ID A0A6B9P8R8_9LILI Unreviewed; 100 AA. AC A0A6B9P8R8; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 07-OCT-2020, entry version 3. DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 4L, chloroplastic {ECO:0000256|HAMAP-Rule:MF_01456}; DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01456}; DE AltName: Full=NAD(P)H dehydrogenase subunit 4L {ECO:0000256|HAMAP-Rule:MF_01456}; DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 4L {ECO:0000256|HAMAP-Rule:MF_01456}; GN Name=ndhE {ECO:0000256|HAMAP-Rule:MF_01456, GN ECO:0000313|EMBL:QHD45457.1}; OS Lilium lankongense. OG Plastid; Chloroplast {ECO:0000313|EMBL:QHD45457.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Liliales; Liliaceae; Lilium. OX NCBI_TaxID=82320 {ECO:0000313|EMBL:QHD45457.1}; RN [1] {ECO:0000313|EMBL:QHD45457.1} RP NUCLEOTIDE SEQUENCE. RA Su D., Li J., Kang L., He X., Yu Y., Zhou S.; RT "The complete chloroplast genome of Lilium Lankongense Franchet RT (Liliaceae)."; RL Mitochondrial DNA Part B Resour 4:1824-1825(2019). 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_01456}. 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_01456}; 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_01456}; 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_01456}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Plastid, CC chloroplast thylakoid membrane {ECO:0000256|HAMAP-Rule:MF_01456}; CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01456}. CC -!- SIMILARITY: Belongs to the complex I subunit 4L family. CC {ECO:0000256|HAMAP-Rule:MF_01456}. 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; MK757466; QHD45457.1; -; 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: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:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule. DR HAMAP; MF_01456; NDH1_NuoK; 1. DR InterPro; IPR001133; NADH_UbQ_OxRdtase_chain4L/K. DR InterPro; IPR039428; NUOK/Mnh_C1-like. DR PANTHER; PTHR11434; PTHR11434; 1. DR Pfam; PF00420; Oxidored_q2; 1. PE 3: Inferred from homology; KW Chloroplast {ECO:0000313|EMBL:QHD45457.1}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01456}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01456}; KW NADP {ECO:0000256|HAMAP-Rule:MF_01456}; KW Plastid {ECO:0000313|EMBL:QHD45457.1}; KW Plastoquinone {ECO:0000256|HAMAP-Rule:MF_01456}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_01456}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01456}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_01456}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_01456}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_01456}; Transport {ECO:0000256|HAMAP-Rule:MF_01456}. FT TRANSMEM 6..22 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01456" FT TRANSMEM 29..48 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01456" FT TRANSMEM 60..83 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01456" SQ SEQUENCE 100 AA; 11099 MW; 8930EB53E99F9923 CRC64; MFEHVLFLSV YLFSIGIYGL ITSRNMVRAL MCLELILNSV NINLVTFSDL FDSRQLKGDI FSIFVIAIAA AEAAIGLAIV SSIHHNKKST RINQANLLNN //