NU1C_MAIZE
ID NU1C_MAIZE Reviewed; 362 AA.
AC P25706;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 3.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic;
DE EC=7.1.1.-;
DE AltName: Full=NAD(P)H dehydrogenase subunit 1;
DE Short=NDH subunit 1;
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 1;
GN Name=ndhA; Synonyms=ndh1;
OS Zea mays (Maize).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND RNA EDITING OF POSITIONS 17; 158;
RP 188 AND 357.
RX PubMed=1498612; DOI=10.2307/3869559;
RA Maier R.M., Hoch B., Zeltz P., Koessel H.;
RT "Internal editing of the maize chloroplast ndhA transcript restores codons
RT for conserved amino acids.";
RL Plant Cell 4:609-616(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=7666415; DOI=10.1006/jmbi.1995.0460;
RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.;
RT "Complete sequence of the maize chloroplast genome: gene content, hotspots
RT of divergence and fine tuning of genetic information by transcript
RT editing.";
RL J. Mol. Biol. 251:614-628(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
RX PubMed=2249254; DOI=10.1007/bf00318388;
RA Maier R.M., Doery I., Igloi G., Koessel H.;
RT "The ndhH genes of gramminean plastomes are linked with the junctions
RT between small single copy and inverted repeat regions.";
RL Curr. Genet. 18:245-250(1990).
RN [4]
RP RNA EDITING OF POSITIONS 17; 158 AND 188.
RX PubMed=16436305; DOI=10.1016/j.jplph.2005.11.014;
RA Darie C.C., De Pascalis L., Mutschler B., Haehnel W.;
RT "Studies of the Ndh complex and photosystem II from mesophyll and bundle
RT sheath chloroplasts of the C(4)-type plant Zea mays.";
RL J. Plant Physiol. 163:800-808(2006).
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 (By similarity).
CC {ECO:0000250}.
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 -!- 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 -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which
CC are encoded in the nucleus. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- RNA EDITING: Modified_positions=17 {ECO:0000269|PubMed:1498612,
CC ECO:0000269|PubMed:16436305}, 158 {ECO:0000269|PubMed:1498612,
CC ECO:0000269|PubMed:16436305}, 188 {ECO:0000269|PubMed:1498612,
CC ECO:0000269|PubMed:16436305}, 357 {ECO:0000269|PubMed:1498612};
CC -!- SIMILARITY: Belongs to the complex I subunit 1 family. {ECO:0000305}.
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DR EMBL; X62370; CAA44228.1; -; Genomic_DNA.
DR EMBL; X86563; CAA60353.1; -; Genomic_DNA.
DR EMBL; X56521; CAA39869.1; -; Genomic_DNA.
DR PIR; JQ1671; JQ1671.
DR RefSeq; NP_043092.1; NC_001666.2.
DR AlphaFoldDB; P25706; -.
DR SMR; P25706; -.
DR STRING; 4577.GRMZM5G874448_P01; -.
DR UCD-2DPAGE; P25706; -.
DR PaxDb; P25706; -.
DR PRIDE; P25706; -.
DR GeneID; 845179; -.
DR KEGG; zma:845179; -.
DR MaizeGDB; 69243; -.
DR eggNOG; KOG4770; Eukaryota.
DR OrthoDB; 1214989at2759; -.
DR Proteomes; UP000007305; Chloroplast.
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:0009060; P:aerobic respiration; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW Reference proteome; 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_0000117509"
FT TRANSMEM 26..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..360
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 362 AA; 40511 MW; BB38174AA9DBA176 CRC64;
MIIDRVEVET INSFSKLELF KEIYGLIWIL PIFALLLGIT IEVLVIVWLE REISASIQQR
IGPEYAGPLG LLQAIADGTK LLLKEDILPS RGDIPLFSIG PSIAVISILL SFLVIPLGYR
FVLADLSIGV FLWIAISSIA PIGLLMAGYS SNNKYSFLGG LRAAAQSISY EIPLTFCVLA
ISLLSNSLST VDIVEAQSKY GFFGWNLWRQ PIGFLVFLIS SLAECERLPF DLPEAEEELV
AGYQTEYSGI KYGLFYLVSY LNLLVSSLFV TVLYLGGWNF SIPYISFFGF FQMNKIIGIL
EMVIGIFITL TKAYLFLFIS ITIRWTLPRM RMDQLLNLGW KFLLPISLGN LLLTTSFQLV
SL
