ID   NU1C_PLAOC              Reviewed;         363 AA.
AC   Q09FZ1;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01350};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01350};
DE   AltName: Full=NAD(P)H dehydrogenase subunit 1 {ECO:0000255|HAMAP-Rule:MF_01350};
DE            Short=NDH subunit 1 {ECO:0000255|HAMAP-Rule:MF_01350};
DE   AltName: Full=NADH-plastoquinone oxidoreductase subunit 1 {ECO:0000255|HAMAP-Rule:MF_01350};
GN   Name=ndhA {ECO:0000255|HAMAP-Rule:MF_01350};
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_01350}.
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_01350};
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_01350};
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_01350}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_01350}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01350}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01350}.
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DR   EMBL; DQ923116; ABI49834.1; -; Genomic_DNA.
DR   RefSeq; YP_740620.1; NC_008335.1.
DR   AlphaFoldDB; Q09FZ1; -.
DR   SMR; Q09FZ1; -.
DR   GeneID; 4271359; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   HAMAP; MF_01350; NDH1_NuoH; 1.
DR   InterPro; IPR001694; NADH_UbQ_OxRdtase_su1/FPO.
DR   InterPro; IPR018086; NADH_UbQ_OxRdtase_su1_CS.
DR   PANTHER; PTHR11432; PTHR11432; 1.
DR   Pfam; PF00146; NADHdh; 1.
DR   PROSITE; PS00667; COMPLEX1_ND1_1; 1.
DR   PROSITE; PS00668; COMPLEX1_ND1_2; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW   Thylakoid; Translocase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..363
FT                   /note="NAD(P)H-quinone oxidoreductase subunit 1,
FT                   chloroplastic"
FT                   /id="PRO_0000298879"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        127..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        248..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        300..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        336..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
SQ   SEQUENCE   363 AA;  40052 MW;  70F495E45A63C09E CRC64;
     MIIDTTEVQA INSFSRSESL KEAYGLIWLL VPIFTPVSGI TIGVLVIVWL EREISAGIQQ
     RIGPEYAGPL GILQALADGT KLLFKEDLLP SRGDTRLFSI GPSIAIISIL LSYSVIPFGY
     RLVLADLSIG VFLWIAISSI APIGLLMSGY GSNNKYSFSG GLRAAAQSIS YEIPLTLCVL
     SISLLSNSLS TVDIVEAQSK YGFWGWNLWR QPIGFAVFLI SSLAECERLP FDLPEAEEEL
     VAGYQTEYSG IKFGLFYVAS YLNLLVSSLF VTVLYLGGWN LSIPYIFIPE LFEINKVSGV
     FGTTIGIFIT LAKAYLFLFI SITTRWTLPR MRMDQLLNLG WKFLLPISLG NLLLTTSSQL
     FSL