ID   NDHH_ATRBE              Reviewed;         393 AA.
AC   Q8S8U4;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit H, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01358};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01358};
DE   AltName: Full=NAD(P)H dehydrogenase subunit H;
DE   AltName: Full=NADH-plastoquinone oxidoreductase 49 kDa subunit {ECO:0000255|HAMAP-Rule:MF_01358};
DE   AltName: Full=NADH-plastoquinone oxidoreductase subunit H {ECO:0000255|HAMAP-Rule:MF_01358};
GN   Name=ndhH {ECO:0000255|HAMAP-Rule:MF_01358};
OS   Atropa belladonna (Belladonna) (Deadly nightshade).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Hyoscyameae; Atropa.
OX   NCBI_TaxID=33113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Ab5p(kan);
RX   PubMed=12200487; DOI=10.1093/oxfordjournals.molbev.a004222;
RA   Schmitz-Linneweber C., Regel R., Du T.G., Hupfer H., Herrmann R.G.,
RA   Maier R.M.;
RT   "The plastid chromosome of Atropa belladonna and its comparison with that
RT   of Nicotiana tabacum: the role of RNA editing in generating divergence in
RT   the process of plant speciation.";
RL   Mol. Biol. Evol. 19:1602-1612(2002).
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_01358}.
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_01358};
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_01358};
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_01358}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_01358}; Peripheral membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01358}; Stromal side {ECO:0000255|HAMAP-
CC       Rule:MF_01358}.
CC   -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01358}.
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DR   EMBL; AJ316582; CAC88102.1; -; Genomic_DNA.
DR   RefSeq; NP_783288.1; NC_004561.1.
DR   AlphaFoldDB; Q8S8U4; -.
DR   SMR; Q8S8U4; -.
DR   GeneID; 806557; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.645.10; -; 1.
DR   HAMAP; MF_01358; NDH1_NuoD; 1.
DR   InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR   InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR   InterPro; IPR022885; NDH1_su_D/H.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   PANTHER; PTHR11993; PTHR11993; 1.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   SUPFAM; SSF56762; SSF56762; 1.
DR   PROSITE; PS00535; COMPLEX1_49K; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW   Thylakoid; Translocase; Transport.
FT   CHAIN           1..393
FT                   /note="NAD(P)H-quinone oxidoreductase subunit H,
FT                   chloroplastic"
FT                   /id="PRO_0000357966"
SQ   SEQUENCE   393 AA;  45532 MW;  FABD7F3C8BCB2EBD CRC64;
     MTTPTTRKDL MIVNMGPQHP SMHGVLRLIV TLDGEDVVDC EPILGYLHRG MEKIAENRTI
     IQYLPYVTRW DYLATMFTEA ITINGPEQLG NIQVPKRASY IRVIMLELSR IASHLLWLGP
     FMADIGAQTP FFYIFREREL IYDLFEAATG MRMMHNYFRI GGVAADLPYG WIDKCLDFCD
     YFLTGIAEYQ KLITRNPIFL ERVEGVGIIG GDEALNWGLS GPMLRASGIE WDLRKVDHYE
     SYDEFDWQVQ WQREGDSLAR YLVRIGEMTE SIKIIQQALE GIPGGPYENL EIRRFDRLKD
     PEWNDFEYRF ISKKPSPTFE LSKQELYVRV EAPKGELGIF LIGDQSVFPW RWKIRPPGFI
     NLQILPQLVK RMKLADIMTI LGSIDIIMGE VDR