NU1C_ATRBE
ID NU1C_ATRBE Reviewed; 363 AA.
AC Q8S8U5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 61.
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 Atropa belladonna (Belladonna) (Deadly nightshade).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Hyoscyameae; Atropa.
OX NCBI_TaxID=33113;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Ab5p(kan);
RX PubMed=12200487; DOI=10.1093/oxfordjournals.molbev.a004222;
RA Schmitz-Linneweber C., Regel R., Du T.G., Hupfer H., Herrmann R.G.,
RA Maier R.M.;
RT "The plastid chromosome of Atropa belladonna and its comparison with that
RT of Nicotiana tabacum: the role of RNA editing in generating divergence in
RT the process of plant speciation.";
RL Mol. Biol. Evol. 19:1602-1612(2002).
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; AJ316582; CAC88101.1; -; Genomic_DNA.
DR RefSeq; NP_783287.1; NC_004561.1.
DR AlphaFoldDB; Q8S8U5; -.
DR SMR; Q8S8U5; -.
DR GeneID; 806482; -.
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_0000117507"
FT TRANSMEM 30..50
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 165..185
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 269..289
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; 39949 MW; 586C623C9A3779B5 CRC64;
MIIDTTEIET INSFSKLESL KEVYGIIWML VPILTLVLGI TIGVLVIVWL EREISAGIQQ
RIGPEYAGPL GILQALADGT KLLFKENLIP STGDPRLFSI GPSIAVISIF LSYSVIPFGD
HLVLADLSIG VFLWIAISSV APVGLLMSGY GSNNKYSFLG GLRAAAQSIS YEIPLALCVL
SISLLSNSSS TVDIVEAQSK YGFLGWNLWR QPIGFIVFLI SSLAECERLP FDLPEAEEEL
VAGYQTEYSG IKFGLFYIAS YLNLLVSSLF VTVLYLGGWN LSIPYIFVPE LFGINKRGKV
FGTLIGIFIT LAKTYLFLFI PIATRWTLPR LRMDQLLNLG WKFLLPISLG NLLLTTSSQL
LSL
