ID A0A6M8AYM7_9ROSI Unreviewed; 120 AA. AC A0A6M8AYM7; DT 07-OCT-2020, integrated into UniProtKB/TrEMBL. DT 07-OCT-2020, sequence version 1. DT 22-FEB-2023, entry version 8. 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:QKD75856.1}; OS Canarium album. OG Plastid; Chloroplast {ECO:0000313|EMBL:QKD75856.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Sapindales; Burseraceae; Canarium. OX NCBI_TaxID=300208 {ECO:0000313|EMBL:QKD75856.1}; RN [1] {ECO:0000313|EMBL:QKD75856.1} RP NUCLEOTIDE SEQUENCE. RA Wang Y., Hao J., Lu B.; RT "The complete chloroplast genome sequence of Canarium album."; RL Mitochondrial DNA Part B Resour 4:3471-3472(2019). 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:ARBA00003257}. 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; MN106250; QKD75856.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6M8AYM7; -. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell. 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; NADH:ubiquinone/plastoquinone oxidoreductase, chain 3; 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; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 3; 1. DR PANTHER; PTHR11058:SF9; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 3; 1. DR Pfam; PF00507; Oxidored_q4; 1. PE 3: Inferred from homology; KW Chloroplast {ECO:0000313|EMBL:QKD75856.1}; 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:QKD75856.1}; 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|ARBA:ARBA00022967, ECO:0000256|HAMAP- KW Rule:MF_01394}; 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; 13952 MW; 0F5CB0A8522BB730 CRC64; MFLLYKYDIF WAFLIISSVI PILAFLISAV LAPISKGPEK LSTYESGIEP MGDAWLQFRI RYYMFALVFV VFDVETVFLY PWAMSFDVLG VYIFIEAFIF MLILIVGSVY AWRKGALEWS //