ID A0A288R3C1_9ERIC Unreviewed; 363 AA. AC A0A288R3C1; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 05-DEC-2018, entry version 5. DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic {ECO:0000256|HAMAP-Rule:MF_01350}; DE EC=1.6.5.- {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:APC61903.1}; OS Camellia pubipetala. OG Plastid; Chloroplast {ECO:0000313|EMBL:APC61903.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; Ericales; Theaceae; Camellia. OX NCBI_TaxID=147930 {ECO:0000313|EMBL:APC61903.1}; RN [1] {ECO:0000313|EMBL:APC61903.1} RP NUCLEOTIDE SEQUENCE. RA Tang S., Liufu Y., Wei S., Chen H.; RT "Molecular taxonomy of yellow Camellias in China inferred from small RT single copy region and nrITS sequences."; RL Submitted (FEB-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 + H(+) + NADPH = a plastoquinol + CC NADP(+); Xref=Rhea:RHEA:42612, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17757, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:62192, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562; CC 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}. 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:RU000471}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KU669053; APC61903.1; -; 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:APC61903.1}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01350}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01350, ECO:0000256|RuleBase:RU000471}; KW NADP {ECO:0000256|HAMAP-Rule:MF_01350, ECO:0000256|RuleBase:RU000474}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01350}; KW Plastid {ECO:0000313|EMBL:APC61903.1}; 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 Transmembrane {ECO:0000256|HAMAP-Rule:MF_01350, KW ECO:0000256|RuleBase:RU000471}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01350}. FT TRANSMEM 26 50 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01350}. FT TRANSMEM 97 116 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01350}. FT TRANSMEM 122 147 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01350}. FT TRANSMEM 255 277 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01350}. FT TRANSMEM 297 322 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01350}. FT TRANSMEM 343 361 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01350}. SQ SEQUENCE 363 AA; 40236 MW; 8489A98110A2C279 CRC64; MIINTIEVQA INSFSRLESL KEVYGIIWMF VPILTLVLGI TIGVLVIVWL EREISAGIQQ RIGPEYAGPL GILQALADGT KLLFKENILP SRGDTRLFSI GPSIAVISIL LSYSIIPFGY RLILADLSIG VFLWIAISSI APVGLLMSGY GSNNKYSFLG GLRAAAQSIS YEIPLTLCVL SISLLSNSSS TVDIVEAQSK YGFWGWNLWR QPIGFIVFLI SSLAECERLP FDLPEAEEEL VAGYQTEYSG IKFGLFYVAS YLNLLVSSLF VTVLYLGGWN ISIPYIFVPE LFEINKAGRV FGTIIGIFIT LAKTYLFLFI SITTRWTLPR LRMDQLLNLG WKFLLPISLG NLLLTTSSQL LSL //