ID A0A8K1PHC2_9LAMI Unreviewed; 176 AA. AC A0A8K1PHC2; DT 03-AUG-2022, integrated into UniProtKB/TrEMBL. DT 03-AUG-2022, sequence version 1. DT 24-JAN-2024, entry version 9. DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 6, chloroplastic {ECO:0000256|ARBA:ARBA00018131, ECO:0000256|RuleBase:RU004431}; DE EC=7.1.1.- {ECO:0000256|RuleBase:RU004431}; GN Name=ndhG {ECO:0000313|EMBL:UDN44237.1}; OS Buddleja officinalis. OG Plastid; Chloroplast {ECO:0000313|EMBL:UDN44237.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Lamiales; Scrophulariaceae; Buddlejeae; Buddleja. OX NCBI_TaxID=714454 {ECO:0000313|EMBL:UDN44237.1}; RN [1] {ECO:0000313|EMBL:UDN44237.1} RP NUCLEOTIDE SEQUENCE. RA Ding S.J., Wang S.J., Deng R.Y., Ma F.X., Zhang H.Y.; RL Submitted (AUG-2021) 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|ARBA:ARBA00004059, ECO:0000256|RuleBase:RU004431}. 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|ARBA:ARBA00001230, CC ECO:0000256|RuleBase:RU004431}; 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|ARBA:ARBA00001558, CC ECO:0000256|RuleBase:RU004431}; CC -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which CC are encoded in the nucleus. {ECO:0000256|ARBA:ARBA00011199, CC ECO:0000256|RuleBase:RU004431}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Plastid, CC chloroplast thylakoid membrane {ECO:0000256|RuleBase:RU004431}. CC -!- SIMILARITY: Belongs to the complex I subunit 6 family. CC {ECO:0000256|ARBA:ARBA00005698, ECO:0000256|RuleBase:RU004431}. 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; MZ955034; UDN44237.1; -; Genomic_DNA. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-UniRule. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR Gene3D; 1.20.120.1200; NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ; 1. DR InterPro; IPR001457; NADH_UbQ/plastoQ_OxRdtase_su6. DR InterPro; IPR042106; Nuo/plastoQ_OxRdtase_6_NuoJ. DR PANTHER; PTHR33269:SF5; NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT 6, CHLOROPLASTIC; 1. DR PANTHER; PTHR33269; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 6; 1. DR Pfam; PF00499; Oxidored_q3; 1. PE 3: Inferred from homology; KW Chloroplast {ECO:0000256|RuleBase:RU004431, ECO:0000313|EMBL:UDN44237.1}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004431}; KW NAD {ECO:0000256|RuleBase:RU004431}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU004431}; KW Plastid {ECO:0000256|RuleBase:RU004431, ECO:0000313|EMBL:UDN44237.1}; KW Plastoquinone {ECO:0000256|ARBA:ARBA00022957, KW ECO:0000256|RuleBase:RU004431}; KW Quinone {ECO:0000256|ARBA:ARBA00022719, ECO:0000256|RuleBase:RU004431}; KW Thylakoid {ECO:0000256|RuleBase:RU004431}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU004431}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU004431}. FT TRANSMEM 12..29 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004431" FT TRANSMEM 36..53 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004431" FT TRANSMEM 59..80 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004431" FT TRANSMEM 92..112 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004431" FT TRANSMEM 152..174 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004431" SQ SEQUENCE 176 AA; 19347 MW; 3AA2A19991CF651F CRC64; MDLPGPIHDF LLVFLGSGLI LGSLAVVLLP NPIYSAFSLG LVLFCISLFY ILSNSYFVAA AQLLIYVGAI NVLIIFAVMF MNGSEYYKDF HLWTVGDGVT SMVCTSLFIS LITTIPDTSW YGIIWTTKSN QILEQDLISN SQQIGIHLST DFFLPFELIS IILLVALIGA IAIARQ //