ID A0A290D3U0_9ASPA Unreviewed; 365 AA. AC A0A290D3U0; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 07-OCT-2020, entry version 12. 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:ATB18613.1}; OS Polygonatum stenophyllum. OG Plastid; Chloroplast {ECO:0000313|EMBL:ATB18613.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Asparagaceae; OC Nolinoideae; Polygonatum. OX NCBI_TaxID=261425 {ECO:0000313|EMBL:ATB18613.1}; RN [1] {ECO:0000313|EMBL:ATB18613.1} RP NUCLEOTIDE SEQUENCE. RA Park H., Kim C., Kim J.-H.; RT "The comparative plastid genome analysis and its phylogenetic implication RT on Asparagaceae s.l."; RL Submitted (SEP-2016) 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; KX822773; ATB18613.1; -; 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-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; 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, ECO:0000313|EMBL:ATB18613.1}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01350, KW ECO:0000256|RuleBase:RU000474}; 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:ATB18613.1}; 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, ECO:0000256|RuleBase:RU000471}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_01350, ECO:0000256|RuleBase:RU000474}. FT TRANSMEM 28..52 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350, FT ECO:0000256|RuleBase:RU000474" FT TRANSMEM 97..118 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350, FT ECO:0000256|RuleBase:RU000474" FT TRANSMEM 124..149 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350, FT ECO:0000256|RuleBase:RU000474" FT TRANSMEM 256..281 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350, FT ECO:0000256|RuleBase:RU000474" FT TRANSMEM 301..326 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350, FT ECO:0000256|RuleBase:RU000474" FT TRANSMEM 338..356 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350, FT ECO:0000256|RuleBase:RU000474" SQ SEQUENCE 365 AA; 40418 MW; F0A7B954FE2415EB CRC64; MIIDTTEVEV QAINSFSRLE SLKEVYELIW IFVPIFTLLL GIIIGVLVIV WLEREISAAI QQRIGPEYAG PLGILQALAD GTKLLFKEDL LPSRGDIRLF SVGPSIAVIS VLLSYLVIPF GYRLILADLS IGVFLWISIS SIAPIGLLMS GYGSNNKYSF LGGLRAAAQS ISYEIPLTLC VLSISLLSNS LSTVDIVEAQ SKYGFLGWNL WRQPIGFVVF LISSLAECER LPFDLPEAEE ELVAGYQTEY SGIKYALFYL ASYLNLLVSS LFITVLYLGG WNLSIPYISI PELFGINQMD GVFGTTIGIF ITLAKAYLFL FIPIAARWTL PRMRMDQLLN LGWKFLLPIS LGNLLLTTSS QLVSL //