ID A0A4D6Q2N8_9ERIC Unreviewed; 120 AA. AC A0A4D6Q2N8; DT 03-JUL-2019, integrated into UniProtKB/TrEMBL. DT 03-JUL-2019, sequence version 1. DT 18-SEP-2019, entry version 3. DE RecName: Full=NADH-quinone oxidoreductase subunit A {ECO:0000256|HAMAP-Rule:MF_01394}; DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01394}; DE AltName: Full=NADH dehydrogenase I subunit A {ECO:0000256|HAMAP-Rule:MF_01394}; DE AltName: Full=NDH-1 subunit A {ECO:0000256|HAMAP-Rule:MF_01394}; DE AltName: Full=NUO1 {ECO:0000256|HAMAP-Rule:MF_01394}; GN Name=ndhC {ECO:0000313|EMBL:QCF39501.1}; GN Synonyms=nuoA {ECO:0000256|HAMAP-Rule:MF_01394}; OS Vaccinium oldhamii. OG Plastid {ECO:0000313|EMBL:QCF39501.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; Ericales; Ericaceae; Vaccinioideae; OC Vaccinieae; Vaccinium. OX NCBI_TaxID=190543 {ECO:0000313|EMBL:QCF39501.1}; RN [1] {ECO:0000313|EMBL:QCF39501.1} RP NUCLEOTIDE SEQUENCE. RA Kim S.-C., Baek S.-H., Lee J.-W., Hyun H.J.; RT "Complete chloroplast genome of Vaccinium oldhamii and phylogenetic RT analysis."; RL Mitochondrial DNA Part B Resour 4:902-903(2019). CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron- CC sulfur (Fe-S) centers, to quinones in the respiratory chain. The CC immediate electron acceptor for the enzyme in this species is CC believed to be ubiquinone. Couples the redox reaction to proton CC translocation (for every two electrons transferred, four hydrogen CC ions are translocated across the cytoplasmic membrane), and thus CC conserves the redox energy in a proton gradient. CC {ECO:0000256|HAMAP-Rule:MF_01394}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + CC NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:132124; Evidence={ECO:0000256|HAMAP-Rule:MF_01394}; CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits CC NuoA, H, J, K, L, M, N constitute the membrane sector of the CC complex. {ECO:0000256|HAMAP-Rule:MF_01394}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_01394}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01394}. CC -!- SIMILARITY: Belongs to the complex I subunit 3 family. CC {ECO:0000256|HAMAP-Rule:MF_01394}. 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; MK049537; QCF39501.1; -; Genomic_DNA. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule. DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. 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 Cell membrane {ECO:0000256|HAMAP-Rule:MF_01394}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01394}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01394}; KW Plastid {ECO:0000313|EMBL:QCF39501.1}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_01394}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_01394}; 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}; KW Ubiquinone {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; 13858 MW; 67E01A5BDF93DAF8 CRC64; MFLLYEYDIF WTFLLISSLI PVLAFLISGV LAPLSKGPEK LSIYESGIEP VGDAWLQFQI RYYMFALVFV VFDVETVFLY PWAMSFDVLG VSVFIEAFIF VLILIVGSVY AWRKGALEWF //