ID P73227_SYNY3 Unreviewed; 495 AA. AC P73227; DT 01-FEB-1997, integrated into UniProtKB/TrEMBL. DT 01-FEB-1997, sequence version 1. DT 10-JUN-2026, entry version 131. DE SubName: Full=NADH dehydrogenase subunit 5 {ECO:0000313|EMBL:BAA17254.1}; GN Name=ndhF {ECO:0000313|EMBL:BAA17254.1}; OS Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa). OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Merismopediaceae; Synechocystis. OX NCBI_TaxID=1111708 {ECO:0000313|EMBL:BAA17254.1, ECO:0000313|Proteomes:UP000001425}; RN [1] {ECO:0000313|EMBL:BAA17254.1, ECO:0000313|Proteomes:UP000001425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27184 / PCC 6803 / Kazusa RC {ECO:0000313|Proteomes:UP000001425}; RX PubMed=8590279; DOI=10.1093/dnares/2.4.153; RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., RA Sugiura M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region RT from map positions 64% to 92% of the genome."; RL DNA Res. 2:153-166(1995). RN [2] {ECO:0000313|EMBL:BAA17254.1, ECO:0000313|Proteomes:UP000001425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27184 / PCC 6803 / Kazusa RC {ECO:0000313|Proteomes:UP000001425}; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). CC -!- FUNCTION: NDH-1 shuttles electrons from NAD(P)H, 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 believed CC to be plastoquinone. Couples the redox reaction to proton translocation CC (for every two electrons transferred, four hydrogen ions are CC translocated across the cytoplasmic membrane), and thus conserves the CC redox energy in a proton gradient. {ECO:0000256|ARBA:ARBA00025624}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane CC {ECO:0000256|RuleBase:RU000320}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU000320}. CC -!- SIMILARITY: Belongs to the CPA3 antiporters (TC 2.A.63) subunit D CC family. {ECO:0000256|ARBA:ARBA00005346}. 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; BA000022; BAA17254.1; -; Genomic_DNA. DR PIR; S75340; S75340. DR AlphaFoldDB; P73227; -. DR STRING; 1148.gene:10498117; -. DR PaxDb; 1148-gene:10498117; -. DR EnsemblBacteria; BAA17254; BAA17254; BAA17254. DR KEGG; syn:slr2009; -. DR eggNOG; COG0651; Bacteria. DR InParanoid; P73227; -. DR PhylomeDB; P73227; -. DR Proteomes; UP000001425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR050586; CPA3_Na-H_Antiporter_D. DR InterPro; IPR001750; ND/Mrp_TM. DR NCBIfam; NF005140; PRK06589.1; 1. DR NCBIfam; NF005564; PRK07234.1-4; 1. DR PANTHER; PTHR42703:SF1; NA(+)_H(+) ANTIPORTER SUBUNIT D1; 1. DR PANTHER; PTHR42703; NADH DEHYDROGENASE; 1. DR Pfam; PF00361; Proton_antipo_M; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000001425}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU000320}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 12..33 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 40..59 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 79..99 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 106..122 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 128..148 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 160..181 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 193..217 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 229..249 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 255..273 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 294..320 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 340..360 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 380..402 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 414..434 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 446..465 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 477..494 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 124..378 FT /note="NADH:quinone oxidoreductase/Mrp antiporter FT transmembrane" FT /evidence="ECO:0000259|Pfam:PF00361" SQ SEQUENCE 495 AA; 53675 MW; A04D7D56ABDF4D21 CRC64; MNFPTAIAPN NLLIAIVALL VLALMGAFGG YLFRPLVRPS ALLMTLGTIL LAAVGFALPN AQQWQLMDRF GILLQLDNLG SYFLLTNGLV TLAVLLYCWA SPRTTFFYVQ LMVLHVSLNA AFLSTDLISL YVCLEVVGLS SFLLIIYPRQ AASSWIGLRY LFVTNTALLF YLIGVMLVYQ ATNSLDFQGL ATAPYEAIAL IFLGLLIKGE IFLSGLWSPQ TSSIASAPVA ALLSGIVVKA GILPLLRFAS LSERLAMMVW GLAIATALLG MGLGMFARDS RRILAYSTIS QMGFILVAPA VGGLYALTHG LAKACLFLLV GSLPERDLDK LQAQPISYKL WLPMVLASSS IIGLPILAGF EAKTLTLETL SLNELPWTGI LMNLAGVGTA IILAKFIFLI PSFDKNVDLD KSPWGLFLAV LLLLGALTLG NVIYPEAFSM ENGIKATASF LLGSAIYWWG LRKIPWQPPD WGERLDHLIG TMAIMLMLLF SSVLI //