ID A0A5P9A0W0_9FABA Unreviewed; 363 AA. AC A0A5P9A0W0; DT 26-FEB-2020, integrated into UniProtKB/TrEMBL. DT 26-FEB-2020, sequence version 1. DT 07-OCT-2020, 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:QFS94932.1}; OS Arachis stenosperma. OG Plastid; Chloroplast {ECO:0000313|EMBL:QFS94932.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis. OX NCBI_TaxID=217475 {ECO:0000313|EMBL:QFS94932.1}; RN [1] {ECO:0000313|EMBL:QFS94932.1} RP NUCLEOTIDE SEQUENCE. RA Wang J., Li Y., Li C., Yan C., Zhao X., Yuan C., Sun Q., Shi C., Shan S.; RT "Twelve complete chloroplast genomes of wild peanuts: great genetic RT resources and a better understanding of Arachis phylogeny."; RL Submitted (NOV-2018) 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; MK144819; QFS94932.1; -; 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:QFS94932.1}; 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:QFS94932.1}; 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 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 128..147 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350, FT ECO:0000256|RuleBase:RU000474" FT TRANSMEM 255..277 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350, FT ECO:0000256|RuleBase:RU000474" FT TRANSMEM 297..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; 40178 MW; A316FB6D4267F6C2 CRC64; MIIDTTEVQD INSFFRLESL KEVYGILWVF APIFTLVLGI TISVLAIVWL EREISAGIQQ RIGPEYAGPL GVLQALADGT KLLFKESLIP SRGDTRLFSI GPSISVISII ISYSVIPFGY NFVLSDLNIG VFLWISISSI APIGLLMSGY GSNNKYSFLG GLRAAAQSIS YEIPLTLCVL SISLLSNSLS TVDIVDAQSK YGFLGWNLWR QPIGFVVFLI SSLAECERLP FDLPEAEEEL VAGYQTEYSG IKFGLFYVAS YLNLLISSLF VTVLYLGGSN ISIPYLFISE SFEITKAYGV FGTTIDIFIT LAKTYLFLFL SITARWTLPR LRMDQLLNLG WKFLLPISLG NLLLTTSSQL FSL //