ID   NU1C_HORVU              Reviewed;         362 AA.
AC   P92432; A1E9P5; O20233;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 4.
DT   02-SEP-2026, entry version 92.
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   Hordeum vulgare (Barley).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND RNA EDITING.
RC   STRAIN=cv. Hassan; TISSUE=Leaf;
RX   PubMed=10666448; DOI=10.1093/nar/28.5.1092;
RA   del Campo E.M., Sabater B., Martin M.;
RT   "Transcripts of the ndhH-D operon of barley plastids: possible role of
RT   unedited site III in splicing of the ndhA intron.";
RL   Nucleic Acids Res. 28:1092-1098(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Morex;
RX   PubMed=17534593; DOI=10.1007/s00122-007-0567-4;
RA   Saski C., Lee S.-B., Fjellheim S., Guda C., Jansen R.K., Luo H.,
RA   Tomkins J., Rognli O.A., Daniell H., Clarke J.L.;
RT   "Complete chloroplast genome sequences of Hordeum vulgare, Sorghum bicolor
RT   and Agrostis stolonifera, and comparative analyses with other grass
RT   genomes.";
RL   Theor. Appl. Genet. 115:571-590(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 + NADH + (n+1) H(+)(in) = a plastoquinol +
CC         NAD(+) + n H(+)(out); 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 + NADPH + (n+1) H(+)(in) = a plastoquinol +
CC         NADP(+) + n H(+)(out); 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   -!- RNA EDITING: Modified_positions=17 {ECO:0000269|PubMed:10666448}, 158
CC       {ECO:0000269|PubMed:10666448}, 188 {ECO:0000269|PubMed:10666448}, 357
CC       {ECO:0000269|PubMed:10666448};
CC   -!- SIMILARITY: Belongs to the complex I subunit 1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01350}.
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DR   EMBL; AJ011848; CAA09812.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; EF115541; ABK79467.1; ALT_SEQ; Genomic_DNA.
DR   PDB; 7EU3; EM; 3.70 A; A=15-360.
DR   PDB; 7F9O; EM; 4.50 A; G=15-360.
DR   AlphaFoldDB; P92432; -.
DR   EMDB; EMD-31307; -.
DR   EMDB; EMD-31498; -.
DR   SMR; P92432; -.
DR   KEGG; hvg:4525172; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003954; F:NADH dehydrogenase activity; IEA:TreeGrafter.
DR   GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0009060; P:aerobic respiration; IEA:TreeGrafter.
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   NCBIfam; NF004741; PRK06076.1-2; 1.
DR   PANTHER; PTHR11432; NADH DEHYDROGENASE SUBUNIT 1; 1.
DR   PANTHER; PTHR11432:SF3; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 1; 1.
DR   Pfam; PF00146; NADHdh; 1.
DR   PROSITE; PS00667; COMPLEX1_ND1_1; 1.
DR   PROSITE; PS00668; COMPLEX1_ND1_2; 1.
DR   PDBsum; 7EU3; -.
DR   PDBsum; 7F9O; -.
PE   1: Evidence at protein level;
KW   3D-structure; Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone;
KW   Quinone; RNA editing; Thylakoid; Translocase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..362
FT                   /note="NAD(P)H-quinone oxidoreductase subunit 1,
FT                   chloroplastic"
FT                   /id="PRO_0000240021"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        103..123
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        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        247..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        342..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
SQ   SEQUENCE   362 AA;  40373 MW;  4DBEE96146BF6154 CRC64;
     MIIDRVEVET INSFSKLELL KEVYGLISIL PILTLLLGIT IEVLVIVWLE REISASIQQR
     IGPEYAGPLG LLQAIADGTK LLFKEDILPS RGDISLFSIG PSIAVISVLL SFLVIPLGYH
     FVLADLSIGV FLWIAISSIA PIGLLMAGYS SNNKYSFLGG LRAAAQSISY EIPLTFCVLA
     ISLLSNSLST VDIVEAQSKY GFFGWNIWRQ PIGFLVFLIS SLAECERLPF DLPEAEEELV
     AGYQTEYSGI KYGLFYLVSY LNLLVSSLFV TVLYLGGWNF SIPYISFFDF FQMNKAVGIL
     EMTMGIFITL TKAYLFLFIS ITIRWTLPRM RMDQLLNLGW KFLLPISLGN LLLTTSFQLV
     SL
//