ID A0A6M8ZJI0_TROMA Unreviewed; 120 AA. AC A0A6M8ZJI0; DT 07-OCT-2020, integrated into UniProtKB/TrEMBL. DT 07-OCT-2020, sequence version 1. DT 29-SEP-2021, entry version 5. DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 3, chloroplastic {ECO:0000256|HAMAP-Rule:MF_01394}; DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01394}; DE AltName: Full=NAD(P)H dehydrogenase subunit 3 {ECO:0000256|HAMAP-Rule:MF_01394}; DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 3 {ECO:0000256|HAMAP-Rule:MF_01394}; GN Name=ndhC {ECO:0000256|HAMAP-Rule:MF_01394, GN ECO:0000313|EMBL:QKK51091.1}; OS Tropaeolum majus (Common nasturtium) (Indian cress). OG Plastid; Chloroplast {ECO:0000313|EMBL:QKK51091.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Tropaeolaceae; Tropaeolum. OX NCBI_TaxID=4020 {ECO:0000313|EMBL:QKK51091.1}; RN [1] {ECO:0000313|EMBL:QKK51091.1} RP NUCLEOTIDE SEQUENCE. RA Rigault P., Hohmann N., Wolf E., Koch M.; RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain CC NADH dehydrogenase (Complex I) that is believed to belong to the CC minimal assembly required for catalysis. Complex I functions in the CC transfer of electrons from NADH to the respiratory chain. The immediate CC electron acceptor for the enzyme is believed to be ubiquinone. CC {ECO:0000256|ARBA:ARBA00002539}. 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_01394}. 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_01394, CC ECO:0000256|RuleBase:RU003641}; 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_01394, CC ECO:0000256|RuleBase:RU003641}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + CC NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA- CC COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; CC Evidence={ECO:0000256|ARBA:ARBA00000766}; 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_01394}. CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane CC {ECO:0000256|ARBA:ARBA00004225}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004225}. Plastid, chloroplast thylakoid CC membrane {ECO:0000256|HAMAP-Rule:MF_01394}; Multi-pass membrane protein CC {ECO:0000256|HAMAP-Rule:MF_01394}. CC -!- SIMILARITY: Belongs to the complex I subunit 3 family. CC {ECO:0000256|ARBA:ARBA00008472, ECO:0000256|HAMAP-Rule:MF_01394, CC ECO:0000256|RuleBase:RU003641}. 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; MK637814; QKK51091.1; -; 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:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule. DR Gene3D; 1.20.58.1610; -; 1. DR HAMAP; MF_01394; NDH1_NuoA; 1. DR InterPro; IPR023043; NAD(P)H_OxRDtase_bac/plastid. DR InterPro; IPR000440; NADH_UbQ/plastoQ_OxRdtase_su3. DR InterPro; IPR038430; NDAH_ubi_oxred_su3_sf. DR PANTHER; PTHR11058; PTHR11058; 1. DR Pfam; PF00507; Oxidored_q4; 1. PE 3: Inferred from homology; KW Chloroplast {ECO:0000313|EMBL:QKK51091.1}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01394}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01394}; KW NADP {ECO:0000256|HAMAP-Rule:MF_01394, ECO:0000256|RuleBase:RU003641}; KW Plastid {ECO:0000313|EMBL:QKK51091.1}; KW Plastoquinone {ECO:0000256|HAMAP-Rule:MF_01394, KW ECO:0000256|RuleBase:RU003641}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_01394, ECO:0000256|RuleBase:RU003641}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01394}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_01394, KW ECO:0000256|RuleBase:RU003641}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_01394}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_01394}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01394}. FT TRANSMEM 12..34 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01394" FT TRANSMEM 62..83 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01394" FT TRANSMEM 89..112 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01394" SQ SEQUENCE 120 AA; 13822 MW; 832C6CEA556A4AD3 CRC64; MFLLYEYDIF WAFLIISSAI PILAFLISGV LAPISKGPEK LSSYESGIEP MGDAWLQFRI RYYMFALVFV VFDVETVFLY PWAMSFDVLG VSVFIEAFIF VLILIFGSVY AWRKGALEWS //