ID A0A346IQ16_9POAL Unreviewed; 120 AA. AC A0A346IQ16; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 22-FEB-2023, entry version 17. 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:AXP21036.1}; GN ORFNames=Papu_gp059 {ECO:0000313|EMBL:AXP21036.1}; OS Paspalum pubiflorum. OG Plastid; Chloroplast {ECO:0000313|EMBL:AXP21036.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; OC Panicoideae; Andropogonodae; Paspaleae; Paspalinae; Paspalum. OX NCBI_TaxID=1424547 {ECO:0000313|EMBL:AXP21036.1}; RN [1] {ECO:0000313|EMBL:AXP21036.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=30075756; DOI=10.1186/s12870-018-1379-1; RA Burke S.V., Ungerer M.C., Duvall M.R.; RT "Investigation of mitochondrial-derived plastome sequences in the Paspalum RT lineage (Panicoideae; Poaceae)."; RL BMC Plant Biol. 18:152-152(2018). 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; MG523996; AXP21036.1; -; Genomic_DNA. DR AlphaFoldDB; A0A346IQ16; -. 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:AXP21036.1}; 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:AXP21036.1}; 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; 13874 MW; D1028C04178141A7 CRC64; MFLLHEYDIF WTFLIIASLI PILVFWISGL LAPVSKGPEK LSSYESGIEP MGGAWLQFRI RYYMFALVFV VFDVETVFLY PWAMSFDVLG LSVFIEAFIF VLILVVGLVY AWRKGALEWS //