NU1C_HORVU
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 25-MAY-2022, entry version 83.
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 + (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 -!- 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 PDBsum; 7EU3; -.
DR PDBsum; 7F9O; -.
DR AlphaFoldDB; P92432; -.
DR SMR; P92432; -.
DR EnsemblPlants; HORVU.MOREX.r2.3HG0235230.1; HORVU.MOREX.r2.3HG0235230.1.CDS.1; HORVU.MOREX.r2.3HG0235230.
DR Gramene; HORVU.MOREX.r2.3HG0235230.1; HORVU.MOREX.r2.3HG0235230.1.CDS.1; HORVU.MOREX.r2.3HG0235230.
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 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
