ID A0A7T7IDU2_9ASTR Unreviewed; 363 AA. AC A0A7T7IDU2; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 22-FEB-2023, entry version 5. DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic {ECO:0000256|HAMAP-Rule:MF_01350}; DE EC=7.1.1.- {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:QQL03375.1}; OS Ligularia stenocephala. OG Plastid; Chloroplast {ECO:0000313|EMBL:QQL03375.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Senecioneae; OC Tussilagininae; Ligularia. OX NCBI_TaxID=189220 {ECO:0000313|EMBL:QQL03375.1}; RN [1] {ECO:0000313|EMBL:QQL03375.1} RP NUCLEOTIDE SEQUENCE. RA Park M.; RL Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases. 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:0000256|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:0000256|HAMAP-Rule:MF_01350, CC ECO:0000256|RuleBase:RU000474}; 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:0000256|HAMAP-Rule:MF_01350, CC ECO:0000256|RuleBase:RU000474}; CC -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which CC are encoded in the nucleus. {ECO:0000256|HAMAP-Rule:MF_01350, CC ECO:0000256|RuleBase:RU000474}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU000471}; CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU000471}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. 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|ARBA:ARBA00010535, ECO:0000256|HAMAP-Rule:MF_01350, CC 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; MT985379; QQL03375.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7T7IDU2; -. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. 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-UniRule. 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; 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. PE 3: Inferred from homology; KW Chloroplast {ECO:0000256|RuleBase:RU000474, ECO:0000313|EMBL:QQL03375.1}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, 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 Plastid {ECO:0000256|RuleBase:RU000474, ECO:0000313|EMBL:QQL03375.1}; KW Plastoquinone {ECO:0000256|HAMAP-Rule:MF_01350, KW ECO:0000256|RuleBase:RU000474}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_01350, ECO:0000256|RuleBase:RU000474}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01350, ECO:0000256|RuleBase:RU000474}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_01350, KW ECO:0000256|RuleBase:RU000474}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_01350}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_01350}. FT TRANSMEM 26..50 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350, FT ECO:0000256|RuleBase:RU000474" FT TRANSMEM 97..116 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350, FT ECO:0000256|RuleBase:RU000474" FT TRANSMEM 122..147 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350, FT ECO:0000256|RuleBase:RU000474" FT TRANSMEM 255..278 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350, FT ECO:0000256|RuleBase:RU000474" FT TRANSMEM 298..322 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350, FT ECO:0000256|RuleBase:RU000474" FT TRANSMEM 343..361 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350, FT ECO:0000256|RuleBase:RU000474" SQ SEQUENCE 363 AA; 40217 MW; 95B0E5570EE857CF CRC64; MIIDTTEVQA INSFSRLESL KEVYGIIWML IPIFTLVLGI TIGVLVIVWL EREISAGIQQ RIGPEYAGPL GILQALADGT KLLFKENLLP SRGDTRLFSI GPSIAVISIL LSYLVIPFGY HLVLADLSIG VFLWIAISSI APVGLLMSGY GSNNKYSFLG GLRAAAQSIS YEIPLTLCVL SISLLSNSSS TVDIVEAQSK YGFWGWNLWR QPIGFLVFLI SSLAECERLP FDLPEAEEEL VAGYQTEYSG IKFGLFYVAS YLNLLVSSLF VTVLYLGGWN LSIPYIFGPE LFEITKRGRV FGTIIGIFIT LAKTYLFLFI SIATRWTLPR LRMDQLLNLG WKFLLPISLG NLLLTTSSQL LSL //