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NU1C_JASNU
ID   NU1C_JASNU              Reviewed;         361 AA.
AC   Q06R75;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, 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}; ORFNames=JNC1315;
OS   Jasminum nudiflorum (Winter jasmine).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Oleaceae; Jasmineae; Jasminum.
OX   NCBI_TaxID=126431;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17329229; DOI=10.1093/molbev/msm036;
RA   Lee H.-L., Jansen R.K., Chumley T.W., Kim K.-J.;
RT   "Gene relocations within chloroplast genomes of Jasminum and Menodora
RT   (Oleaceae) are due to multiple, overlapping inversions.";
RL   Mol. Biol. Evol. 24:1161-1180(2007).
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; DQ673255; ABG74684.1; -; Genomic_DNA.
DR   RefSeq; YP_778546.1; NC_008407.1.
DR   AlphaFoldDB; Q06R75; -.
DR   SMR; Q06R75; -.
DR   GeneID; 4319837; -.
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..361
FT                   /note="NAD(P)H-quinone oxidoreductase subunit 1,
FT                   chloroplastic"
FT                   /id="PRO_0000275582"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        249..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        301..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        341..361
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
SQ   SEQUENCE   361 AA;  40336 MW;  B69F2CEA29632749 CRC64;
     MIIYNTTELQ AIHSFSRLEF LKEVYGSIWV LIPILTLVLG ITLGVLVIVW LEREISAGIQ
     QRIGPEYAGP LGILQALADG TKLLFKENLF PSRGDTRLFT IGPSIAVISI LLSYSVIPFG
     YRLILGDLSI GVFLWIAVSS LAPIGLLMSG YGSNNKYSFL GGLRAAAQSI SYEIPLTLCV
     LSISLLSNSF STVDIVEAQS KYGFWGWNLW RQPIGFIVFL ISSLAECERL PFDLPEAEEE
     LVAGYQTEYS GIKFGLFYVA SYLNLLVSSL FVTVLYLGGW NLSIPYLFVP ELFERGKVFE
     TIICIFITLA KTYLFLFISI ATRWTLPRLR MDQLLNLGWK FLLPISLGNL LLTTSFQLLS
     L
 
 
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