ID   A0A290D3U0_9ASPA        Unreviewed;       365 AA.
AC   A0A290D3U0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   13-FEB-2019, entry version 7.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic {ECO:0000256|HAMAP-Rule:MF_01350};
DE            EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01350};
DE   AltName: Full=NAD(P)H dehydrogenase subunit 1 {ECO:0000256|HAMAP-Rule:MF_01350};
DE            Short=NDH subunit 1 {ECO:0000256|HAMAP-Rule:MF_01350};
DE   AltName: Full=NADH-plastoquinone oxidoreductase subunit 1 {ECO:0000256|HAMAP-Rule:MF_01350};
GN   Name=ndhA {ECO:0000256|HAMAP-Rule:MF_01350,
GN   ECO:0000313|EMBL:ATB18613.1};
OS   Polygonatum stenophyllum.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:ATB18613.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Asparagales; Asparagaceae;
OC   Nolinoideae; Polygonatum.
OX   NCBI_TaxID=261425 {ECO:0000313|EMBL:ATB18613.1};
RN   [1] {ECO:0000313|EMBL:ATB18613.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Park H., Kim C., Kim J.-H.;
RT   "The comparative plastid genome analysis and its phylogenetic
RT   implication on Asparagaceae s.l.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via
CC       FMN and iron-sulfur (Fe-S) centers, to quinones in the
CC       photosynthetic chain and possibly in a chloroplast respiratory
CC       chain. The immediate electron acceptor for the enzyme in this
CC       species is believed to be plastoquinone. Couples the redox
CC       reaction to proton translocation, and thus conserves the redox
CC       energy in a proton gradient. {ECO:0000256|HAMAP-Rule:MF_01350}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol
CC         + n H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA-
CC         COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17757, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:62192; Evidence={ECO:0000256|HAMAP-Rule:MF_01350,
CC         ECO:0000256|RuleBase:RU000474};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol
CC         + n H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-
CC         COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17757, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:62192; Evidence={ECO:0000256|HAMAP-Rule:MF_01350,
CC         ECO:0000256|RuleBase:RU000474};
CC   -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of
CC       which are encoded in the nucleus. {ECO:0000256|HAMAP-
CC       Rule:MF_01350, ECO:0000256|RuleBase:RU000474}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000256|RuleBase:RU000471}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU000471}. Plastid, chloroplast thylakoid
CC       membrane {ECO:0000256|HAMAP-Rule:MF_01350,
CC       ECO:0000256|RuleBase:RU000474}; Multi-pass membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_01350, ECO:0000256|RuleBase:RU000474}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01350, ECO:0000256|RuleBase:RU000474}.
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DR   EMBL; KX822773; ATB18613.1; -; Genomic_DNA.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 {ECO:0000256|RuleBase:RU000474,
KW   ECO:0000313|EMBL:ATB18613.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01350,
KW   ECO:0000256|RuleBase:RU000474};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01350, ECO:0000256|RuleBase:RU000474};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_01350, ECO:0000256|RuleBase:RU000474};
KW   Plastid {ECO:0000256|RuleBase:RU000474, ECO:0000313|EMBL:ATB18613.1};
KW   Plastoquinone {ECO:0000256|HAMAP-Rule:MF_01350,
KW   ECO:0000256|RuleBase:RU000474};
KW   Quinone {ECO:0000256|HAMAP-Rule:MF_01350,
KW   ECO:0000256|RuleBase:RU000474};
KW   Thylakoid {ECO:0000256|HAMAP-Rule:MF_01350,
KW   ECO:0000256|RuleBase:RU000474};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_01350,
KW   ECO:0000256|RuleBase:RU000474};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01350,
KW   ECO:0000256|RuleBase:RU000474};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01350,
KW   ECO:0000256|RuleBase:RU000474}.
FT   TRANSMEM     28     52       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01350, ECO:0000256|RuleBase:RU000474}.
FT   TRANSMEM     97    118       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01350, ECO:0000256|RuleBase:RU000474}.
FT   TRANSMEM    124    149       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01350, ECO:0000256|RuleBase:RU000474}.
FT   TRANSMEM    256    281       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01350, ECO:0000256|RuleBase:RU000474}.
FT   TRANSMEM    301    326       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01350, ECO:0000256|RuleBase:RU000474}.
FT   TRANSMEM    338    356       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01350, ECO:0000256|RuleBase:RU000474}.
SQ   SEQUENCE   365 AA;  40418 MW;  F0A7B954FE2415EB CRC64;
     MIIDTTEVEV QAINSFSRLE SLKEVYELIW IFVPIFTLLL GIIIGVLVIV WLEREISAAI
     QQRIGPEYAG PLGILQALAD GTKLLFKEDL LPSRGDIRLF SVGPSIAVIS VLLSYLVIPF
     GYRLILADLS IGVFLWISIS SIAPIGLLMS GYGSNNKYSF LGGLRAAAQS ISYEIPLTLC
     VLSISLLSNS LSTVDIVEAQ SKYGFLGWNL WRQPIGFVVF LISSLAECER LPFDLPEAEE
     ELVAGYQTEY SGIKYALFYL ASYLNLLVSS LFITVLYLGG WNLSIPYISI PELFGINQMD
     GVFGTTIGIF ITLAKAYLFL FIPIAARWTL PRMRMDQLLN LGWKFLLPIS LGNLLLTTSS
     QLVSL
//