   SEQUENCE   158 AA;  18625 MW;  304DDAC7D71D8673 CRC64;
     MQGRSSAWLV KHELVHRSLG FDYQGVETLQ IKPEDWYSIA VISYVYGYNY LRSQCAYDVA
     PGGLLASVYH LTRIQYGVDQ PEEVCIKVFV PRSNPRIPSV FWIWKSADFQ ERESYDMLGI
     SYDNHPRMKR ILMPESWIGW PLRKDYIAPN FYELQDAY
 
 
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