ID   NDHH_DRIGR              Reviewed;         393 AA.
AC   Q06GU0;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-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   Drimys granadensis.
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Magnoliidae; Canellales; Winteraceae; Drimys.
OX   NCBI_TaxID=224735;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17020608; DOI=10.1186/1471-2148-6-77;
RA   Cai Z., Penaflor C., Kuehl J.V., Leebens-Mack J., Carlson J.E.,
RA   dePamphilis C.W., Boore J.L., Jansen R.K.;
RT   "Complete plastid genome sequences of Drimys, Liriodendron, and Piper:
RT   implications for the phylogenetic relationships of magnoliids.";
RL   BMC Evol. Biol. 6:77-77(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; DQ887676; ABH88354.1; -; Genomic_DNA.
DR   RefSeq; YP_784443.1; NC_008456.1.
DR   AlphaFoldDB; Q06GU0; -.
DR   SMR; Q06GU0; -.
DR   PRIDE; Q06GU0; -.
DR   GeneID; 4363564; -.
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_0000357987"
SQ   SEQUENCE   393 AA;  45487 MW;  F3E0D9127A69AF48 CRC64;
     MTVPATKKDL MIINMGPHHP SMHGVLRLIV TLDGEDVIDC EPILGYLHRG MEKIAENRTI
     IQYLPYVTRW DYLATMFTEA ITVNAPEQLG NIQVPKRASY IRVIMLELSR IASHLLWLGP
     FMADIGAQTP FFYIFREREL LYDLFEAATG MRMMHNYFRI GGVAADLPHG WIDKCLDFCD
     YSLTGVVEYQ KLITRNPIFL ERVEEVGIIG GEEAINWGLS GPMLRASGIQ WDLRKVDHYE
     CYDEFDWEVQ WQKEGDSLAR YLVRISEMTE SIKILQQALE GIPGGPYENL EVRRFDRAKD
     SEWNDFEYRF ISKKPSPTFE LLKQELYVRV EAPKGELGIF LIGDNSVFPW RWKIRPPGFI
     NLQILPQLVK RMKLADIMTI LGSIDIIMGE VDR