ID A0A346IQ16_9POAL Unreviewed; 120 AA. AC A0A346IQ16; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 13-FEB-2019, entry version 4. 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; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACMAD clade; Panicoideae; 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=.1186/s12870-018-1379-1; RA Burke S.V., Ungerer M.C., Duvall M.R.; RT "Investigation of mitochondrial-derived plastome sequences in the RT Paspalum lineage (Panicoideae; Poaceae)."; RL BMC Plant Biol. 18:152-152(2018). CC -!- FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via CC FMN and iron-sulfur (Fe-S) centers, to quinones in the CC photosynthetic chain and possibly in a chloroplast respiratory CC chain. The immediate electron acceptor for the enzyme in this CC species is believed to be plastoquinone. Couples the redox CC reaction to proton translocation, and thus conserves the redox CC energy in a proton gradient. {ECO:0000256|HAMAP-Rule:MF_01394}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol CC + n H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA- CC COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17757, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:62192; 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 CC + n H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA- CC COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17757, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:62192; Evidence={ECO:0000256|HAMAP-Rule:MF_01394, CC ECO:0000256|RuleBase:RU003641}; CC -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of CC which are encoded in the nucleus. {ECO:0000256|HAMAP- CC Rule:MF_01394}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {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|HAMAP-Rule:MF_01394, 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 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:InterPro. 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:AXP21036.1}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01394}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01394, ECO:0000256|RuleBase:RU003641}; 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, KW 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|HAMAP-Rule:MF_01394}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01394}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01394}. FT TRANSMEM 12 34 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01394}. FT TRANSMEM 62 83 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01394}. FT TRANSMEM 89 112 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01394}. SQ SEQUENCE 120 AA; 13874 MW; D1028C04178141A7 CRC64; MFLLHEYDIF WTFLIIASLI PILVFWISGL LAPVSKGPEK LSSYESGIEP MGGAWLQFRI RYYMFALVFV VFDVETVFLY PWAMSFDVLG LSVFIEAFIF VLILVVGLVY AWRKGALEWS //