ID   NDHH_AMBTC              Reviewed;         393 AA.
AC   Q70XV8;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 82.
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   Amborella trichopoda.
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX   NCBI_TaxID=13333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12832641; DOI=10.1093/molbev/msg159;
RA   Goremykin V.V., Hirsch-Ernst K.I., Wolfl S., Hellwig F.H.;
RT   "Analysis of the Amborella trichopoda chloroplast genome sequence suggests
RT   that Amborella is not a basal angiosperm.";
RL   Mol. Biol. Evol. 20:1499-1505(2003).
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; AJ506156; CAD45162.1; -; Genomic_DNA.
DR   RefSeq; NP_904155.1; NC_005086.1.
DR   AlphaFoldDB; Q70XV8; -.
DR   SMR; Q70XV8; -.
DR   STRING; 13333.ERN04788; -.
DR   GeneID; 2546617; -.
DR   KEGG; atr:2546617; -.
DR   eggNOG; KOG2870; Eukaryota.
DR   eggNOG; KOG4770; Eukaryota.
DR   OrthoDB; 444312at2759; -.
DR   Proteomes; UP000017836; Chloroplast.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:GO_Central.
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   Reference proteome; Thylakoid; Translocase; Transport.
FT   CHAIN           1..393
FT                   /note="NAD(P)H-quinone oxidoreductase subunit H,
FT                   chloroplastic"
FT                   /id="PRO_0000357963"
SQ   SEQUENCE   393 AA;  45638 MW;  983ADFA7E8A092D7 CRC64;
     MTVPATRNDL MIVNMGPHHP SMHGVLRLIV TLDGEDVIDC EPILGYLHRG MEKIAENRTI
     IQYLPYVTRW DYLATMFTEA ITVNAPEELG NIQVPRRASY IRVIMLELSR IASHLLWLGP
     FMADIGAQTP FFYIFREREL LYDLFETATG MRMMHNFFRI GGVAADLPHG WIDKCLDFCD
     YFLPEVAEYQ KLITRNPIFL ERVEGVGFIA EEEAINWGLS GPMLRASGIP WDLRKVDHYE
     CYDEFDWEVQ WQKEGDSLAR YLVRISEMIE SVKIIQQALE GIPGGPYENL EARRFDRVRN
     IEWNDFEYRF ISKKPSPTFE LSKQELYVRV EAPKGELGIF LIGDNSVFPW RWKIRPPGLI
     NLQILPQLVK RMKLADIMTI LGSIDIIMGE VDR