NU1C_ARAHI
ID NU1C_ARAHI Reviewed; 365 AA.
AC A4QK75;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 42.
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 Arabis hirsuta (Hairy rock-cress) (Turritis hirsuta).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX NCBI_TaxID=78191;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JO23;
RA Hosouchi T., Tsuruoka H., Kotani H.;
RT "Sequencing analysis of Arabis hirsuta chloroplast DNA.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; AP009369; BAF50080.1; -; Genomic_DNA.
DR RefSeq; YP_001123255.1; NC_009268.1.
DR AlphaFoldDB; A4QK75; -.
DR SMR; A4QK75; -.
DR GeneID; 4962577; -.
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..365
FT /note="NAD(P)H-quinone oxidoreductase subunit 1,
FT chloroplastic"
FT /id="PRO_0000298865"
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 129..149
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 203..223
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
SQ SEQUENCE 365 AA; 40683 MW; A031A3C56179FA97 CRC64;
MIIYATEVET INSFVRLESL KELYSLVWIF VPIFSLVLGI ITGVLVIAWI ERELSAGIQQ
RIGPEYAGPL GILQALADGT KLLFKEDLRP SRGNTPLFSI GPSIAVISIL LSYSVIPFSN
HLVLADLNIG IFLWIAISSI APIGLLMSGY GSNNKYSFLG GLRAAAQSIS YEIPLTLCVL
SISLLSNSLS TVDIVEAQSK YGFWGWNLWR QPIGFIIFLI SSLAECERLP FDLPEAEEEL
IAGYQTEYSG IKFGLFYVAS YINLLISSLF VTILYLGGWN ISIPYISIPY ISILELFERD
PIFGTTIGIF ITLAKTYLFL FISIATRWTL PRLRMDQLLN LGWKFLLPIS LGNLLLTTSF
QLFSL
