ID   NDHH_ADICA              Reviewed;         394 AA.
AC   Q85FG9;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   02-SEP-2026, entry version 84.
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   Adiantum capillus-veneris (Maidenhair fern).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Polypodiopsida; Polypodiidae; Polypodiales; Pteridineae; Pteridaceae;
OC   Vittarioideae; Adiantum.
OX   NCBI_TaxID=13818;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. H3;
RX   PubMed=12755170; DOI=10.1093/dnares/10.2.59;
RA   Wolf P.G., Rowe C.A., Sinclair R.B., Hasebe M.;
RT   "Complete nucleotide sequence of the chloroplast genome from a
RT   leptosporangiate fern, Adiantum capillus-veneris L.";
RL   DNA Res. 10:59-65(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RC   STRAIN=cv. H3; TISSUE=Frond;
RX   PubMed=15363849; DOI=10.1016/j.gene.2004.06.018;
RA   Wolf P.G., Rowe C.A., Hasebe M.;
RT   "High levels of RNA editing in a vascular plant chloroplast genome:
RT   analysis of transcripts from the fern Adiantum capillus-veneris.";
RL   Gene 339:89-97(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_01358}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + NADH + (n+1) H(+)(in) = a plastoquinol +
CC         NAD(+) + n H(+)(out); 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 + NADPH + (n+1) H(+)(in) = a plastoquinol +
CC         NADP(+) + n H(+)(out); 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   -!- RNA EDITING: Modified_positions=1 {ECO:0000269|PubMed:15363849}, 32
CC       {ECO:0000269|PubMed:15363849}, 106 {ECO:0000269|PubMed:15363849}, 361
CC       {ECO:0000269|PubMed:15363849}; Note=The initiator methionine is created
CC       by RNA editing.;
CC   -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01358}.
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DR   EMBL; AY178864; AAP29447.2; -; Genomic_DNA.
DR   RefSeq; NP_848116.2; NC_004766.1.
DR   AlphaFoldDB; Q85FG9; -.
DR   SMR; Q85FG9; -.
DR   GeneID; 807451; -.
DR   Proteomes; UP000886520; Chloroplast.
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:InterPro.
DR   GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 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   NCBIfam; NF004739; PRK06075.1; 1.
DR   NCBIfam; NF005649; PRK07415.1; 1.
DR   PANTHER; PTHR11993:SF10; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11993; NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT; 1.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR   PROSITE; PS00535; COMPLEX1_49K; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW   Reference proteome; RNA editing; Thylakoid; Translocase; Transport.
FT   CHAIN           1..394
FT                   /note="NAD(P)H-quinone oxidoreductase subunit H,
FT                   chloroplastic"
FT                   /id="PRO_0000118596"
SQ   SEQUENCE   394 AA;  45441 MW;  969A1E70A511DE1E CRC64;
     MSIRLEDIDP VVVSMGPHHP SMHGVLRLVV ALQGENVVDC ELILGYLHRG MEKIAENRTT
     SQYLPYVTRW DYLATMFTEA VTVNAPEKLA NIQIPERASY IRVIMLELSR IASHLLWLGP
     FLADIGAQTP FFYIFREREM IYDLFEAATG MRMMHNYFRI GGVAADLPYG WIDKCLDFCQ
     YCLPKIYEYE RLVTKNPIFL KRVQGVGFIN RQEAINWGLS GPSLRASGVQ WDLRKIDHYE
     CYDKLDWQIQ WQGEGDSLAR YLVRIDEMKE SINILRQALK LLPGGPYENL EGRRLVQKKD
     KIDWNGFNYQ FVGKKSSPTL KLPKQEHYVR VEAPKGELGI FLIGDDSVFP WRLKIRPPGF
     INLQIVPQLI RGMKLADIVT ILGSIDIIMG EVDR
//