ID   NDHH_PLAOC              Reviewed;         393 AA.
AC   Q09FZ0;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 62.
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   Platanus occidentalis (Sycamore) (American plane tree).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Proteales; Platanaceae; Platanus.
OX   NCBI_TaxID=4403;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16934154; DOI=10.1186/1471-2229-6-17;
RA   Moore M.J., Dhingra A., Soltis P.S., Shaw R., Farmerie W.G., Folta K.M.,
RA   Soltis D.E.;
RT   "Rapid and accurate pyrosequencing of angiosperm plastid genomes.";
RL   BMC Plant Biol. 6:17-17(2006).
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; DQ923116; ABI49835.1; -; Genomic_DNA.
DR   RefSeq; YP_740621.1; NC_008335.1.
DR   AlphaFoldDB; Q09FZ0; -.
DR   SMR; Q09FZ0; -.
DR   GeneID; 4271360; -.
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_0000358022"
SQ   SEQUENCE   393 AA;  45363 MW;  733D6A900659F143 CRC64;
     MTVPATRKDL MIVNMGPHHP SMHGVLRLIV TLDGEDVIDC EPVLGYLHRG MEKIAENRTI
     IQYLPYVTRW DYLATMFTEA ITVNAPEQLG NIQVPKRASY IRAIMLELSR IASHLLWLGP
     FMADIGAQTP FFYIFREREL IYDLFEAATG MRMMHNYFRI GGVAADLPHG WIDKCLDFCD
     YFLTGIAEYQ KLITRNPIFL ERVEGVGIIG GEEAINWGLS GPMLRASGIQ WDLRKVDHYG
     CYDEFDWEVQ WQKEGDSLAR YLVRISEMTE SVKIIQQALE GIPGGPYENL EVRRFDRARD
     SEWNDFEYRF ISKKPSPTFE LSKQELYVRV EAPKGELGIF LIGDQSVFPW RWKIRPPGFI
     NLQILPQLVK RMKLADIMTI LGSIDIIMGE VDR