NU1C_ARATH
ID NU1C_ARATH Reviewed; 360 AA.
AC Q37165;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 133.
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}; OrderedLocusNames=AtCg01100;
OS Arabidopsis thaliana (Mouse-ear cress).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. C24;
RA Schuster W.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10574454; DOI=10.1093/dnares/6.5.283;
RA Sato S., Nakamura Y., Kaneko T., Asamizu E., Tabata S.;
RT "Complete structure of the chloroplast genome of Arabidopsis thaliana.";
RL DNA Res. 6:283-290(1999).
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; X98298; CAA66944.1; -; Genomic_DNA.
DR EMBL; AP000423; BAA84442.1; -; Genomic_DNA.
DR RefSeq; NP_051114.1; NC_000932.1.
DR PDB; 7WFF; EM; 3.59 A; A=1-360.
DR PDB; 7WG5; EM; 3.89 A; A=1-360.
DR PDBsum; 7WFF; -.
DR PDBsum; 7WG5; -.
DR AlphaFoldDB; Q37165; -.
DR SMR; Q37165; -.
DR STRING; 3702.ATCG01100.1; -.
DR TCDB; 3.D.1.8.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; Q37165; -.
DR PRIDE; Q37165; -.
DR ProteomicsDB; 248990; -.
DR EnsemblPlants; ATCG01100.1; ATCG01100.1; ATCG01100.
DR GeneID; 844804; -.
DR Gramene; ATCG01100.1; ATCG01100.1; ATCG01100.
DR KEGG; ath:ArthCp079; -.
DR Araport; ATCG01100; -.
DR TAIR; locus:504954733; ATCG01100.
DR eggNOG; KOG4770; Eukaryota.
DR HOGENOM; CLU_015134_0_1_1; -.
DR InParanoid; Q37165; -.
DR OMA; WSGWASN; -.
DR OrthoDB; 1214989at2759; -.
DR BioCyc; ARA:ATCG01100-MON; -.
DR PRO; PR:Q37165; -.
DR Proteomes; UP000006548; Chloroplast.
DR ExpressionAtlas; Q37165; baseline and differential.
DR Genevisible; Q37165; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
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:0016651; F:oxidoreductase activity, acting on NAD(P)H; NAS:TAIR.
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:0015979; P:photosynthesis; TAS:TAIR.
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; Reference proteome; Thylakoid; Translocase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..360
FT /note="NAD(P)H-quinone oxidoreductase subunit 1,
FT chloroplastic"
FT /id="PRO_0000117506"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT CONFLICT 14
FT /note="F -> I (in Ref. 1; CAA66944)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="C -> S (in Ref. 1; CAA66944)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="I -> S (in Ref. 1; CAA66944)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="G -> A (in Ref. 1; CAA66944)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 40021 MW; 55974E9686AFC29E CRC64;
MIIYATAVQT INSFVKLESL KEVYGLIWIF VPIFSLVLGI ITGVLVIVWL EREISAGIQQ
RIGPEYAGPL GILQALADGT KLLFKENLRP SRGNTPLFSI GPSIAVISIL LSYSVIPFSN
HLVLADLNIG IFLWIAISSI APIGLLMSGY GSNNKYSFLG GLRAAAQSIS YEIPLTLCVL
SISLLSNSLS TVDIVEAQSK YGFWGWNLWR QPIGFIIFLI SSLAECERLP FDLPEAEEEL
IAGYQTEYSG IKFGLFYVAS YLNLLISSLF VTVLYLGGWN ISIPYISILE LFQRDQIFGT
TIGIFITLAK TYLFLFVSIA TRWTLPRLRM DQLLNLGWKF LLPISLGNLL LTTSFQLFSL
