ID A0A6B9CPM2_9MAGN Unreviewed; 176 AA. AC A0A6B9CPM2; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 13-SEP-2023, entry version 14. DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 6, chloroplastic {ECO:0000256|RuleBase:RU004431}; DE EC=7.1.1.- {ECO:0000256|RuleBase:RU004431}; GN Name=ndhG {ECO:0000313|EMBL:QGW53468.1}; OS Distylium macrophyllum. OG Plastid; Chloroplast {ECO:0000313|EMBL:QGW53468.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC Saxifragales; Hamamelidaceae; Distylium. OX NCBI_TaxID=2684111 {ECO:0000313|EMBL:QGW53468.1}; RN [1] {ECO:0000313|EMBL:QGW53468.1} RP NUCLEOTIDE SEQUENCE. RA Chen S., Li Y., Fang Y., Ding H.; RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:QTF75163.1} RP NUCLEOTIDE SEQUENCE. RA Dong W.; RT "Plastid phylogenomic insights into the evolution of Distylium RT (Hamamelidaceae)."; RL Submitted (NOV-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|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|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|RuleBase:RU004431}; CC -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which CC are encoded in the nucleus. {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; MN729500; QGW53468.1; -; Genomic_DNA. DR EMBL; MW248111; QTF75163.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6B9CPM2; -. 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:QGW53468.1}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004431}; KW NAD {ECO:0000256|RuleBase:RU004431}; NADP {ECO:0000256|RuleBase:RU004431}; KW Plastid {ECO:0000256|RuleBase:RU004431, ECO:0000313|EMBL:QGW53468.1}; KW Plastoquinone {ECO:0000256|RuleBase:RU004431}; KW Quinone {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 7..27 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004431" FT TRANSMEM 33..51 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004431" FT TRANSMEM 63..81 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; 19036 MW; 15FE8C9AE55761E2 CRC64; MDLPGPIHDF LLVFLGSGLI LGGLGVVLLT NPIYSAFSLG LVLVCISLFY ISSNSHFVAA AQLLIYVGAI NVLIIFAVMF MNGSGYSKDF DLWTVGDGVT SMVCTSIFVS LITTIPDTSW YGIIWTTRSN QIIEQDLISN SQQIGIHLST DFFLPFELIS IILLVALIGA IAVARQ //