ID A0A1V0IQ92_9ROSA Unreviewed; 510 AA. AC A0A1V0IQ92; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 11-DEC-2019, entry version 12. DE RecName: Full=NADH-quinone oxidoreductase subunit N {ECO:0000256|HAMAP-Rule:MF_00445}; DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_00445}; DE AltName: Full=NADH dehydrogenase I subunit N {ECO:0000256|HAMAP-Rule:MF_00445}; DE AltName: Full=NDH-1 subunit N {ECO:0000256|HAMAP-Rule:MF_00445}; GN Name=ndhB {ECO:0000313|EMBL:ARC98629.1}; GN Synonyms=nuoN {ECO:0000256|HAMAP-Rule:MF_00445}; OS Pyracantha fortuneana. OG Plastid {ECO:0000313|EMBL:ARC98629.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Pyracantha. OX NCBI_TaxID=144562 {ECO:0000313|EMBL:ARC98629.1}; RN [1] {ECO:0000313|EMBL:ARC98629.1} RP NUCLEOTIDE SEQUENCE. RA Zhang S.-D., Jin J.-J., Chen S.-Y., Chase M.W., Soltis D.E., Li H.-T., RA Yang J.-B., Li D.-Z., Yi T.-S.; RT "Diversification of Rosaceae since the Late Cretaceous based on plastid RT phylogenomics."; RL New Phytol. 0:0-0(2017). RN [2] {ECO:0000313|EMBL:QBO27098.1} RP NUCLEOTIDE SEQUENCE. RA Duan N.; RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:QBO27098.1} RP NUCLEOTIDE SEQUENCE. RA Wang Q., Qu Z., Tian X.; RT "Complete chloroplast genome of an endangered oil tree, Deutzianthus RT tonkinensis (Euphorbiaceae)."; RL Mitochondrial DNA Part B Resour 4:299-300(2019). CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur CC (Fe-S) centers, to quinones in the respiratory chain. The immediate CC electron acceptor for the enzyme in this species is believed to be CC ubiquinone. Couples the redox reaction to proton translocation (for CC every two electrons transferred, four hydrogen ions are translocated CC across the cytoplasmic membrane), and thus conserves the redox energy CC in a proton gradient. {ECO:0000256|HAMAP-Rule:MF_00445}. 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, ChEBI:CHEBI:24646, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00445}; CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoA, H, CC J, K, L, M, N constitute the membrane sector of the complex. CC {ECO:0000256|HAMAP-Rule:MF_00445}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00445}; CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00445}. CC -!- SIMILARITY: Belongs to the complex I subunit 2 family. CC {ECO:0000256|HAMAP-Rule:MF_00445}. 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; KY419954; ARC98629.1; -; Genomic_DNA. DR EMBL; MH890570; QBO27098.1; -; Genomic_DNA. DR EMBL; MH890570; QBO27114.1; -; Genomic_DNA. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR HAMAP; MF_00445; NDH1_NuoN_1; 1. DR InterPro; IPR010096; NADH-Q_OxRdtase_suN/2. DR InterPro; IPR001750; ND/Mrp_mem. DR Pfam; PF00361; Proton_antipo_M; 1. DR TIGRFAMs; TIGR01770; NDH_I_N; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00445}; KW Chloroplast {ECO:0000313|EMBL:QBO27098.1}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00445}; KW NAD {ECO:0000256|HAMAP-Rule:MF_00445}; KW Plastid {ECO:0000313|EMBL:ARC98629.1}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_00445}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_00445}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00445}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00445}; KW Transport {ECO:0000256|HAMAP-Rule:MF_00445}; KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_00445}. FT TRANSMEM 22..47 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 59..79 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 99..119 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 126..143 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 223..244 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 296..316 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 323..342 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 348..372 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 393..415 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 427..448 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 480..502 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT DOMAIN 146..442 FT /note="Proton_antipo_M" FT /evidence="ECO:0000259|Pfam:PF00361" SQ SEQUENCE 510 AA; 56554 MW; DC17F942B6DABFE5 CRC64; MIWHVQNENF ILDSTRIFMK AFHLLLFDGS FIFPECILIF GLILLLMIDS TSDQKDIPWL YFISSTSLVM SITALLFRWR EEPTISFSGN FQTNNFNEIF QFLILLCSTL CIPLSVEYIE CTEMAITEFL LFVLTATLGG MFLCGANDLI TIFVAPECFS LCSYLLSGYT KKDVRSNEAT TKYLLMGGAS SSILVHGFSW LYGSSGGEIE LQEIVNGLIN TQMYNSPGIS IALIFITVGI GFKLSPAPSH QWTPDVYEGS PTPVVAFLSV TSKVAASASA TRIFDIPFYF SSNEWHLLLE ILAILSMILG NLIAITQTSM KRMLAYSSIG QIGYVIIGII VGDSNGGYAS MITYMLFYIS MNLGTFACIV SFGLRTGTDN IRDYAGLYTK DPFLALSLAL CLLSLGGLPP LAGFFGKLHL FWCGWQAGLY FLVSIGLLTS VVSIYYYLKI IKLLMTGRNQ EITPHVRNYR RSPLRSNNSI ELSMIVCVIA STIPGISMNP IIEIAQDTLF //