ID A0A1V0IQ92_9ROSA Unreviewed; 510 AA. AC A0A1V0IQ92; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 16-JAN-2019, entry version 7. DE RecName: Full=NADH-quinone oxidoreductase subunit N {ECO:0000256|HAMAP-Rule:MF_00445}; DE EC=1.6.5.11 {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; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Rosales; Rosaceae; Amygdaloideae; OC 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 RT plastid phylogenomics."; RL New Phytol. 0:0-0(2017). 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_00445}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a quinone + H(+) + NADH = a quinol + NAD(+); CC Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; CC EC=1.6.5.11; Evidence={ECO:0000256|HAMAP-Rule:MF_00445}; 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_00445}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_00445}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC 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 GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009536; C:plastid; 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: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 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 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 59 79 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 99 119 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 126 143 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 223 244 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 296 316 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 323 342 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 348 372 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 393 415 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 427 448 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 480 502 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT DOMAIN 146 442 Proton_antipo_M. {ECO:0000259|Pfam: FT 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 //